Consequences of Rab GTPase dysfunction in genetic or acquired human diseases

References

• Hutagalung AH, Novick PJ. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev. 2011;91(1):119–49. https://doi.org/10.1152/physrev.00059.2009
   PubMed Web of Science ®Google Scholar
• Li G, Marlin MC. Rab family of GTPases. Methods Mol Biol. 2015;1298:1–15. https://doi.org/10.1007/978-1-4939-2569-8_1
   PubMedGoogle Scholar
• Pfeffer SR. Rab GTPase localization and Rab cascades in Golgi transport. Biochem Soc Trans. 2012;40(6):1373–7. https://doi.org/10.1042/BST20120168
   PubMedGoogle Scholar
• Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol. 2009;10(8):513–25. https://doi.org/10.1038/nrm2728
   PubMed Web of Science ®Google Scholar
• Wandinger-Ness A, Zerial M. Rab proteins and the compartmentalization of the endosomal system. Cold Spring Harb Perspect Biol. 2014;6(11):a022616. https://doi.org/10.1101/cshperspect.a022616
   PubMed Web of Science ®Google Scholar
• Klopper TH, Kienle N, Fasshauer D, et al. Untangling the evolution of Rab G proteins: implications of a comprehensive genomic analysis. BMC Biol. 2012;10:71. https://doi.org/10.1186/1741-7007-10-71
   PubMed Web of Science ®Google Scholar
• Carroll KS, Hanna J, Simon I, et al. Role of Rab9 GTPase in facilitating receptor recruitment by TIP47. Science. 2001;292(5520):1373–6. https://doi.org/10.1126/science.1056791
   PubMed Web of Science ®Google Scholar
• McLauchlan H, Newell J, Morrice N, et al. A novel role for Rab5-GDI in ligand sequestration into clathrin-coated pits. Curr Biol. 1998;8(1):34–45. https://doi.org/10.1016/S0960-9822(98)70018-1
   PubMed Web of Science ®Google Scholar
• Miserey-Lenkei S, Chalancon G, Bardin S, et al. Rab and actomyosin-dependent fission of transport vesicles at the Golgi complex. Nat Cell Biol. 2010;12(7):645–54. https://doi.org/10.1038/ncb2067
   PubMed Web of Science ®Google Scholar
• Pellinen T, Arjonen A, Vuoriluoto K, et al. Small GTPase Rab21 regulates cell adhesion and controls endosomal traffic of beta1-integrins. J Cell Biol. 2006;173(5):767–80. https://doi.org/10.1083/jcb.200509019
   PubMed Web of Science ®Google Scholar
• Casavola EC, Catucci A, Bielli P, et al. Ypt32p and Mlc1p bind within the vesicle binding region of the class V myosin Myo2p globular tail domain. Mol Microbiol. 2008;67(5):1051–66. https://doi.org/10.1111/j.1365-2958.2008.06106.x
   PubMed Web of Science ®Google Scholar
• Echard A, Jollivet F, Martinez O, et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science. 1998;279(5350):580–5. https://doi.org/10.1126/science.279.5350.580
   PubMed Web of Science ®Google Scholar
• Fukuda M, Kuroda TS, Mikoshiba K. Slac2-a/melanophilin, the missing link between Rab27 and myosin Va: implications of a tripartite protein complex for melanosome transport. J Biol Chem. 2002;277(14):12432–6. https://doi.org/10.1074/jbc.C200005200
   PubMed Web of Science ®Google Scholar
• Govindan B, Bowser R, Novick P. The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol. 1995;128(6):1055–68. https://doi.org/10.1083/jcb.128.6.1055
   PubMed Web of Science ®Google Scholar
• Guo X, Farias GG, Mattera R, et al. Rab5 and its effector FHF contribute to neuronal polarity through dynein-dependent retrieval of somatodendritic proteins from the axon. Proc Natl Acad Sci U S A. 2016;113(36):E5318–27. https://doi.org/10.1073/pnas.1601844113
   PubMed Web of Science ®Google Scholar
• Hoepfner S, Severin F, Cabezas A, et al. Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B. Cell. 2005;121(3):437–50. https://doi.org/10.1016/j.cell.2005.02.017
   PubMed Web of Science ®Google Scholar
• Johansson M, Rocha N, Zwart W, et al. Activation of endosomal dynein motors by stepwise assembly of Rab7-RILP-p150Glued, ORP1L, and the receptor betalll spectrin. J Cell Biol. 2007;176(4):459–71. https://doi.org/10.1083/jcb.200606077
   PubMed Web of Science ®Google Scholar
• Jordens I, Fernandez-Borja M, Marsman M, et al. The Rab7 effector protein RILP controls lysosomal transport by inducing the recruitment of dynein-dynactin motors. Curr Biol. 2001;11(21):1680–5. https://doi.org/10.1016/S0960-9822(01)00531-0
   PubMed Web of Science ®Google Scholar
• Roland JT, Kenworthy AK, Peranen J, et al. Myosin Vb interacts with Rab8a on a tubular network containing EHD1 and EHD3. Mol Biol Cell. 2007;18(8):2828–37. https://doi.org/10.1091/mbc.E07-02-0169
   PubMed Web of Science ®Google Scholar
• Schlager MA, Kapitein LC, Grigoriev I, et al. Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis. EMBO J. 2010;29(10):1637–51. https://doi.org/10.1038/emboj.2010.51
   PubMed Web of Science ®Google Scholar
• Wu XS, Rao K, Zhang H, et al. Identification of an organelle receptor for myosin-Va. Nat Cell Biol. 2002;4(4):271–8. https://doi.org/10.1038/ncb760
   PubMed Web of Science ®Google Scholar
• Hickey CM, Wickner W. HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell. 2010;21(13):2297–305. https://doi.org/10.1091/mbc.E10-01-0044
   PubMed Web of Science ®Google Scholar
• Nielsen E, Christoforidis S, Uttenweiler-Joseph S, et al. Rabenosyn-5, a novel Rab5 effector, is complexed with hVPS45 and recruited to endosomes through a FYVE finger domain. J Cell Biol. 2000;151(3):601–12. https://doi.org/10.1083/jcb.151.3.601
   PubMed Web of Science ®Google Scholar
• Ohya T, Miaczynska M, Coskun U, et al. Reconstitution of Rab- and SNARE-dependent membrane fusion by synthetic endosomes. Nature. 2009;459(7250):1091–7. https://doi.org/10.1038/nature08107
   PubMed Web of Science ®Google Scholar
• Price A, Seals D, Wickner W, et al. The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J Cell Biol. 2000;148(6):1231–8. https://doi.org/10.1083/jcb.148.6.1231
   PubMed Web of Science ®Google Scholar
• Simonsen A, Lippe R, Christoforidis S, et al. EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature. 1998;394(6692):494–8. https://doi.org/10.1038/28879
   PubMed Web of Science ®Google Scholar
• TerBush DR, Maurice T, Roth D, et al. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 1996;15(23):6483–94.
   PubMed Web of Science ®Google Scholar
• Ali BR, Wasmeier C, Lamoreux L, et al. Multiple regions contribute to membrane targeting of Rab GTPases. J Cell Sci. 2004;117(Pt 26):6401–12. https://doi.org/10.1242/jcs.01542
   PubMed Web of Science ®Google Scholar
• Blumer J, Rey J, Dehmelt L, et al. RabGEFs are a major determinant for specific Rab membrane targeting. J Cell Biol. 2013;200(3):287–300. https://doi.org/10.1083/jcb.201209113
   PubMed Web of Science ®Google Scholar
• Chavrier P, Parton RG, Hauri HP, et al. Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments. Cell. 1990;62(2):317–29. https://doi.org/10.1016/0092-8674(90)90369-P
   PubMed Web of Science ®Google Scholar
• Pfeffer S, Aivazian D. Targeting Rab GTPases to distinct membrane compartments. Nat Rev Mol Cell Biol. 2004;5(11):886–96. https://doi.org/10.1038/nrm1500
   PubMed Web of Science ®Google Scholar
• Leung KF, Baron R, Seabra MC. Thematic review series: lipid posttranslational modifications. geranylgeranylation of Rab GTPases. J Lipid Res. 2006;47(3):467–75. https://doi.org/10.1194/jlr.R500017-JLR200
   PubMed Web of Science ®Google Scholar
• Christoforidis S, McBride HM, Burgoyne RD, et al. The Rab5 effector EEA1 is a core component of endosome docking. Nature. 1999;397(6720):621–5. https://doi.org/10.1038/17618
   PubMed Web of Science ®Google Scholar
• Barr F, Lambright DG. Rab GEFs and GAPs. Curr Opin Cell Biol. 2010;22(4):461–70. https://doi.org/10.1016/j.ceb.2010.04.007
   PubMed Web of Science ®Google Scholar
• Novick P. Regulation of membrane traffic by Rab GEF and GAP cascades. Small GTPases. 2016;7(4):252–6. https://doi.org/10.1080/21541248.2016.1213781
   PubMedGoogle Scholar
• Soldati T, Riederer MA, Pfeffer SR. Rab GDI: a solubilizing and recycling factor for rab9 protein. Mol Biol Cell. 1993;4(4):425–34. https://doi.org/10.1091/mbc.4.4.425
   PubMed Web of Science ®Google Scholar
• Ullrich O, Stenmark H, Alexandrov K, et al. Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. J Biol Chem. 1993;268(24):18143–50.
   PubMed Web of Science ®Google Scholar
• Li G. Rab GTPases, membrane trafficking and diseases. Curr Drug Targets. 2011;12(8):1188–93. https://doi.org/10.2174/138945011795906561
   PubMed Web of Science ®Google Scholar
• Mitra S, Cheng KW, Mills GB. Rab GTPases implicated in inherited and acquired disorders. Semin Cell Dev Biol. 2011;22(1):57–68. https://doi.org/10.1016/j.semcdb.2010.12.005
   PubMed Web of Science ®Google Scholar
• Seixas E, Barros M, Seabra MC, et al. Rab and Arf proteins in genetic diseases. Traffic. 2013;14(8):871–85. https://doi.org/10.1111/tra.12072
   PubMed Web of Science ®Google Scholar
• Szigeti K, Lupski JR. Charcot-Marie-Tooth disease. Eur J Hum Genet. 2009;17(6):703–10. https://doi.org/10.1038/ejhg.2009.31
   PubMed Web of Science ®Google Scholar
• Ponomareva OY, Eliceiri KW, Halloran MC. Charcot-Marie-Tooth 2b associated Rab7 mutations cause axon growth and guidance defects during vertebrate sensory neuron development. Neural Dev. 2016;11:2. https://doi.org/10.1186/s13064-016-0058-x
   PubMed Web of Science ®Google Scholar
• Wang X, Han C, Liu W, et al. A novel RAB7 mutation in a Chinese family with Charcot-Marie-Tooth type 2B disease. Gene. 2014;534(2):431–4. https://doi.org/10.1016/j.gene.2013.10.023
   PubMed Web of Science ®Google Scholar
• Bucci C, Bakke O, Progida C. Rab7b and receptors trafficking. Commun Integr Biol. 2010;3(5):401–4. https://doi.org/10.4161/cib.3.5.12341
   PubMedGoogle Scholar
• Progida C, Cogli L, Piro F, et al. Rab7b controls trafficking from endosomes to the TGN. J Cell Sci. 2010;123(Pt 9):1480–91. https://doi.org/10.1242/jcs.051474
   PubMed Web of Science ®Google Scholar
• Yang M, Chen T, Han C, et al. Rab7b, a novel lysosome-associated small GTPase, is involved in monocytic differentiation of human acute promyelocytic leukemia cells. Biochem Biophys Res Commun. 2004;318(3):792–9. https://doi.org/10.1016/j.bbrc.2004.04.115
   PubMed Web of Science ®Google Scholar
• Feng Y, Press B, Wandinger-Ness A. Rab 7: an important regulator of late endocytic membrane traffic. J Cell Biol. 1995;131(6 Pt 1):1435–52. https://doi.org/10.1083/jcb.131.6.1435
   PubMed Web of Science ®Google Scholar
• Guerra F, Bucci C. Multiple Roles of the Small GTPase Rab7. Cells. 2016;5(3):https://doi.org/10.3390/cells5030034
   PubMed Web of Science ®Google Scholar
• Rink J, Ghigo E, Kalaidzidis Y, et al. Rab conversion as a mechanism of progression from early to late endosomes. Cell. 2005;122(5):735–49. https://doi.org/10.1016/j.cell.2005.06.043
   PubMed Web of Science ®Google Scholar
• Bucci C, De Luca M. Molecular basis of Charcot-Marie-Tooth type 2B disease. Biochem Soc Trans. 2012;40(6):1368–72. https://doi.org/10.1042/BST20120197
   PubMedGoogle Scholar
• Cogli L, Progida C, Lecci R, et al. CMT2B-associated Rab7 mutants inhibit neurite outgrowth. Acta Neuropathol. 2010;120(4):491–501. https://doi.org/10.1007/s00401-010-0696-8
   PubMed Web of Science ®Google Scholar
• De Luca A, Progida C, Spinosa MR, et al. Characterization of the Rab7K157N mutant protein associated with Charcot-Marie-Tooth type 2B. Biochem Biophys Res Commun. 2008;372(2):283–7. https://doi.org/10.1016/j.bbrc.2008.05.060
   PubMed Web of Science ®Google Scholar
• Spinosa MR, Progida C, De Luca A, et al. Functional characterization of Rab7 mutant proteins associated with Charcot-Marie-Tooth type 2B disease. J Neurosci. 2008;28(7):1640–8. https://doi.org/10.1523/JNEUROSCI.3677-07.2008
   PubMed Web of Science ®Google Scholar
• Zhang K, Fishel Ben Kenan R, Osakada Y, et al. Defective axonal transport of Rab7 GTPase results in dysregulated trophic signaling. J Neurosci. 2013;33(17):7451–62. https://doi.org/10.1523/JNEUROSCI.4322-12.2013
   PubMed Web of Science ®Google Scholar
• Hong L, Simons P, Waller A, et al. A small molecule pan-inhibitor of Ras-superfamily GTPases with high efficacy towards Rab7. Bethesda (MD): Probe Reports from the NIH Molecular Libraries Program; 2010.
   Google Scholar
• Cherry S, Jin EJ, Ozel MN, et al. Charcot-Marie-Tooth 2B mutations in rab7 cause dosage-dependent neurodegeneration due to partial loss of function. Elife. 2013;2:e01064. https://doi.org/10.7554/eLife.01064
   PubMed Web of Science ®Google Scholar
• Bem D, Yoshimura S, Nunes-Bastos R, et al. Loss-of-function mutations in RAB18 cause Warburg micro syndrome. Am J Hum Genet. 2011;88(4):499–507. https://doi.org/10.1016/j.ajhg.2011.03.012
   PubMed Web of Science ®Google Scholar
• Gerondopoulos A, Bastos RN, Yoshimura S, et al. Rab18 and a Rab18 GEF complex are required for normal ER structure. J Cell Biol. 2014;205(5):707–20. https://doi.org/10.1083/jcb.201403026
   PubMed Web of Science ®Google Scholar
• Handley MT, Morris-Rosendahl DJ, Brown S, et al. Mutation spectrum in RAB3GAP1, RAB3GAP2, and RAB18 and genotype-phenotype correlations in warburg micro syndrome and Martsolf syndrome. Hum Mutat. 2013;34(5):686–96. https://doi.org/10.1002/humu.22296
   PubMed Web of Science ®Google Scholar
• Fukui K, Sasaki T, Imazumi K, et al. Isolation and characterization of a GTPase activating protein specific for the Rab3 subfamily of small G proteins. J Biol Chem. 1997;272(8):4655–8. https://doi.org/10.1074/jbc.272.8.4655
   PubMed Web of Science ®Google Scholar
• Jenkins D, Seelow D, Jehee FS, et al. RAB23 mutations in Carpenter syndrome imply an unexpected role for hedgehog signaling in cranial-suture development and obesity. Am J Hum Genet. 2007;80(6):1162–70. https://doi.org/10.1086/518047
   PubMed Web of Science ®Google Scholar
• Olkkonen VM, Peterson JR, Dupree P, et al. Isolation of a mouse cDNA encoding Rab23, a small novel GTPase expressed predominantly in the brain. Gene. 1994;138(1-2):207–11. https://doi.org/10.1016/0378-1119(94)90809-5
   PubMed Web of Science ®Google Scholar
• Evans TM, Ferguson C, Wainwright BJ, et al. Rab23, a negative regulator of hedgehog signaling, localizes to the plasma membrane and the endocytic pathway. Traffic. 2003;4(12):869–84. https://doi.org/10.1046/j.1600-0854.2003.00141.x
   PubMed Web of Science ®Google Scholar
• Eggenschwiler JT, Espinoza E, Anderson KV. Rab23 is an essential negative regulator of the mouse Sonic hedgehog signalling pathway. Nature. 2001;412(6843):194–8. https://doi.org/10.1038/35084089
   PubMed Web of Science ®Google Scholar
• Boehlke C, Bashkurov M, Buescher A, et al. Differential role of Rab proteins in ciliary trafficking: Rab23 regulates smoothened levels. J Cell Sci. 2010;123(Pt 9):1460–7. https://doi.org/10.1242/jcs.058883
   PubMed Web of Science ®Google Scholar
• Griscelli C, Prunieras M. Pigment dilution and immunodeficiency: a new syndrome. Int J Dermatol. 1978;17(10):788–91. https://doi.org/10.1111/j.1365-4362.1978.tb05980.x
   PubMed Web of Science ®Google Scholar
• Menasche G, Pastural E, Feldmann J, et al. Mutations in RAB27A cause Griscelli syndrome associated with haemophagocytic syndrome. Nat Genet. 2000;25(2):173–6. https://doi.org/10.1038/76024
   PubMed Web of Science ®Google Scholar
• Stinchcombe JC, Barral DC, Mules EH, et al. Rab27a is required for regulated secretion in cytotoxic T lymphocytes. J Cell Biol. 2001;152(4):825–34. https://doi.org/10.1083/jcb.152.4.825
   PubMed Web of Science ®Google Scholar
• Bahadoran P, Aberdam E, Mantoux F, et al. Rab27a: A key to melanosome transport in human melanocytes. J Cell Biol. 2001;152(4):843–50. https://doi.org/10.1083/jcb.152.4.843
   PubMed Web of Science ®Google Scholar
• Hume AN, Collinson LM, Rapak A, et al. Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J Cell Biol. 2001;152(4):795–808. https://doi.org/10.1083/jcb.152.4.795
   PubMed Web of Science ®Google Scholar
• Van Gele M, Dynoodt P, Lambert J. Griscelli syndrome: a model system to study vesicular trafficking. Pigment Cell Melanoma Res. 2009;22(3):268–82. https://doi.org/10.1111/j.1755-148X.2009.00558.x
   PubMed Web of Science ®Google Scholar
• Wu X, Wang F, Rao K, et al. Rab27a is an essential component of melanosome receptor for myosin Va. Mol Biol Cell. 2002;13(5):1735–49. https://doi.org/10.1091/mbc.01-12-0595
   PubMed Web of Science ®Google Scholar
• Barral DC, Ramalho JS, Anders R, et al. Functional redundancy of Rab27 proteins and the pathogenesis of Griscelli syndrome. J Clin Invest. 2002;110(2):247–57. https://doi.org/10.1172/JCI0215058
   PubMed Web of Science ®Google Scholar
• Wu X, Bowers B, Rao K, et al. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function In vivo. J Cell Biol. 1998;143(7):1899–918. https://doi.org/10.1083/jcb.143.7.1899
   PubMed Web of Science ®Google Scholar
• Lipsker D. Haemophagocytic lymphohistiocytosis and silvery hair in Griscelli syndrome. Br J Haematol. 2016;175(1):11. https://doi.org/10.1111/bjh.14252
   PubMed Web of Science ®Google Scholar
• Wilson SM, Yip R, Swing DA, et al. A mutation in Rab27a causes the vesicle transport defects observed in ashen mice. Proc Natl Acad Sci U S A. 2000;97(14):7933–8. https://doi.org/10.1073/pnas.140212797
   PubMed Web of Science ®Google Scholar
• Westbroek W, Lambert J, De Schepper S, et al. Rab27b is up-regulated in human Griscelli syndrome type II melanocytes and linked to the actin cytoskeleton via exon F-Myosin Va transcripts. Pigment Cell Res. 2004;17(5):498–505. https://doi.org/10.1111/j.1600-0749.2004.00173.x
   PubMedGoogle Scholar
• Boda B, Mas C, Muller D. Activity-dependent regulation of genes implicated in X-linked non-specific mental retardation. Neuroscience. 2002;114(1):13–7. https://doi.org/10.1016/S0306-4522(02)00218-X
   PubMed Web of Science ®Google Scholar
• Giannandrea M, Bianchi V, Mignogna ML, et al. Mutations in the small GTPase gene RAB39B are responsible for X-linked mental retardation associated with autism, epilepsy, and macrocephaly. Am J Hum Genet. 2010;86(2):185–95. https://doi.org/10.1016/j.ajhg.2010.01.011
   PubMed Web of Science ®Google Scholar
• Bienvenu T, des Portes V, Saint Martin A, et al. Non-specific X-linked semidominant mental retardation by mutations in a Rab GDP-dissociation inhibitor. Hum Mol Genet. 1998;7(8):1311–5. https://doi.org/10.1093/hmg/7.8.1311
   PubMed Web of Science ®Google Scholar
• D'Adamo P, Menegon A, Lo Nigro C, et al. Mutations in GDI1 are responsible for X-linked non-specific mental retardation. Nat Genet. 1998;19(2):134–9. https://doi.org/10.1038/487
   PubMed Web of Science ®Google Scholar
• Sasaki T, Kikuchi A, Araki S, et al. Purification and characterization from bovine brain cytosol of a protein that inhibits the dissociation of GDP from and the subsequent binding of GTP to smg p25A, a ras p21-like GTP-binding protein. J Biol Chem. 1990;265(4):2333–7.
   PubMed Web of Science ®Google Scholar
• van den Hurk JA, Schwartz M, van Bokhoven H, et al. Molecular basis of choroideremia (CHM): mutations involving the Rab escort protein-1 (REP-1) gene. Hum Mutat. 1997;9(2):110–7. https://doi.org/10.1002/(SICI)1098-1004(1997)9:2%3c110::AID-HUMU2%3e3.0.CO;2-D
   PubMed Web of Science ®Google Scholar
• Lee TK, McTaggart KE, Sieving PA, et al. Clinical diagnoses that overlap with choroideremia. Can J Ophthalmol. 2003;38(5):364–72. quiz 72. https://doi.org/10.1016/S0008-4182(03)80047-9
   PubMed Web of Science ®Google Scholar
• Pereira-Leal JB, Hume AN, Seabra MC. Prenylation of Rab GTPases: molecular mechanisms and involvement in genetic disease. FEBS Lett. 2001;498(2-3):197–200. https://doi.org/10.1016/S0014-5793(01)02483-8
   PubMed Web of Science ®Google Scholar
• Seabra MC, Ho YK, Anant JS. Deficient geranylgeranylation of Ram/Rab27 in choroideremia. J Biol Chem. 1995;270(41):24420–7. https://doi.org/10.1074/jbc.270.41.24420
   PubMed Web of Science ®Google Scholar
• Chen D, Guo J, Miki T, et al. Molecular cloning and characterization of rab27a and rab27b, novel human rab proteins shared by melanocytes and platelets. Biochem Mol Med. 1997;60(1):27–37. https://doi.org/10.1006/bmme.1996.2559
   PubMedGoogle Scholar
• Moosajee M, Tracey-White D, Smart M, et al. Functional rescue of REP1 following treatment with PTC124 and novel derivative PTC-414 in human choroideremia fibroblasts and the nonsense-mediated zebrafish model. Hum Mol Genet. 2016;https://doi.org/10.1093/hmg/ddw184
   PubMed Web of Science ®Google Scholar
• Anand V, Barral DC, Zeng Y, et al. Gene therapy for choroideremia: in vitro rescue mediated by recombinant adenovirus. Vision Res. 2003;43(8):919–26. https://doi.org/10.1016/S0042-6989(02)00389-9
   PubMed Web of Science ®Google Scholar
• MacLaren RE, Groppe M, Barnard AR, et al. Retinal gene therapy in patients with choroideremia: initial findings from a phase 1/2 clinical trial. Lancet. 2014;383(9923):1129–37. https://doi.org/10.1016/S0140-6736(13)62117-0
   PubMed Web of Science ®Google Scholar
• Tolmachova T, Tolmachov OE, Wavre-Shapton ST, et al. CHM/REP1 cDNA delivery by lentiviral vectors provides functional expression of the transgene in the retinal pigment epithelium of choroideremia mice. J Gene Med. 2012;14(3):158–68. https://doi.org/10.1002/jgm.1652
   PubMed Web of Science ®Google Scholar
• Rodrigues ML, Pereira-Leal JB. Novel Rab GTPases. In: Li G, Segev N, editors. Rab GTPases and Membrane Trafficking. Bentham Science Publishers; 2012. p. 155–68.
   Google Scholar
• Wheeler DB, Zoncu R, Root DE, et al. Identification of an oncogenic RAB protein. Science. 2015;350(6257):211–7. https://doi.org/10.1126/science.aaa4903
   PubMed Web of Science ®Google Scholar
• Klinkert K, Echard A. Rab35 GTPase: A Central Regulator of Phosphoinositides and F-actin in Endocytic Recycling and Beyond. Traffic. 2016;17(10):1063–77. https://doi.org/10.1111/tra.12422
   PubMed Web of Science ®Google Scholar
• Zhu AX, Zhao Y, Flier JS. Molecular cloning of two small GTP-binding proteins from human skeletal muscle. Biochem Biophys Res Commun. 1994;205(3):1875–82. https://doi.org/10.1006/bbrc.1994.2889
   PubMed Web of Science ®Google Scholar
• Sheach LA, Adeney EM, Kucukmetin A, et al. Androgen-related expression of G-proteins in ovarian cancer. Br J Cancer. 2009;101(3):498–503. https://doi.org/10.1038/sj.bjc.6605153
   PubMed Web of Science ®Google Scholar
• Abe Y, Takeuchi T, Imai Y, et al. A Small Ras-like protein Ray/Rab1c modulates the p53-regulating activity of PRPK. Biochem Biophys Res Commun. 2006;344(1):377–85. https://doi.org/10.1016/j.bbrc.2006.03.071
   PubMed Web of Science ®Google Scholar
• Cheng KW, Lahad JP, Kuo WL, et al. The RAB25 small GTPase determines aggressiveness of ovarian and breast cancers. Nat Med. 2004;10(11):1251–6. https://doi.org/10.1038/nm1125
   PubMed Web of Science ®Google Scholar
• Fukui K, Tamura S, Wada A, et al. Expression of Rab5a in hepatocellular carcinoma: Possible involvement in epidermal growth factor signaling. Hepatol Res. 2007;37(11):957–65. https://doi.org/10.1111/j.1872-034X.2007.00143.x
   PubMed Web of Science ®Google Scholar
• Hooper S, Gaggioli C, Sahai E. A chemical biology screen reveals a role for Rab21-mediated control of actomyosin contractility in fibroblast-driven cancer invasion. Br J Cancer. 2010;102(2):392–402. https://doi.org/10.1038/sj.bjc.6605469
   PubMed Web of Science ®Google Scholar
• Hou Q, Wu YH, Grabsch H, et al. Integrative genomics identifies RAB23 as an invasion mediator gene in diffuse-type gastric cancer. Cancer Res. 2008;68(12):4623–30. https://doi.org/10.1158/0008-5472.CAN-07-5870
   PubMed Web of Science ®Google Scholar
• Kanda I, Nishimura N, Nakatsuji H, et al. Involvement of Rab13 and JRAB/MICAL-L2 in epithelial cell scattering. Oncogene. 2008;27(12):1687–95. https://doi.org/10.1038/sj.onc.1210812
   PubMed Web of Science ®Google Scholar
• Li Y, Meng X, Feng H, et al. Over-expression of the RAB5 gene in human lung adenocarcinoma cells with high metastatic potential. Chin Med Sci J. 1999;14(2):96–101.
   PubMedGoogle Scholar
• Liu J, Lamb D, Chou MM, et al. Nerve growth factor-mediated neurite outgrowth via regulation of Rab5. Mol Biol Cell. 2007;18(4):1375–84. https://doi.org/10.1091/mbc.E06-08-0725
   PubMed Web of Science ®Google Scholar
• Wang T, Gilkes DM, Takano N, et al. Hypoxia-inducible factors and RAB22A mediate formation of microvesicles that stimulate breast cancer invasion and metastasis. Proc Natl Acad Sci U S A. 2014;111(31):E3234–42. https://doi.org/10.1073/pnas.1410041111
   PubMed Web of Science ®Google Scholar
• Ng EL, Wang Y, Tang BL. Rab22B's role in trans-Golgi network membrane dynamics. Biochem Biophys Res Commun. 2007;361(3):751–7. https://doi.org/10.1016/j.bbrc.2007.07.076
   PubMed Web of Science ®Google Scholar
• Rodriguez-Gabin AG, Yin X, Si Q, et al. Transport of mannose-6-phosphate receptors from the trans-Golgi network to endosomes requires Rab31. Exp Cell Res. 2009;315(13):2215–30. https://doi.org/10.1016/j.yexcr.2009.03.020
   PubMed Web of Science ®Google Scholar
• Chua CE, Tang BL. The role of the small GTPase Rab31 in cancer. J Cell Mol Med. 2015;19(1):1–10. https://doi.org/10.1111/jcmm.12403
   PubMed Web of Science ®Google Scholar
• Grismayer B, Solch S, Seubert B, et al. Rab31 expression levels modulate tumor-relevant characteristics of breast cancer cells. Mol Cancer. 2012;11:62. https://doi.org/10.1186/1476-4598-11-62
   PubMed Web of Science ®Google Scholar
• Abba MC, Hu Y, Sun H, et al. Gene expression signature of estrogen receptor alpha status in breast cancer. BMC Genomics. 2005;6:37. https://doi.org/10.1186/1471-2164-6-37
   PubMed Web of Science ®Google Scholar
• Jin C, Rajabi H, Pitroda S, et al. Cooperative interaction between the MUC1-C oncoprotein and the Rab31 GTPase in estrogen receptor-positive breast cancer cells. PLoS One. 2012;7(7):e39432. https://doi.org/10.1371/journal.pone.0039432
   PubMed Web of Science ®Google Scholar
• Wei X, Xu H, Kufe D. MUC1 oncoprotein stabilizes and activates estrogen receptor alpha. Mol Cell. 2006;21(2):295–305. https://doi.org/10.1016/j.molcel.2005.11.030
   PubMed Web of Science ®Google Scholar
• Bravo-Cordero JJ, Marrero-Diaz R, Megias D, et al. MT1-MMP proinvasive activity is regulated by a novel Rab8-dependent exocytic pathway. EMBO J. 2007;26(6):1499–510. https://doi.org/10.1038/sj.emboj.7601606
   PubMed Web of Science ®Google Scholar
• Hendrix A, Maynard D, Pauwels P, et al. Effect of the secretory small GTPase Rab27B on breast cancer growth, invasion, and metastasis. J Natl Cancer Inst. 2010;102(12):866–80. https://doi.org/10.1093/jnci/djq153
   PubMedGoogle Scholar
• Li Y, Jia Q, Zhang Q, et al. Rab25 upregulation correlates with the proliferation, migration, and invasion of renal cell carcinoma. Biochem Biophys Res Commun. 2015;458(4):745–50. https://doi.org/10.1016/j.bbrc.2015.01.144
   PubMed Web of Science ®Google Scholar
• Cao C, Lu C, Xu J, et al. Expression of Rab25 correlates with the invasion and metastasis of gastric cancer. Chin J Cancer Res. 2013;25(2):192–9.
   PubMed Web of Science ®Google Scholar
• Gomez-Roman N, Sahasrabudhe NM, McGregor F, et al. Hypoxia-inducible factor 1 alpha is required for the tumourigenic and aggressive phenotype associated with Rab25 expression in ovarian cancer. Oncotarget. 2016;7(16):22650–64. https://doi.org/10.18632/oncotarget.7998
   PubMed Web of Science ®Google Scholar
• Ma YF, Yang B, Li J, et al. Expression of Ras-related protein 25 predicts chemotherapy resistance and prognosis in advanced non-small cell lung cancer. Genet Mol Res. 2015;14(4):13998–4008. https://doi.org/10.4238/2015.October.29.19
   PubMed Web of Science ®Google Scholar
• Casanova JE, Wang X, Kumar R, et al. Association of Rab25 and Rab11a with the apical recycling system of polarized Madin-Darby canine kidney cells. Mol Biol Cell. 1999;10(1):47–61. https://doi.org/10.1091/mbc.10.1.47
   PubMed Web of Science ®Google Scholar
• Caswell PT, Chan M, Lindsay AJ, et al. Rab-coupling protein coordinates recycling of alpha5beta1 integrin and EGFR1 to promote cell migration in 3D microenvironments. J Cell Biol. 2008;183(1):143–55. https://doi.org/10.1083/jcb.200804140
   PubMed Web of Science ®Google Scholar
• Caswell PT, Spence HJ, Parsons M, et al. Rab25 associates with alpha5beta1 integrin to promote invasive migration in 3D microenvironments. Dev Cell. 2007;13(4):496–510. https://doi.org/10.1016/j.devcel.2007.08.012
   PubMed Web of Science ®Google Scholar
• Goldenring JR, Shen KR, Vaughan HD, et al. Identification of a small GTP-binding protein, Rab25, expressed in the gastrointestinal mucosa, kidney, and lung. J Biol Chem. 1993;268(25):18419–22.
   PubMed Web of Science ®Google Scholar
• Cheng JM, Volk L, Janaki DK, et al. Tumor suppressor function of Rab25 in triple-negative breast cancer. Int J Cancer. 2010;126(12):2799–812.
   PubMed Web of Science ®Google Scholar
• Nam KT, Lee HJ, Smith JJ, et al. Loss of Rab25 promotes the development of intestinal neoplasia in mice and is associated with human colorectal adenocarcinomas. J Clin Invest. 2010;120(3):840–9. https://doi.org/10.1172/JCI40728
   PubMed Web of Science ®Google Scholar
• Dozynkiewicz MA, Jamieson NB, Macpherson I, et al. Rab25 and CLIC3 collaborate to promote integrin recycling from late endosomes/lysosomes and drive cancer progression. Dev Cell. 2012;22(1):131–45. https://doi.org/10.1016/j.devcel.2011.11.008
   PubMed Web of Science ®Google Scholar
• Lall P, Horgan CP, Oda S, et al. Structural and functional analysis of FIP2 binding to the endosome-localised Rab25 GTPase. Biochim Biophys Acta. 2013;1834(12):2679–90. https://doi.org/10.1016/j.bbapap.2013.09.005
   PubMedGoogle Scholar
• Krstic D, Knuesel I. Deciphering the mechanism underlying late-onset Alzheimer disease. Nat Rev Neurol. 2013;9(1):25–34. https://doi.org/10.1038/nrneurol.2012.236
   PubMed Web of Science ®Google Scholar
• Kimberly WT, Esler WP, Ye W, et al. Notch and the amyloid precursor protein are cleaved by similar gamma-secretase(s). Biochemistry. 2003;42(1):137–44. https://doi.org/10.1021/bi026888g
   PubMed Web of Science ®Google Scholar
• Lin X, Koelsch G, Wu S, et al. Human aspartic protease memapsin 2 cleaves the beta-secretase site of beta-amyloid precursor protein. Proc Natl Acad Sci U S A. 2000;97(4):1456–60. https://doi.org/10.1073/pnas.97.4.1456
   PubMed Web of Science ®Google Scholar
• Sinha S, Anderson JP, Barbour R, et al. Purification and cloning of amyloid precursor protein beta-secretase from human brain. Nature. 1999;402(6761):537–40. https://doi.org/10.1038/990114
   PubMed Web of Science ®Google Scholar
• Vassar R, Bennett BD, Babu-Khan S, et al. Beta-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science. 1999;286(5440):735–41. https://doi.org/10.1126/science.286.5440.735
   PubMed Web of Science ®Google Scholar
• Jiang Y, Mullaney KA, Peterhoff CM, et al. Alzheimer's-related endosome dysfunction in Down syndrome is Abeta-independent but requires APP and is reversed by BACE-1 inhibition. Proc Natl Acad Sci U S A. 2010;107(4):1630–5. https://doi.org/10.1073/pnas.0908953107
   PubMed Web of Science ®Google Scholar
• Salehi A, Delcroix JD, Belichenko PV, et al. Increased App expression in a mouse model of Down's syndrome disrupts NGF transport and causes cholinergic neuron degeneration. Neuron. 2006;51(1):29–42. https://doi.org/10.1016/j.neuron.2006.05.022
   PubMed Web of Science ®Google Scholar
• Kim S, Sato Y, Mohan PS, et al. Evidence that the rab5 effector APPL1 mediates APP-betaCTF-induced dysfunction of endosomes in Down syndrome and Alzheimer's disease. Mol Psychiatry. 2016;21(5):707–16. https://doi.org/10.1038/mp.2015.97
   PubMed Web of Science ®Google Scholar
• Cataldo AM, Peterhoff CM, Troncoso JC, et al. Endocytic pathway abnormalities precede amyloid beta deposition in sporadic Alzheimer's disease and Down syndrome: differential effects of APOE genotype and presenilin mutations. Am J Pathol. 2000;157(1):277–86. https://doi.org/10.1016/S0002-9440(10)64538-5
   PubMed Web of Science ®Google Scholar
• Ginsberg SD, Mufson EJ, Alldred MJ, et al. Upregulation of select rab GTPases in cholinergic basal forebrain neurons in mild cognitive impairment and Alzheimer's disease. J Chem Neuroanat. 2011;42(2):102–10. https://doi.org/10.1016/j.jchemneu.2011.05.012
   PubMed Web of Science ®Google Scholar
• Ginsberg SD, Mufson EJ, Counts SE, et al. Regional selectivity of rab5 and rab7 protein upregulation in mild cognitive impairment and Alzheimer's disease. J Alzheimers Dis. 2010;22(2):631–9. https://doi.org/10.3233/JAD-2010-101080
   PubMed Web of Science ®Google Scholar
• Grbovic OM, Mathews PM, Jiang Y, et al. Rab5-stimulated up-regulation of the endocytic pathway increases intracellular beta-cleaved amyloid precursor protein carboxyl-terminal fragment levels and Abeta production. J Biol Chem. 2003;278(33):31261–8. https://doi.org/10.1074/jbc.M304122200
   PubMed Web of Science ®Google Scholar
• Kalaidzidis I, Miaczynska M, Brewinska-Olchowik M, et al. APPL endosomes are not obligatory endocytic intermediates but act as stable cargo-sorting compartments. J Cell Biol. 2015;211(1):123–44. https://doi.org/10.1083/jcb.201311117
   PubMed Web of Science ®Google Scholar
• Miaczynska M, Christoforidis S, Giner A, et al. APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. Cell. 2004;116(3):445–56. https://doi.org/10.1016/S0092-8674(04)00117-5
   PubMed Web of Science ®Google Scholar
• Schenck A, Goto-Silva L, Collinet C, et al. The endosomal protein Appl1 mediates Akt substrate specificity and cell survival in vertebrate development. Cell. 2008;133(3):486–97. https://doi.org/10.1016/j.cell.2008.02.044
   PubMed Web of Science ®Google Scholar
• Bacon RA, Salminen A, Ruohola H, et al. The GTP-binding protein Ypt1 is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants. J Cell Biol. 1989;109(3):1015–22. https://doi.org/10.1083/jcb.109.3.1015
   PubMed Web of Science ®Google Scholar
• Cooper AA, Gitler AD, Cashikar A, et al. Alpha-synuclein blocks ER-Golgi traffic and Rab1 rescues neuron loss in Parkinson's models. Science. 2006;313(5785):324–8. https://doi.org/10.1126/science.1129462
   PubMed Web of Science ®Google Scholar
• Coune PG, Bensadoun JC, Aebischer P, et al. Rab1A over-expression prevents Golgi apparatus fragmentation and partially corrects motor deficits in an alpha-synuclein based rat model of Parkinson's disease. J Parkinsons Dis. 2011;1(4):373–87.
   PubMedGoogle Scholar
• Nikoshkov A, Broliden K, Attarha S, et al. Expression pattern of the PRDX2, RAB1A, RAB1B, RAB5A and RAB25 genes in normal and cancer cervical tissues. Int J Oncol. 2015;46(1):107–12. https://doi.org/10.3892/ijo.2014.2724
   PubMed Web of Science ®Google Scholar
• Quan Y, Song Q, Wang J, et al. MiR-1202 functions as a tumor suppressor in glioma cells by targeting Rab1A. Tumour Biol. 2017;39(4):1010428317697565. https://doi.org/10.1177/1010428317697565
   Google Scholar
• Sannerud R, Marie M, Nizak C, et al. Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Mol Biol Cell. 2006;17(4):1514–26. https://doi.org/10.1091/mbc.E05-08-0792
   PubMed Web of Science ®Google Scholar
• Saraste J, Lahtinen U, Goud B. Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway. J Cell Sci. 1995;108(Pt 4):1541–52.
   PubMedGoogle Scholar
• Segev N, Mulholland J, Botstein D. The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery. Cell. 1988;52(6):915–24. https://doi.org/10.1016/0092-8674(88)90433-3
   PubMed Web of Science ®Google Scholar
• Shimada K, Uzawa K, Kato M, et al. Aberrant expression of RAB1A in human tongue cancer. Br J Cancer. 2005;92(10):1915–21. https://doi.org/10.1038/sj.bjc.6602594
   PubMed Web of Science ®Google Scholar
• Thomas JD, Zhang YJ, Wei YH, et al. Rab1A is an mTORC1 activator and a colorectal oncogene. Cancer Cell. 2014;26(5):754–69. https://doi.org/10.1016/j.ccell.2014.09.008
   PubMed Web of Science ®Google Scholar
• Tisdale EJ, Bourne JR, Khosravi-Far R, et al. GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J Cell Biol. 1992;119(4):749–61. https://doi.org/10.1083/jcb.119.4.749
   PubMed Web of Science ®Google Scholar
• Wang X, Liu F, Qin X, et al. Expression of Rab1A is upregulated in human lung cancer and associated with tumor size and T stage. Aging (Albany NY). 2016;8(11):2790–8. https://doi.org/10.18632/aging.101087
   PubMedGoogle Scholar
• Webster CP, Smith EF, Bauer CS, et al. The C9orf72 protein interacts with Rab1a and the ULK1 complex to regulate initiation of autophagy. EMBO J. 2016;35(15):1656–76. https://doi.org/10.15252/embj.201694401
   PubMed Web of Science ®Google Scholar
• Wilson BS, Nuoffer C, Meinkoth JL, et al. A Rab1 mutant affecting guanine nucleotide exchange promotes disassembly of the Golgi apparatus. J Cell Biol. 1994;125(3):557–71. https://doi.org/10.1083/jcb.125.3.557
   PubMed Web of Science ®Google Scholar
• Winslow AR, Chen CW, Corrochano S, et al. alpha-Synuclein impairs macroautophagy: implications for Parkinson's disease. J Cell Biol. 2010;190(6):1023–37. https://doi.org/10.1083/jcb.201003122
   PubMed Web of Science ®Google Scholar
• Wu G, Yussman MG, Barrett TJ, et al. Increased myocardial Rab GTPase expression: a consequence and cause of cardiomyopathy. Circ Res. 2001;89(12):1130–7. https://doi.org/10.1161/hh2401.100427
   PubMed Web of Science ®Google Scholar
• Xu H, Qian M, Zhao B, et al. Inhibition of RAB1A suppresses epithelial-mesenchymal transition and proliferation of triple-negative breast cancer cells. Oncol Rep. 2017;37(3):1619–26. https://doi.org/10.3892/or.2017.5404
   PubMed Web of Science ®Google Scholar
• Zenner HL, Yoshimura S, Barr FA, et al. Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment. J Virol. 2011;85(16):8012–21. https://doi.org/10.1128/JVI.00500-11
   PubMed Web of Science ®Google Scholar
• Connor MG, Pulsifer AR, Price CT, et al. Yersinia pestis Requires Host Rab1b for Survival in Macrophages. PLoS Pathog. 2015;11(10):e1005241. https://doi.org/10.1371/journal.ppat.1005241
   PubMed Web of Science ®Google Scholar
• Dugan JM, deWit C, McConlogue L, et al. The Ras-related GTP-binding protein, Rab1B, regulates early steps in exocytic transport and processing of beta-amyloid precursor protein. J Biol Chem. 1995;270(18):10982–9. https://doi.org/10.1074/jbc.270.18.10982
   PubMed Web of Science ®Google Scholar
• Halberg N, Sengelaub CA, Navrazhina K, et al. PITPNC1 Recruits RAB1B to the Golgi Network to Drive Malignant Secretion. Cancer Cell. 2016;29(3):339–53. https://doi.org/10.1016/j.ccell.2016.02.013
   PubMed Web of Science ®Google Scholar
• He H, Dai F, Yu L, et al. Identification and characterization of nine novel human small GTPases showing variable expressions in liver cancer tissues. Gene Expr. 2002;10(5-6):231–42. https://doi.org/10.3727/000000002783992406
   PubMed Web of Science ®Google Scholar
• Jiang HL, Sun HF, Gao SP, et al. Loss of RAB1B promotes triple-negative breast cancer metastasis by activating TGF-beta/SMAD signaling. Oncotarget. 2015;6(18):16352–65. https://doi.org/10.18632/oncotarget.3877
   PubMed Web of Science ®Google Scholar
• Kakuta S, Yamaguchi J, Suzuki C, et al. Small GTPase Rab1B is associated with ATG9A vesicles and regulates autophagosome formation. FASEB J. 2017;31(9):3757–73. https://org/10.1096/fj.201601052
   PubMed Web of Science ®Google Scholar
• Mihai Gazdag E, Streller A, Haneburger I, et al. Mechanism of Rab1b deactivation by the Legionella pneumophila GAP LepB. EMBO Rep. 2013;14(2):199–205. https://doi.org/10.1038/embor.2012.211
   PubMed Web of Science ®Google Scholar
• Mochizuki Y, Ohashi R, Kawamura T, et al. Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6) is regulated by small GTPase Rab1B in the early secretory and autophagic pathways. J Biol Chem. 2013;288(2):1009–21. https://doi.org/10.1074/jbc.M112.395087
   PubMed Web of Science ®Google Scholar
• Muller MP, Peters H, Blumer J, et al. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science. 2010;329(5994):946–9. https://doi.org/10.1126/science.1192276
   PubMed Web of Science ®Google Scholar
• Yadav V, Panganiban AT, Honer Zu Bentrup K, et al. Influenza infection modulates vesicular trafficking and induces Golgi complex disruption. Virusdisease. 2016;27(4):357–68. https://doi.org/10.1007/s13337-016-0347-3
   PubMedGoogle Scholar
• Yamayoshi S, Neumann G, Kawaoka Y. Role of the GTPase Rab1b in ebolavirus particle formation. J Virol. 2010;84(9):4816–20. https://doi.org/10.1128/JVI.00010-10
   PubMed Web of Science ®Google Scholar
• Yang XZ, Cui SZ, Zeng LS, et al. Overexpression of Rab1B and MMP9 predicts poor survival and good response to chemotherapy in patients with colorectal cancer. Aging (Albany NY). 2017;9(3):914–31.
   PubMedGoogle Scholar
• Dey KK, Pal I, Bharti R, et al. Identification of RAB2A and PRDX1 as the potential biomarkers for oral squamous cell carcinoma using mass spectrometry-based comparative proteomic approach. Tumour Biol. 2015;36(12):9829–37. https://doi.org/10.1007/s13277-015-3758-7
   PubMedGoogle Scholar
• Fujita N, Huang W, Lin TH, et al. Genetic screen in Drosophila muscle identifies autophagy-mediated T-tubule remodeling and a Rab2 role in autophagy. Elife. 2017;6:https://doi.org/10.7554/eLife.23367
   Web of Science ®Google Scholar
• Lomnytska MI, Becker S, Hellman K, et al. Diagnostic protein marker patterns in squamous cervical cancer. Proteomics Clin Appl. 2010;4(1):17–31. https://doi.org/10.1002/prca.200900086
   PubMed Web of Science ®Google Scholar
• Lorincz P, Toth S, Benko P, et al. Rab2 promotes autophagic and endocytic lysosomal degradation. J Cell Biol. 2017;216(7):1937–47. https://doi.org/10.1083/jcb.201611027
   PubMed Web of Science ®Google Scholar
• Ortiz Sandoval C, Simmen T. Rab proteins of the endoplasmic reticulum: functions and interactors. Biochem Soc Trans. 2012;40(6):1426–32. https://doi.org/10.1042/BST20120158
   PubMedGoogle Scholar
• Saraste J. Spatial and Functional Aspects of ER-Golgi Rabs and Tethers. Front Cell Dev Biol. 2016;4:28. https://doi.org/10.3389/fcell.2016.00028
   PubMed Web of Science ®Google Scholar
• Tisdale EJ, Jackson MR. Rab2 protein enhances coatomer recruitment to pre-Golgi intermediates. J Biol Chem. 1998;273(27):17269–77. https://doi.org/10.1074/jbc.273.27.17269
   PubMed Web of Science ®Google Scholar
• White JA, 2nd, Anderson E, Zimmerman K, et al. Huntingtin differentially regulates the axonal transport of a sub-set of Rab-containing vesicles in vivo. Hum Mol Genet. 2015;24(25):7182–95. https://doi.org/10.1093/hmg/ddv415
   PubMed Web of Science ®Google Scholar
• Aizawa M, Fukuda M. Small GTPase Rab2B and Its Specific Binding Protein Golgi-associated Rab2B Interactor-like 4 (GARI-L4) Regulate Golgi Morphology. J Biol Chem. 2015;290(36):22250–61. https://doi.org/10.1074/jbc.M115.669242
   PubMed Web of Science ®Google Scholar
• Ni X, Ma Y, Cheng H, et al. Molecular cloning and characterization of a novel human Rab (Rab2B) gene. J Hum Genet. 2002;47(10):548–51. https://doi.org/10.1007/s100380200083
   PubMed Web of Science ®Google Scholar
• Bereczki E, Francis PT, Howlett D, et al. Synaptic proteins predict cognitive decline in Alzheimer's disease and Lewy body dementia. Alzheimers Dement. 2016;12(11):1149–58. https://doi.org/10.1016/j.jalz.2016.04.005
   PubMed Web of Science ®Google Scholar
• Bustos MA, Lucchesi O, Ruete MC, et al. Small GTPases in acrosomal exocytosis. Methods Mol Biol. 2015;1298:141–60. https://doi.org/10.1007/978-1-4939-2569-8_12
   PubMedGoogle Scholar
• Chen RH, Wislet-Gendebien S, Samuel F, et al. alpha-Synuclein membrane association is regulated by the Rab3a recycling machinery and presynaptic activity. J Biol Chem. 2013;288(11):7438–49. https://doi.org/10.1074/jbc.M112.439497
   PubMed Web of Science ®Google Scholar
• Encarnacao M, Espada L, Escrevente C, et al. A Rab3a-dependent complex essential for lysosome positioning and plasma membrane repair. J Cell Biol. 2016;213(6):631–40. https://doi.org/10.1083/jcb.201511093
   PubMed Web of Science ®Google Scholar
• Fischer von Mollard G, Mignery GA, Baumert M, et al. rab3 is a small GTP-binding protein exclusively localized to synaptic vesicles. Proc Natl Acad Sci U S A. 1990;87(5):1988–92. https://doi.org/10.1073/pnas.87.5.1988
   PubMed Web of Science ®Google Scholar
• Hong Y, Zhao T, Li XJ, et al. Mutant Huntingtin Impairs BDNF Release from Astrocytes by Disrupting Conversion of Rab3a-GTP into Rab3a-GDP. J Neurosci. 2016;36(34):8790–801. https://doi.org/10.1523/JNEUROSCI.0168-16.2016
   PubMed Web of Science ®Google Scholar
• Kang HJ, Voleti B, Hajszan T, et al. Decreased expression of synapse-related genes and loss of synapses in major depressive disorder. Nat Med. 2012;18(9):1413–7. https://doi.org/10.1038/nm.2886
   PubMed Web of Science ®Google Scholar
• Kim JK, Lee SY, Park CW, et al. Rab3a promotes brain tumor initiation and progression. Mol Biol Rep. 2014;41(9):5903–11. https://doi.org/10.1007/s11033-014-3465-2
   PubMed Web of Science ®Google Scholar
• Lodhi SS, Farmer R, Singh AK, et al. 3D structure generation, virtual screening and docking of human Ras-associated binding (Rab3A) protein involved in tumourigenesis. Mol Biol Rep. 2014;41(6):3951–9. https://doi.org/10.1007/s11033-014-3263-x
   PubMed Web of Science ®Google Scholar
• Pavlos NJ, Jahn R. Distinct yet overlapping roles of Rab GTPases on synaptic vesicles. Small GTPases. 2011;2(2):77–81. https://doi.org/10.4161/sgtp.2.2.15201
   PubMedGoogle Scholar
• Raiborg C, Stenmark H. Plasma membrane repairs by small GTPase Rab3a. J Cell Biol. 2016;213(6):613–5. https://doi.org/10.1083/jcb.201606006
   PubMed Web of Science ®Google Scholar
• Saetre P, Jazin E, Emilsson L. Age-related changes in gene expression are accelerated in Alzheimer's disease. Synapse. 2011;65(9):971–4. https://doi.org/10.1002/syn.20933
   PubMed Web of Science ®Google Scholar
• Chung CY, Koprich JB, Hallett PJ, et al. Functional enhancement and protection of dopaminergic terminals by RAB3B overexpression. Proc Natl Acad Sci U S A. 2009;106(52):22474–9. https://doi.org/10.1073/pnas.0912193106
   PubMed Web of Science ®Google Scholar
• Liu Q, Tang H, Liu X, et al. miR-200b as a prognostic factor targets multiple members of RAB family in glioma. Med Oncol. 2014;31(3):859. https://doi.org/10.1007/s12032-014-0859-x
   PubMed Web of Science ®Google Scholar
• Nishioka H, Haraoka J. Significance of immunohistochemical expression of Rab3B and SNAP-25 in growth hormone-producing pituitary adenomas. Acta Neuropathol. 2005;109(6):598–602. https://doi.org/10.1007/s00401-005-1008-6
   PubMed Web of Science ®Google Scholar
• Piper Hanley K, Hearn T, Berry A, et al. In vitro expression of NGN3 identifies RAB3B as the predominant Ras-associated GTP-binding protein 3 family member in human islets. J Endocrinol. 2010;207(2):151–61. https://doi.org/10.1677/JOE-10-0120
   PubMed Web of Science ®Google Scholar
• Schluter OM, Khvotchev M, Jahn R, et al. Localization versus function of Rab3 proteins. Evidence for a common regulatory role in controlling fusion. J Biol Chem. 2002;277(43):40919–29. https://doi.org/10.1074/jbc.M203704200
   PubMed Web of Science ®Google Scholar
• Schluter OM, Schmitz F, Jahn R, et al. A complete genetic analysis of neuronal Rab3 function. J Neurosci. 2004;24(29):6629–37. https://doi.org/10.1523/JNEUROSCI.1610-04.2004
   PubMed Web of Science ®Google Scholar
• Schonn JS, van Weering JR, Mohrmann R, et al. Rab3 proteins involved in vesicle biogenesis and priming in embryonic mouse chromaffin cells. Traffic. 2010;11(11):1415–28. https://doi.org/10.1111/j.1600-0854.2010.01107.x
   PubMed Web of Science ®Google Scholar
• Tsetsenis T, Younts TJ, Chiu CQ, et al. Rab3B protein is required for long-term depression of hippocampal inhibitory synapses and for normal reversal learning. Proc Natl Acad Sci U S A. 2011;108(34):14300–5. https://doi.org/10.1073/pnas.1112237108
   PubMed Web of Science ®Google Scholar
• van ISC, Tuvim MJ, Weimbs T, et al. Direct interaction between Rab3b and the polymeric immunoglobulin receptor controls ligand-stimulated transcytosis in epithelial cells. Dev Cell. 2002;2(2):219–28. https://doi.org/10.1016/S1534-5807(02)00115-6
   PubMed Web of Science ®Google Scholar
• Ye F, Tang H, Liu Q, et al. miR-200b as a prognostic factor in breast cancer targets multiple members of RAB family. J Transl Med. 2014;12:17. https://doi.org/10.1186/1479-5876-12-17
   PubMed Web of Science ®Google Scholar
• Zou L, Zhou J, Zhang J, et al. The GTPase Rab3b/3c-positive recycling vesicles are involved in cross-presentation in dendritic cells. Proc Natl Acad Sci U S A. 2009;106(37):15801–6. https://doi.org/10.1073/pnas.0905684106
   PubMed Web of Science ®Google Scholar
• Carroll K, Ray K, Helm B, et al. Differential expression of Rab3 isoforms in high- and low-secreting mast cell lines. Eur J Cell Biol. 2001;80(4):295–302. https://doi.org/10.1078/0171-9335-00161
   PubMed Web of Science ®Google Scholar
• Cheng H, Ma Y, Ni X, et al. Cloning, mapping, and characterization of the human Rab3C gene. Biochem Genet. 2002;40(7-8):263–72. https://doi.org/10.1023/A:1019834901190
   PubMed Web of Science ®Google Scholar
• Fischer von Mollard G, Stahl B, Khokhlatchev A, et al. Rab3C is a synaptic vesicle protein that dissociates from synaptic vesicles after stimulation of exocytosis. J Biol Chem. 1994;269(15):10971–4.
   PubMed Web of Science ®Google Scholar
• Uphues I, Chern Y, Eckel J. Insulin-dependent translocation of the small GTP-binding protein rab3C in cardiac muscle: studies on insulin-resistant Zucker rats. FEBS Lett. 1995;377(2):109–12. https://doi.org/10.1016/0014-5793(95)01315-6
   PubMed Web of Science ®Google Scholar
• Larkin JM, Woo B, Balan V, et al. Rab3D, a small GTP-binding protein implicated in regulated secretion, is associated with the transcytotic pathway in rat hepatocytes. Hepatology. 2000;32(2):348–56. https://doi.org/10.1053/jhep.2000.9110
   PubMed Web of Science ®Google Scholar
• Luo Y, Ye GY, Qin SL, et al. High expression of Rab3D predicts poor prognosis and associates with tumor progression in colorectal cancer. Int J Biochem Cell Biol. 2016;75:53–62. https://doi.org/10.1016/j.biocel.2016.03.017
   PubMed Web of Science ®Google Scholar
• Martelli AM, Baldini G, Tabellini G, et al. Rab3A and Rab3D control the total granule number and the fraction of granules docked at the plasma membrane in PC12 cells. Traffic. 2000;1(12):976–86.
   PubMed Web of Science ®Google Scholar
• Millar AL, Pavios NJ, Xu J, et al. Rab3D: a regulator of exocytosis in non-neuronal cells. Histol Histopathol. 2002;17(3):929–36.
   PubMed Web of Science ®Google Scholar
• Pavlos NJ, Xu J, Riedel D, et al. Rab3D regulates a novel vesicular trafficking pathway that is required for osteoclastic bone resorption. Mol Cell Biol. 2005;25(12):5253–69. https://doi.org/10.1128/MCB.25.12.5253-5269.2005
   PubMed Web of Science ®Google Scholar
• Yang J, Liu W, Lu X, et al. High expression of small GTPase Rab3D promotes cancer progression and metastasis. Oncotarget. 2015;6(13):11125–38. https://doi.org/10.18632/oncotarget.3575
   PubMed Web of Science ®Google Scholar
• Zhang J, Kong R, Sun L. Silencing of Rab3D suppresses the proliferation and invasion of esophageal squamous cell carcinoma cells. Biomed Pharmacother. 2017;91:402–7. https://doi.org/10.1016/j.biopha.2017.04.010
   PubMed Web of Science ®Google Scholar
• Zhu S, Chim SM, Cheng T, et al. Calmodulin interacts with Rab3D and modulates osteoclastic bone resorption. Sci Rep. 2016;6:37963. https://doi.org/10.1038/srep37963
   PubMed Web of Science ®Google Scholar
• Arjonen A, Alanko J, Veltel S, et al. Distinct recycling of active and inactive beta1 integrins. Traffic. 2012;13(4):610–25. https://doi.org/10.1111/j.1600-0854.2012.01327.x
   PubMed Web of Science ®Google Scholar
• Barbarin A, Frade R. Procathepsin L secretion, which triggers tumour progression, is regulated by Rab4a in human melanoma cells. Biochem J. 2011;437(1):97–107. https://doi.org/10.1042/BJ20110361
   PubMedGoogle Scholar
• Chen Y, Wang Y, Zhang J, et al. Rab10 and myosin-Va mediate insulin-stimulated GLUT4 storage vesicle translocation in adipocytes. J Cell Biol. 2012;198(4):545–60. https://doi.org/10.1083/jcb.201111091
   PubMed Web of Science ®Google Scholar
• Do MT, Chai TF, Casey PJ, et al. Isoprenylcysteine carboxylmethyltransferase function is essential for RAB4A-mediated integrin beta3 recycling, cell migration and cancer metastasis. Oncogene. 2017;36(14):5757–67. https://doi.org/10.1038/onc.2017.183
   PubMedGoogle Scholar
• Lazzarino DA, Blier P, Mellman I. The monomeric guanosine triphosphatase rab4 controls an essential step on the pathway of receptor-mediated antigen processing in B cells. J Exp Med. 1998;188(10):1769–74. https://doi.org/10.1084/jem.188.10.1769
   PubMed Web of Science ®Google Scholar
• Uphues I, Kolter T, Goud B, et al. Failure of insulin-regulated recruitment of the glucose transporter GLUT4 in cardiac muscle of obese Zucker rats is associated with alterations of small-molecular-mass GTP-binding proteins. Biochem J. 1995;311(Pt 1):161–6. https://doi.org/10.1042/bj3110161
   PubMedGoogle Scholar
• van der Sluijs P, Hull M, Webster P, et al. The small GTP-binding protein rab4 controls an early sorting event on the endocytic pathway. Cell. 1992;70(5):729–40. https://doi.org/10.1016/0092-8674(92)90307-X
   PubMed Web of Science ®Google Scholar
• Van Der Sluijs P, Hull M, Zahraoui A, et al. The small GTP-binding protein rab4 is associated with early endosomes. Proc Natl Acad Sci U S A. 1991;88(14):6313–7. https://doi.org/10.1073/pnas.88.14.6313
   PubMed Web of Science ®Google Scholar
• Hou L, Cai MJ, Liu W, et al. Small GTPase Rab4b participates in the gene transcription of 20-hydroxyecdysone and insulin pathways to regulate glycogen level and metamorphosis. Dev Biol. 2012;371(1):13–22. https://doi.org/10.1016/j.ydbio.2012.06.015
   PubMed Web of Science ®Google Scholar
• Kaddai V, Gonzalez T, Keslair F, et al. Rab4b is a small GTPase involved in the control of the glucose transporter GLUT4 localization in adipocyte. PLoS One. 2009;4(4):e5257. https://doi.org/10.1371/journal.pone.0005257
   PubMed Web of Science ®Google Scholar
• Krawczyk M, Leimgruber E, Seguin-Estevez Q, et al. Expression of RAB4B, a protein governing endocytic recycling, is co-regulated with MHC class II genes. Nucleic Acids Res. 2007;35(2):595–605. https://doi.org/10.1093/nar/gkl980
   PubMed Web of Science ®Google Scholar
• Perrin L, Lacas-Gervais S, Gilleron J, et al. Rab4b controls an early endosome sorting event by interacting with the gamma-subunit of the clathrin adaptor complex 1. J Cell Sci. 2013;126(Pt 21):4950–62. https://doi.org/10.1242/jcs.130575
   PubMed Web of Science ®Google Scholar
• Thean LF, Wong YH, Lo M, et al. Chromosome 19q13 disruption alters expressions of CYP2A7, MIA and MIA-RAB4B lncRNA and contributes to FAP-like phenotype in APC mutation-negative familial colorectal cancer patients. PLoS One. 2017;12(3):e0173772. https://doi.org/10.1371/journal.pone.0173772
   PubMed Web of Science ®Google Scholar
• Gorvel JP, Chavrier P, Zerial M, et al. rab5 controls early endosome fusion in vitro. Cell. 1991;64(5):915–25. https://doi.org/10.1016/0092-8674(91)90316-Q
   PubMed Web of Science ®Google Scholar
• Lu Y, Dong S, Hao B, et al. Vacuolin-1 potently and reversibly inhibits autophagosome-lysosome fusion by activating RAB5A. Autophagy. 2014;10(11):1895–905. https://doi.org/10.4161/auto.32200
   PubMed Web of Science ®Google Scholar
• Saitoh S, Maruyama T, Yako Y, et al. Rab5-regulated endocytosis plays a crucial role in apical extrusion of transformed cells. Proc Natl Acad Sci U S A. 2017;114(12):E2327–E36. https://doi.org/10.1073/pnas.1602349114
   PubMed Web of Science ®Google Scholar
• Silva P, Soto N, Diaz J, et al. Down-regulation of Rab5 decreases characteristics associated with maintenance of cell transformation. Biochem Biophys Res Commun. 2015;464(2):642–6. https://doi.org/10.1016/j.bbrc.2015.06.176
   PubMed Web of Science ®Google Scholar
• Xu Y, An Y, Wang Y, et al. miR-101 inhibits autophagy and enhances cisplatin-induced apoptosis in hepatocellular carcinoma cells. Oncol Rep. 2013;29(5):2019–24. https://doi.org/10.3892/or.2013.2338
   PubMed Web of Science ®Google Scholar
• Yu MH, Luo Y, Qin SL, et al. Increased expression of Rab5A predicts metastasis and poor prognosis in colorectal cancer patients. Int J Clin Exp Pathol. 2015;8(6):6974–80.
   PubMed Web of Science ®Google Scholar
• Arnett AL, Bayazitov I, Blaabjerg M, et al. Antisense oligonucleotide against GTPase Rab5b inhibits metabotropic agonist DHPG-induced neuroprotection. Brain Res. 2004;1028(1):59–65. https://doi.org/10.1016/j.brainres.2004.08.064
   PubMed Web of Science ®Google Scholar
• Bucci C, Lutcke A, Steele-Mortimer O, et al. Co-operative regulation of endocytosis by three Rab5 isoforms. FEBS Lett. 1995;366(1):65–71. https://doi.org/10.1016/0014-5793(95)00477-Q
   PubMed Web of Science ®Google Scholar
• Yun HJ, Kim H, Ga I, et al. An early endosome regulator, Rab5b, is an LRRK2 kinase substrate. J Biochem. 2015;157(6):485–95. https://doi.org/10.1093/jb/mvv005
   PubMed Web of Science ®Google Scholar
• Onodera Y, Nam JM, Hashimoto A, et al. Rab5c promotes AMAP1-PRKD2 complex formation to enhance beta1 integrin recycling in EGF-induced cancer invasion. J Cell Biol. 2012;197(7):983–96. https://doi.org/10.1083/jcb.201201065
   PubMed Web of Science ®Google Scholar
• Tan YS, Kim M, Kingsbury TJ, et al. Regulation of RAB5C is important for the growth inhibitory effects of MiR-509 in human precursor-B acute lymphoblastic leukemia. PLoS One. 2014;9(11):e111777. https://doi.org/10.1371/journal.pone.0111777
   PubMed Web of Science ®Google Scholar
• Vizoso M, Ferreira HJ, Lopez-Serra P, et al. Epigenetic activation of a cryptic TBC1D16 transcript enhances melanoma progression by targeting EGFR. Nat Med. 2015;21(7):741–50. https://doi.org/10.1038/nm.3863
   PubMed Web of Science ®Google Scholar
• Bardin S, Miserey-Lenkei S, Hurbain I, et al. Phenotypic characterisation of RAB6A knockout mouse embryonic fibroblasts. Biol Cell. 2015;107(12):427–39. https://doi.org/10.1111/boc.201400083
   PubMed Web of Science ®Google Scholar
• Elfrink HL, Zwart R, Cavanillas ML, et al. Rab6 is a modulator of the unfolded protein response: implications for Alzheimer's disease. J Alzheimers Dis. 2012;28(4):917–29.
   PubMed Web of Science ®Google Scholar
• Goud B, Akhmanova A. Rab6 GTPase. In: Li G, Segev N, editors. Rab GTPases and Membrane Trafficking. Bentham Science Publishers; 2012. p. 34–46.
   Google Scholar
• Lee PL, Ohlson MB, Pfeffer SR. Rab6 regulation of the kinesin family KIF1C motor domain contributes to Golgi tethering. Elife. 2015;4:https://doi.org/10.7554/eLife.06029
   Web of Science ®Google Scholar
• Peeters K, Litvinenko I, Asselbergh B, et al. Molecular defects in the motor adaptor BICD2 cause proximal spinal muscular atrophy with autosomal-dominant inheritance. Am J Hum Genet. 2013;92(6):955–64. https://doi.org/10.1016/j.ajhg.2013.04.013
   PubMed Web of Science ®Google Scholar
• Seifert W, Kuhnisch J, Maritzen T, et al. Cohen syndrome-associated protein COH1 physically and functionally interacts with the small GTPase RAB6 at the Golgi complex and directs neurite outgrowth. J Biol Chem. 2015;290(6):3349–58. https://doi.org/10.1074/jbc.M114.608174
   PubMed Web of Science ®Google Scholar
• White J, Johannes L, Mallard F, et al. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J Cell Biol. 1999;147(4):743–60. https://doi.org/10.1083/jcb.147.4.743
   PubMed Web of Science ®Google Scholar
• Opdam FJ, Echard A, Croes HJ, et al. The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus. J Cell Sci. 2000;113(Pt 15):2725–35.
   PubMed Web of Science ®Google Scholar
• Wanschers BF, van de Vorstenbosch R, Schlager MA, et al. A role for the Rab6B Bicaudal-D1 interaction in retrograde transport in neuronal cells. Exp Cell Res. 2007;313(16):3408–20. https://doi.org/10.1016/j.yexcr.2007.05.032
   PubMed Web of Science ®Google Scholar
• Shan J, Mason JM, Yuan L, et al. Rab6c, a new member of the rab gene family, is involved in drug resistance in MCF7/AdrR cells. Gene. 2000;257(1):67–75. https://doi.org/10.1016/S0378-1119(00)00395-4
   PubMed Web of Science ®Google Scholar
• Young J, Menetrey J, Goud B. RAB6C is a retrogene that encodes a centrosomal protein involved in cell cycle progression. J Mol Biol. 2010;397(1):69–88. https://doi.org/10.1016/j.jmb.2010.01.009
   PubMed Web of Science ®Google Scholar
• Chi ZL, Akahori M, Obazawa M, et al. Overexpression of optineurin E50K disrupts Rab8 interaction and leads to a progressive retinal degeneration in mice. Hum Mol Genet. 2010;19(13):2606–15. https://doi.org/10.1093/hmg/ddq146
   PubMed Web of Science ®Google Scholar
• Hagemann N, Hou X, Goody RS, et al. Crystal structure of the Rab binding domain of OCRL1 in complex with Rab8 and functional implications of the OCRL1/Rab8 module for Lowe syndrome. Small GTPases. 2012;3(2):107–10. https://doi.org/10.4161/sgtp.19380
   PubMedGoogle Scholar
• Huber LA, Pimplikar S, Parton RG, et al. Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol. 1993;123(1):35–45. https://doi.org/10.1083/jcb.123.1.35
   PubMed Web of Science ®Google Scholar
• Kim MJ, Deng HX, Wong YC, et al. The Parkinson's disease-linked protein TMEM230 is required for Rab8a-mediated secretory vesicle trafficking and retromer trafficking. Hum Mol Genet. 2017;26(4):729–41.
   PubMed Web of Science ®Google Scholar
• Lai YC, Kondapalli C, Lehneck R, et al. Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J. 2015;34(22):2840–61. https://doi.org/10.15252/embj.201591593
   PubMed Web of Science ®Google Scholar
• Ao X, Zou L, Wu Y. Regulation of autophagy by the Rab GTPase network. Cell Death Differ. 2014;21(3):348–58. https://doi.org/10.1038/cdd.2013.187
   PubMed Web of Science ®Google Scholar
• Goncalves SA, Outeiro TF. Traffic jams and the complex role of alpha-Synuclein aggregation in Parkinson disease. Small GTPases. 2017;8(2):78–84. https://doi.org/10.1080/21541248.2016.1199191
   PubMedGoogle Scholar
• Heidrych P, Zimmermann U, Bress A, et al. Rab8b GTPase, a protein transport regulator, is an interacting partner of otoferlin, defective in a human autosomal recessive deafness form. Hum Mol Genet. 2008;17(23):3814–21. https://doi.org/10.1093/hmg/ddn279
   PubMed Web of Science ®Google Scholar
• Kobayashi S, Suzuki T, Kawaguchi A, et al. Rab8b Regulates Transport of West Nile Virus Particles from Recycling Endosomes. J Biol Chem. 2016;291(12):6559–68. https://doi.org/10.1074/jbc.M115.712760
   PubMed Web of Science ®Google Scholar
• Sato T, Iwano T, Kunii M, et al. Rab8a and Rab8b are essential for several apical transport pathways but insufficient for ciliogenesis. J Cell Sci. 2014;127(Pt 2):422–31. https://doi.org/10.1242/jcs.136903
   PubMed Web of Science ®Google Scholar
• Ganley IG, Pfeffer SR. Cholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cells. J Biol Chem. 2006;281(26):17890–9. https://doi.org/10.1074/jbc.M601679200
   PubMed Web of Science ®Google Scholar
• Hirota Y, Yamashita S, Kurihara Y, et al. Mitophagy is primarily due to alternative autophagy and requires the MAPK1 and MAPK14 signaling pathways. Autophagy. 2015;11(2):332–43. https://doi.org/10.1080/15548627.2015.1023047
   PubMed Web of Science ®Google Scholar
• Kaptzan T, West SA, Holicky EL, et al. Development of a Rab9 transgenic mouse and its ability to increase the lifespan of a murine model of Niemann-Pick type C disease. Am J Pathol. 2009;174(1):14–20. https://doi.org/10.2353/ajpath.2009.080660
   PubMed Web of Science ®Google Scholar
• Lombardi D, Soldati T, Riederer MA, et al. Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J. 1993;12(2):677–82.
   PubMed Web of Science ®Google Scholar
• Murray JL, Mavrakis M, McDonald NJ, et al. Rab9 GTPase is required for replication of human immunodeficiency virus type 1, filoviruses, and measles virus. J Virol. 2005;79(18):11742–51. https://doi.org/10.1128/JVI.79.18.11742-11751.2005
   PubMed Web of Science ®Google Scholar
• Seki N, Azuma T, Yoshikawa T, et al. cDNA cloning of a new member of the Ras superfamily, RAB9-like, on the human chromosome Xq22.1-q22.3 region. J Hum Genet. 2000;45(5):318–22. https://doi.org/10.1007/s100380070025
   PubMed Web of Science ®Google Scholar
• Bruno J, Brumfield A, Chaudhary N, et al. SEC16A is a RAB10 effector required for insulin-stimulated GLUT4 trafficking in adipocytes. J Cell Biol. 2016;214(1):61–76. https://doi.org/10.1083/jcb.201509052
   PubMed Web of Science ®Google Scholar
• Isabella AJ, Horne-Badovinac S. Rab10-Mediated Secretion Synergizes with Tissue Movement to Build a Polarized Basement Membrane Architecture for Organ Morphogenesis. Dev Cell. 2016;38(1):47–60. https://doi.org/10.1016/j.devcel.2016.06.009
   PubMed Web of Science ®Google Scholar
• Jiang W, Liu J, Xu T, et al. MiR-329 suppresses osteosarcoma development by downregulating Rab10. FEBS Lett. 2016;590(17):2973–81. https://doi.org/10.1002/1873-3468.12337
   PubMed Web of Science ®Google Scholar
• Li Z, Schulze RJ, Weller SG, et al. A novel Rab10-EHBP1-EHD2 complex essential for the autophagic engulfment of lipid droplets. Sci Adv. 2016;2(12):e1601470. https://doi.org/10.1126/sciadv.1601470
   PubMed Web of Science ®Google Scholar
• Sano H, Eguez L, Teruel MN, et al. Rab10, a target of the AS160 Rab GAP, is required for insulin-stimulated translocation of GLUT4 to the adipocyte plasma membrane. Cell Metab. 2007;5(4):293–303. https://doi.org/10.1016/j.cmet.2007.03.001
   PubMed Web of Science ®Google Scholar
• Vazirani RP, Verma A, Sadacca LA, et al. Disruption of Adipose Rab10-Dependent Insulin Signaling Causes Hepatic Insulin Resistance. Diabetes. 2016;65(6):1577–89. https://doi.org/10.2337/db15-1128
   PubMed Web of Science ®Google Scholar
• Bruce EA, Digard P, Stuart AD. The Rab11 pathway is required for influenza A virus budding and filament formation. J Virol. 2010;84(12):5848–59. https://doi.org/10.1128/JVI.00307-10
   PubMed Web of Science ®Google Scholar
• Kelly EE, Horgan CP, McCaffrey MW. Rab11 proteins in health and disease. Biochem Soc Trans. 2012;40(6):1360–7. https://doi.org/10.1042/BST20120157
   PubMed Web of Science ®Google Scholar
• Li J, Kanekiyo T, Shinohara M, et al. Differential regulation of amyloid-beta endocytic trafficking and lysosomal degradation by apolipoprotein E isoforms. J Biol Chem. 2012;287(53):44593–601. https://doi.org/10.1074/jbc.M112.420224
   PubMed Web of Science ®Google Scholar
• Li X, Valencia A, Sapp E, et al. Aberrant Rab11-dependent trafficking of the neuronal glutamate transporter EAAC1 causes oxidative stress and cell death in Huntington's disease. J Neurosci. 2010;30(13):4552–61. https://doi.org/10.1523/JNEUROSCI.5865-09.2010
   PubMed Web of Science ®Google Scholar
• Roberts RC, Peden AA, Buss F, et al. Mistargeting of SH3TC2 away from the recycling endosome causes Charcot-Marie-Tooth disease type 4C. Hum Mol Genet. 2010;19(6):1009–18. https://doi.org/10.1093/hmg/ddp565
   PubMed Web of Science ®Google Scholar
• Rzomp KA, Scholtes LD, Briggs BJ, et al. Rab GTPases are recruited to chlamydial inclusions in both a species-dependent and species-independent manner. Infect Immun. 2003;71(10):5855–70. https://doi.org/10.1128/IAI.71.10.5855-5870.2003
   PubMed Web of Science ®Google Scholar
• Ullrich O, Reinsch S, Urbe S, et al. Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol. 1996;135(4):913–24. https://doi.org/10.1083/jcb.135.4.913
   PubMed Web of Science ®Google Scholar
• Grimsey NJ, Coronel LJ, Cordova IC, et al. Recycling and Endosomal Sorting of Protease-activated Receptor-1 Is Distinctly Regulated by Rab11A and Rab11B Proteins. J Biol Chem. 2016;291(5):2223–36. https://doi.org/10.1074/jbc.M115.702993
   PubMed Web of Science ®Google Scholar
• Tarafder AK, Bolasco G, Correia MS, et al. Rab11b mediates melanin transfer between donor melanocytes and acceptor keratinocytes via coupled exo/endocytosis. J Invest Dermatol. 2014;134(4):1056–66. https://doi.org/10.1038/jid.2013.432
   PubMed Web of Science ®Google Scholar
• Efergan A, Azouz NP, Klein O, et al. Rab12 Regulates Retrograde Transport of Mast Cell Secretory Granules by Interacting with the RILP-Dynein Complex. J Immunol. 2016;196(3):1091–101. https://doi.org/10.4049/jimmunol.1500731
   PubMed Web of Science ®Google Scholar
• Matsui T, Fukuda M. Small GTPase Rab12 regulates transferrin receptor degradation: Implications for a novel membrane trafficking pathway from recycling endosomes to lysosomes. Cell Logist. 2011;1(4):155–8. https://doi.org/10.4161/cl.1.4.18152
   PubMedGoogle Scholar
• Xu J, Fotouhi M, McPherson PS. Phosphorylation of the exchange factor DENND3 by ULK in response to starvation activates Rab12 and induces autophagy. EMBO Rep. 2015;16(6):709–18. https://doi.org/10.15252/embr.201440006
   PubMed Web of Science ®Google Scholar
• Yoshida T, Kobayashi T, Itoda M, et al. Clinical omics analysis of colorectal cancer incorporating copy number aberrations and gene expression data. Cancer Inform. 2010;9:147–61. https://doi.org/10.4137/CIN.S3851
   PubMedGoogle Scholar
• Ioannou MS, McPherson PS. Regulation of Cancer Cell Behavior by the Small GTPase Rab13. J Biol Chem. 2016;291(19):9929–37. https://doi.org/10.1074/jbc.R116.715193
   PubMed Web of Science ®Google Scholar
• Morimoto S, Nishimura N, Terai T, et al. Rab13 mediates the continuous endocytic recycling of occludin to the cell surface. J Biol Chem. 2005;280(3):2220–8. https://doi.org/10.1074/jbc.M406906200
   PubMed Web of Science ®Google Scholar
• Nokes RL, Fields IC, Collins RN, et al. Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells. J Cell Biol. 2008;182(5):845–53. https://doi.org/10.1083/jcb.200802176
   PubMed Web of Science ®Google Scholar
• Ohira M, Oshitani N, Hosomi S, et al. Dislocation of Rab13 and vasodilator-stimulated phosphoprotein in inactive colon epithelium in patients with Crohn's disease. Int J Mol Med. 2009;24(6):829–35.
   PubMed Web of Science ®Google Scholar
• Zahraoui A, Joberty G, Arpin M, et al. A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells. J Cell Biol. 1994;124(1-2):101–15. https://doi.org/10.1083/jcb.124.1.101
   PubMed Web of Science ®Google Scholar
• Brewer PD, Habtemichael EN, Romenskaia I, et al. Rab14 limits the sorting of Glut4 from endosomes into insulin-sensitive regulated secretory compartments in adipocytes. Biochem J. 2016;473(10):1315–27. https://doi.org/10.1042/BCJ20160020
   PubMedGoogle Scholar
• Guo B, Wang W, Zhao Z, et al. Rab14 Act as Oncogene and Induce Proliferation of Gastric Cancer Cells via AKT Signaling Pathway. PLoS One. 2017;12(1):e0170620. https://doi.org/10.1371/journal.pone.0170620
   PubMed Web of Science ®Google Scholar
• Junutula JR, De Maziere AM, Peden AA, et al. Rab14 is involved in membrane trafficking between the Golgi complex and endosomes. Mol Biol Cell. 2004;15(5):2218–29. https://doi.org/10.1091/mbc.E03-10-0777
   PubMed Web of Science ®Google Scholar
• Kim EA, Kim TG, Sung EG, et al. miR-148a increases the sensitivity to cisplatin by targeting Rab14 in renal cancer cells. Int J Oncol. 2017;50(3):984–92. https://doi.org/10.3892/ijo.2017.3851
   PubMed Web of Science ®Google Scholar
• Linford A, Yoshimura S, Nunes Bastos R, et al. Rab14 and its exchange factor FAM116 link endocytic recycling and adherens junction stability in migrating cells. Dev Cell. 2012;22(5):952–66. https://doi.org/10.1016/j.devcel.2012.04.010
   PubMed Web of Science ®Google Scholar
• Lu R, Johnson DL, Stewart L, et al. Rab14 regulation of claudin-2 trafficking modulates epithelial permeability and lumen morphogenesis. Mol Biol Cell. 2014;25(11):1744–54. https://doi.org/10.1091/mbc.E13-12-0724
   PubMed Web of Science ®Google Scholar
• Yu J, Wang L, Yang H, et al. Rab14 Suppression Mediated by MiR-320a Inhibits Cell Proliferation, Migration and Invasion in Breast Cancer. J Cancer. 2016;7(15):2317–26. https://doi.org/10.7150/jca.15737
   PubMed Web of Science ®Google Scholar
• Nishimura N, Van Huyen Pham T, Hartomo TB, et al. Rab15 expression correlates with retinoic acid-induced differentiation of neuroblastoma cells. Oncol Rep. 2011;26(1):145–51.
   PubMed Web of Science ®Google Scholar
• Strick DJ, Elferink LA. Rab15 effector protein: a novel protein for receptor recycling from the endocytic recycling compartment. Mol Biol Cell. 2005;16(12):5699–709. https://doi.org/10.1091/mbc.E05-03-0204
   PubMed Web of Science ®Google Scholar
• Zuk PA, Elferink LA. Rab15 differentially regulates early endocytic trafficking. J Biol Chem. 2000;275(35):26754–64.
   PubMed Web of Science ®Google Scholar
• Beaumont KA, Hamilton NA, Moores MT, et al. The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking. Traffic. 2011;12(5):627–43. https://doi.org/10.1111/j.1600-0854.2011.01172.x
   PubMed Web of Science ®Google Scholar
• Haobam B, Nozawa T, Minowa-Nozawa A, et al. Rab17-mediated recycling endosomes contribute to autophagosome formation in response to Group A Streptococcus invasion. Cell Microbiol. 2014;16(12):1806–21. https://doi.org/10.1111/cmi.12329
   PubMed Web of Science ®Google Scholar
• Hunziker W, Peters PJ. Rab17 localizes to recycling endosomes and regulates receptor-mediated transcytosis in epithelial cells. J Biol Chem. 1998;273(25):15734–41. https://doi.org/10.1074/jbc.273.25.15734
   PubMed Web of Science ®Google Scholar
• Mori Y, Fukuda M, Henley JM. Small GTPase Rab17 regulates the surface expression of kainate receptors but not alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors in hippocampal neurons via dendritic trafficking of Syntaxin-4 protein. J Biol Chem. 2014;289(30):20773–87. https://doi.org/10.1074/jbc.M114.550632
   PubMed Web of Science ®Google Scholar
• von Thun A, Birtwistle M, Kalna G, et al. ERK2 drives tumour cell migration in three-dimensional microenvironments by suppressing expression of Rab17 and liprin-beta2. J Cell Sci. 2012;125(Pt 6):1465–77.
   PubMed Web of Science ®Google Scholar
• Wang K, Mao Z, Liu L, et al. Rab17 inhibits the tumourigenic properties of hepatocellular carcinomas via the Erk pathway. Tumour Biol. 2015;36(8):5815–24. https://doi.org/10.1007/s13277-015-3251-3
   PubMedGoogle Scholar
• Zacchi P, Stenmark H, Parton RG, et al. Rab17 regulates membrane trafficking through apical recycling endosomes in polarized epithelial cells. J Cell Biol. 1998;140(5):1039–53. https://doi.org/10.1083/jcb.140.5.1039
   PubMed Web of Science ®Google Scholar
• Feldmann A, Bekbulat F, Huesmann H, et al. The RAB GTPase RAB18 modulates macroautophagy and proteostasis. Biochem Biophys Res Commun. 2017;486(3):738–43. https://doi.org/10.1016/j.bbrc.2017.03.112
   PubMed Web of Science ®Google Scholar
• Li C, Luo X, Zhao S, et al. COPI-TRAPPII activates Rab18 and regulates its lipid droplet association. EMBO J. 2017;36(4):441–57. https://doi.org/10.15252/embj.201694866
   PubMed Web of Science ®Google Scholar
• Martin S, Driessen K, Nixon SJ, et al. Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism. J Biol Chem. 2005;280(51):42325–35. https://doi.org/10.1074/jbc.M506651200
   PubMed Web of Science ®Google Scholar
• You X, Liu F, Zhang T, et al. Hepatitis B virus X protein upregulates oncogene Rab18 to result in the dysregulation of lipogenesis and proliferation of hepatoma cells. Carcinogenesis. 2013;34(7):1644–52. https://doi.org/10.1093/carcin/bgt089
   PubMed Web of Science ®Google Scholar
• Zhong K, Chen K, Han L, et al. MicroRNA-30b/c inhibits non-small cell lung cancer cell proliferation by targeting Rab18. BMC Cancer. 2014;14:703. https://doi.org/10.1186/1471-2407-14-703
   PubMed Web of Science ®Google Scholar
• Gillingham AK, Sinka R, Torres IL, et al. Toward a comprehensive map of the effectors of rab GTPases. Dev Cell. 2014;31(3):358–73. https://doi.org/10.1016/j.devcel.2014.10.007
   PubMed Web of Science ®Google Scholar
• Amillet JM, Ferbus D, Real FX, et al. Characterization of human Rab20 overexpressed in exocrine pancreatic carcinoma. Hum Pathol. 2006;37(3):256–63. https://doi.org/10.1016/j.humpath.2005.10.017
   PubMed Web of Science ®Google Scholar
• Egami Y, Araki N. Rab20 regulates phagosome maturation in RAW264 macrophages during Fc gamma receptor-mediated phagocytosis. PLoS One. 2012;7(4):e35663. https://doi.org/10.1371/journal.pone.0035663
   PubMed Web of Science ®Google Scholar
• Ho JR, Chapeaublanc E, Kirkwood L, et al. Deregulation of Rab and Rab effector genes in bladder cancer. PLoS One. 2012;7(6):e39469. https://doi.org/10.1371/journal.pone.0039469
   PubMed Web of Science ®Google Scholar
• Pei G, Schnettger L, Bronietzki M, et al. Interferon-gamma-inducible Rab20 regulates endosomal morphology and EGFR degradation in macrophages. Mol Biol Cell. 2015;26(17):3061–70. https://doi.org/10.1091/mbc.E14-11-1547
   PubMed Web of Science ®Google Scholar
• Seto S, Tsujimura K, Koide Y. Rab GTPases regulating phagosome maturation are differentially recruited to mycobacterial phagosomes. Traffic. 2011;12(4):407–20. https://doi.org/10.1111/j.1600-0854.2011.01165.x
   PubMed Web of Science ®Google Scholar
• Hognas G, Tuomi S, Veltel S, et al. Cytokinesis failure due to derailed integrin traffic induces aneuploidy and oncogenic transformation in vitro and in vivo. Oncogene. 2012;31(31):3597–606. https://doi.org/10.1038/onc.2011.527
   PubMed Web of Science ®Google Scholar
• Simpson JC, Griffiths G, Wessling-Resnick M, et al. A role for the small GTPase Rab21 in the early endocytic pathway. J Cell Sci. 2004;117(Pt 26):6297–311. https://doi.org/10.1242/jcs.01560
   PubMed Web of Science ®Google Scholar
• Kauppi M, Simonsen A, Bremnes B, et al. The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking. J Cell Sci. 2002;115(Pt 5):899–911.
   PubMed Web of Science ®Google Scholar
• Mesa R, Salomon C, Roggero M, et al. Rab22a affects the morphology and function of the endocytic pathway. J Cell Sci. 2001;114(Pt 22):4041–9.
   PubMed Web of Science ®Google Scholar
• Su F, Chen Y, Zhu S, et al. RAB22A overexpression promotes the tumor growth of melanoma. Oncotarget. 2016;7(44):71744–53. https://doi.org/10.18632/oncotarget.12329
   PubMed Web of Science ®Google Scholar
• Wang L, Liang Z, Li G. Rab22 controls NGF signaling and neurite outgrowth in PC12 cells. Mol Biol Cell. 2011;22(20):3853–60. https://doi.org/10.1091/mbc.E11-03-0277
   PubMed Web of Science ®Google Scholar
• Weigert R, Yeung AC, Li J, et al. Rab22a regulates the recycling of membrane proteins internalized independently of clathrin. Mol Biol Cell. 2004;15(8):3758–70. https://doi.org/10.1091/mbc.E04-04-0342
   PubMed Web of Science ®Google Scholar
• Yang D, Liu G, Wang K. miR-203 Acts as a Tumor Suppressor Gene in Osteosarcoma by Regulating RAB22A. PLoS One. 2015;10(9):e0132225. https://doi.org/10.1371/journal.pone.0132225
   PubMed Web of Science ®Google Scholar
• Yu H, Yang W. MiR-211 is epigenetically regulated by DNMT1 mediated methylation and inhibits EMT of melanoma cells by targeting RAB22A. Biochem Biophys Res Commun. 2016;476(4):400–5. https://doi.org/10.1016/j.bbrc.2016.05.133
   PubMed Web of Science ®Google Scholar
• Zhang Y, Zhao FJ, Chen LL, et al. MiR-373 targeting of the Rab22a oncogene suppresses tumor invasion and metastasis in ovarian cancer. Oncotarget. 2014;5(23):12291–303. https://doi.org/10.18632/oncotarget.2577
   PubMed Web of Science ®Google Scholar
• Chen Y, Ng F, Tang BL. Rab23 activities and human cancer-emerging connections and mechanisms. Tumour Biol. 2016;37(10):12959–67. https://doi.org/10.1007/s13277-016-5207-7
   PubMedGoogle Scholar
• Zheng LQ, Chi SM, Li CX. Rab23's genetic structure, function and related diseases: a review. Biosci Rep. 2017;37(2):https://doi.org/10.1042/BSR20160410
   Google Scholar
• Agler C, Nielsen DM, Urkasemsin G, et al. Canine hereditary ataxia in old english sheepdogs and gordon setters is associated with a defect in the autophagy gene encoding RAB24. PLoS Genet. 2014;10(2):e1003991. https://doi.org/10.1371/journal.pgen.1003991
   PubMed Web of Science ®Google Scholar
• Amaya C, Militello RD, Calligaris SD, et al. Rab24 interacts with the Rab7/Rab interacting lysosomal protein complex to regulate endosomal degradation. Traffic. 2016;17(11):1181–96. https://doi.org/10.1111/tra.12431
   PubMed Web of Science ®Google Scholar
• Igci M, Baysan M, Yigiter R, et al. Gene expression profiles of autophagy-related genes in multiple sclerosis. Gene. 2016;588(1):38–46. https://doi.org/10.1016/j.gene.2016.04.042
   PubMed Web of Science ®Google Scholar
• Jacobsen M, Repsilber D, Gutschmidt A, et al. Ras-associated small GTPase 33A, a novel T cell factor, is down-regulated in patients with tuberculosis. J Infect Dis. 2005;192(7):1211–8. https://doi.org/10.1086/444428
   PubMed Web of Science ®Google Scholar
• Munafo DB, Colombo MI. Induction of autophagy causes dramatic changes in the subcellular distribution of GFP-Rab24. Traffic. 2002;3(7):472–82. https://doi.org/10.1034/j.1600-0854.2002.30704.x
   PubMed Web of Science ®Google Scholar
• Olkkonen VM, Dupree P, Killisch I, et al. Molecular cloning and subcellular localization of three GTP-binding proteins of the rab subfamily. J Cell Sci. 1993;106(Pt 4):1249–61.
   PubMedGoogle Scholar
• Yla-Anttila P, Eskelinen EL. Roles for RAB24 in autophagy and disease. Small GTPases. 2017;1–9. https://doi.org/10.1080/21541248.2017.1317699
   PubMedGoogle Scholar
• Yla-Anttila P, Mikkonen E, Happonen KE, et al. RAB24 facilitates clearance of autophagic compartments during basal conditions. Autophagy. 2015;11(10):1833–48. https://doi.org/10.1080/15548627.2015.1086522
   PubMed Web of Science ®Google Scholar
• Binotti B, Pavlos NJ, Riedel D, et al. The GTPase Rab26 links synaptic vesicles to the autophagy pathway. Elife. 2015;4:e05597. https://doi.org/10.7554/eLife.05597
   PubMed Web of Science ®Google Scholar
• Jin RU, Mills JC. RAB26 coordinates lysosome traffic and mitochondrial localization. J Cell Sci. 2014;127(Pt 5):1018–32. https://doi.org/10.1242/jcs.138776
   PubMed Web of Science ®Google Scholar
• Yoshie S, Imai A, Nashida T, et al. Expression, characterization, and localization of Rab26, a low molecular weight GTP-binding protein, in the rat parotid gland. Histochem Cell Biol. 2000;113(4):259–63. https://doi.org/10.1007/s004180000130
   PubMed Web of Science ®Google Scholar
• Chang C, Liu T, Huang Y, et al. MicroRNA-134-3p is a novel potential inhibitor of human ovarian cancer stem cells by targeting RAB27A. Gene. 2017;605:99–107. https://doi.org/10.1016/j.gene.2016.12.030
   PubMed Web of Science ®Google Scholar
• Haddad EK, Wu X, Hammer JA, 3rd, et al. Defective granule exocytosis in Rab27a-deficient lymphocytes from Ashen mice. J Cell Biol. 2001;152(4):835–42. https://doi.org/10.1083/jcb.152.4.835
   PubMed Web of Science ®Google Scholar
• Li Y, Chen S, Shan Z, et al. miR-182-5p improves the viability, mitosis, migration, and invasion ability of human gastric cancer cells by down-regulating RAB27A. Biosci Rep. 2017;37(3):https://doi.org/10.1042/BSR20170136
   Google Scholar
• Wang Q, Ni Q, Wang X, et al. High expression of RAB27A and TP53 in pancreatic cancer predicts poor survival. Med Oncol. 2015;32(1):372. https://doi.org/10.1007/s12032-014-0372-2
   PubMed Web of Science ®Google Scholar
• Worst TS, Meyer Y, Gottschalt M, et al. RAB27A, RAB27B and VPS36 are downregulated in advanced prostate cancer and show functional relevance in prostate cancer cells. Int J Oncol. 2017;50(3):920–32. https://doi.org/10.3892/ijo.2017.3872
   PubMed Web of Science ®Google Scholar
• Wu X, Rao K, Bowers MB, et al. Rab27a enables myosin Va-dependent melanosome capture by recruiting the myosin to the organelle. J Cell Sci. 2001;114(Pt 6):1091–100.
   PubMed Web of Science ®Google Scholar
• Zhang X, Zhang Y, Yang J, et al. Upregulation of miR-582-5p inhibits cell proliferation, cell cycle progression and invasion by targeting Rab27a in human colorectal carcinoma. Cancer Gene Ther. 2015;22(10):475–80. https://doi.org/10.1038/cgt.2015.44
   PubMed Web of Science ®Google Scholar
• Chen Y, Samaraweera P, Sun TT, et al. Rab27b association with melanosomes: dominant negative mutants disrupt melanosomal movement. J Invest Dermatol. 2002;118(6):933–40. https://doi.org/10.1046/j.1523-1747.2002.01754.x
   PubMed Web of Science ®Google Scholar
• Huang D, Bian G, Pan Y, et al. MiR-20a-5p promotes radio-resistance by targeting Rab27B in nasopharyngeal cancer cells. Cancer Cell Int. 2017;17:32. https://doi.org/10.1186/s12935-017-0389-7
   PubMed Web of Science ®Google Scholar
• Munoz I, Danelli L, Claver J, et al. Kinesin-1 controls mast cell degranulation and anaphylaxis through PI3K-dependent recruitment to the granular Slp3/Rab27b complex. J Cell Biol. 2016;215(2):203–16. https://doi.org/10.1083/jcb.201605073
   PubMed Web of Science ®Google Scholar
• Ren P, Yang XQ, Zhai XL, et al. Overexpression of Rab27B is correlated with distant metastasis and poor prognosis in ovarian cancer. Oncol Lett. 2016;12(2):1539–45.
   PubMed Web of Science ®Google Scholar
• Shen YT, Gu Y, Su WF, et al. Rab27b is Involved in Lysosomal Exocytosis and Proteolipid Protein Trafficking in Oligodendrocytes. Neurosci Bull. 2016;32(4):331–40. https://doi.org/10.1007/s12264-016-0045-6
   PubMed Web of Science ®Google Scholar
• Zhao H, Wang Q, Wang X, et al. Correlation Between RAB27B and p53 Expression and Overall Survival in Pancreatic Cancer. Pancreas. 2016;45(2):204–10. https://doi.org/10.1097/MPA.0000000000000453
   PubMed Web of Science ®Google Scholar
• Jensen VL, Carter S, Sanders AA, et al. Whole-Organism Developmental Expression Profiling Identifies RAB-28 as a Novel Ciliary GTPase Associated with the BBSome and Intraflagellar Transport. PLoS Genet. 2016;12(12):e1006469. https://doi.org/10.1371/journal.pgen.1006469
   PubMed Web of Science ®Google Scholar
• Roosing S, Rohrschneider K, Beryozkin A, et al. Mutations in RAB28, encoding a farnesylated small GTPase, are associated with autosomal-recessive cone-rod dystrophy. Am J Hum Genet. 2013;93(1):110–7. https://doi.org/10.1016/j.ajhg.2013.05.005
   PubMed Web of Science ®Google Scholar
• Aoki Y, Manzano R, Lee Y, et al. C9orf72 and RAB7L1 regulate vesicle trafficking in amyotrophic lateral sclerosis and frontotemporal dementia. Brain. 2017;140(4):887–97. https://doi.org/10.1093/brain/awx024
   PubMedGoogle Scholar
• Guo XY, Chen YP, Song W, et al. An association analysis of the rs1572931 polymorphism of the RAB7L1 gene in Parkinson's disease, amyotrophic lateral sclerosis and multiple system atrophy in China. Eur J Neurol. 2014;21(10):1337–43. https://doi.org/10.1111/ene.12490
   PubMed Web of Science ®Google Scholar
• Khaligh A, Goudarzian M, Moslem A, et al. RAB7L1 promoter polymorphism and risk of Parkinson's disease; a case-control study. Neurol Res. 2017;39(5):468–71. https://doi.org/10.1080/01616412.2017.1297558
   PubMed Web of Science ®Google Scholar
• Onnis A, Finetti F, Patrussi L, et al. The small GTPase Rab29 is a common regulator of immune synapse assembly and ciliogenesis. Cell Death Differ. 2015;22(10):1687–99. https://doi.org/10.1038/cdd.2015.17
   PubMed Web of Science ®Google Scholar
• Spano S, Liu X, Galan JE. Proteolytic targeting of Rab29 by an effector protein distinguishes the intracellular compartments of human-adapted and broad-host Salmonella. Proc Natl Acad Sci U S A. 2011;108(45):18418–23. https://doi.org/10.1073/pnas.1111959108
   PubMed Web of Science ®Google Scholar
• Wang S, Ma Z, Xu X, et al. A role of Rab29 in the integrity of the trans-Golgi network and retrograde trafficking of mannose-6-phosphate receptor. PLoS One. 2014;9(5):e96242. https://doi.org/10.1371/journal.pone.0096242
   PubMed Web of Science ®Google Scholar
• Kelly EE, Giordano F, Horgan CP, et al. Rab30 is required for the morphological integrity of the Golgi apparatus. Biol Cell. 2012;104(2):84–101. https://doi.org/10.1111/boc.201100080
   PubMed Web of Science ®Google Scholar
• Oda S, Nozawa T, Nozawa-Minowa A, et al. Golgi-Resident GTPase Rab30 Promotes the Biogenesis of Pathogen-Containing Autophagosomes. PLoS One. 2016;11(1):e0147061. https://doi.org/10.1371/journal.pone.0147061
   PubMed Web of Science ®Google Scholar
• Bultema JJ, Boyle JA, Malenke PB, et al. Myosin vc interacts with Rab32 and Rab38 proteins and works in the biogenesis and secretion of melanosomes. J Biol Chem. 2014;289(48):33513–28. https://doi.org/10.1074/jbc.M114.578948
   PubMed Web of Science ®Google Scholar
• Gerondopoulos A, Langemeyer L, Liang JR, et al. BLOC-3 mutated in Hermansky-Pudlak syndrome is a Rab32/38 guanine nucleotide exchange factor. Curr Biol. 2012;22(22):2135–9. https://doi.org/10.1016/j.cub.2012.09.020
   PubMed Web of Science ®Google Scholar
• Li Q, Wang J, Wan Y, et al. Depletion of Rab32 decreases intracellular lipid accumulation and induces lipolysis through enhancing ATGL expression in hepatocytes. Biochem Biophys Res Commun. 2016;471(4):492–6. https://doi.org/10.1016/j.bbrc.2016.02.047
   PubMed Web of Science ®Google Scholar
• Li Y, Wang Y, Zou L, et al. Analysis of the Rab GTPase Interactome in Dendritic Cells Reveals Anti-microbial Functions of the Rab32 Complex in Bacterial Containment. Immunity. 2016;44(2):422–37. https://doi.org/10.1016/j.immuni.2016.01.027
   PubMed Web of Science ®Google Scholar
• Niyogi S, Jimenez V, Girard-Dias W, et al. Rab32 is essential for maintaining functional acidocalcisomes, and for growth and infectivity of Trypanosoma cruzi. J Cell Sci. 2015;128(12):2363–73. https://doi.org/10.1242/jcs.169466
   PubMed Web of Science ®Google Scholar
• Pham TM, Tran SC, Lim YS, et al. Hepatitis C Virus-Induced Rab32 Aggregation and Its Implications for Virion Assembly. J Virol. 2017;91(3):https://doi.org/10.1128/JVI.01662-16
   Web of Science ®Google Scholar
• Solano-Collado V, Rofe A, Spano S. Rab32 restriction of intracellular bacterial pathogens. Small GTPases. 2016;1–8. https://doi.org/10.1080/21541248.2016.1219207
   PubMedGoogle Scholar
• Spano S. Host restriction in Salmonella: insights from Rab GTPases. Cell Microbiol. 2014;16(9):1321–8. https://doi.org/10.1111/cmi.12327
   PubMed Web of Science ®Google Scholar
• Wasmeier C, Romao M, Plowright L, et al. Rab38 and Rab32 control post-Golgi trafficking of melanogenic enzymes. J Cell Biol. 2006;175(2):271–81. https://doi.org/10.1083/jcb.200606050
   PubMed Web of Science ®Google Scholar
• Zhang F, Liu H, Chen S, et al. Identification of two new loci at IL23R and RAB32 that influence susceptibility to leprosy. Nat Genet. 2011;43(12):1247–51. https://doi.org/10.1038/ng.973
   PubMed Web of Science ®Google Scholar
• Imai A, Tsujimura M, Yoshie S, et al. The small GTPase Rab33A participates in regulation of amylase release from parotid acinar cells. Biochem Biophys Res Commun. 2015;461(3):469–74. https://doi.org/10.1016/j.bbrc.2015.04.022
   PubMed Web of Science ®Google Scholar
• Moller RS, Jensen LR, Maas SM, et al. X-linked congenital ptosis and associated intellectual disability, short stature, microcephaly, cleft palate, digital and genital abnormalities define novel Xq25q26 duplication syndrome. Hum Genet. 2014;133(5):625–38. https://doi.org/10.1007/s00439-013-1403-3
   PubMed Web of Science ®Google Scholar
• Nakazawa H, Sada T, Toriyama M, et al. Rab33a mediates anterograde vesicular transport for membrane exocytosis and axon outgrowth. J Neurosci. 2012;32(37):12712–25. https://doi.org/10.1523/JNEUROSCI.0989-12.2012
   PubMed Web of Science ®Google Scholar
• Alshammari MJ, Al-Otaibi L, Alkuraya FS. Mutation in RAB33B, which encodes a regulator of retrograde Golgi transport, defines a second Dyggve–Melchior–Clausen locus. J Med Genet. 2012;49(7):455–61. https://doi.org/10.1136/jmedgenet-2011-100666
   PubMed Web of Science ®Google Scholar
• Doring T, Prange R. Rab33B and its autophagic Atg5/12/16L1 effector assist in hepatitis B virus naked capsid formation and release. Cell Microbiol. 2015;17(5):747–64. https://doi.org/10.1111/cmi.12398
   PubMed Web of Science ®Google Scholar
• Dupuis N, Lebon S, Kumar M, et al. A novel RAB33B mutation in Smith-McCort dysplasia. Hum Mutat. 2013;34(2):283–6. https://doi.org/10.1002/humu.22235
   PubMed Web of Science ®Google Scholar
• Itoh T, Fujita N, Kanno E, et al. Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol Biol Cell. 2008;19(7):2916–25. https://doi.org/10.1091/mbc.E07-12-1231
   PubMed Web of Science ®Google Scholar
• Itoh T, Kanno E, Uemura T, et al. OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J Cell Biol. 2011;192(5):839–53. https://doi.org/10.1083/jcb.201008107
   PubMed Web of Science ®Google Scholar
• Pusapati GV, Luchetti G, Pfeffer SR. Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase. J Biol Chem. 2012;287(50):42129–37. https://doi.org/10.1074/jbc.M112.414565
   PubMed Web of Science ®Google Scholar
• Salian S, Cho TJ, Phadke SR, et al. Additional three patients with Smith-McCort dysplasia due to novel RAB33B mutations. Am J Med Genet A. 2017;173(3):588–95. https://doi.org/10.1002/ajmg.a.38064
   PubMed Web of Science ®Google Scholar
• Starr T, Sun Y, Wilkins N, et al. Rab33b and Rab6 are functionally overlapping regulators of Golgi homeostasis and trafficking. Traffic. 2010;11(5):626–36. https://doi.org/10.1111/j.1600-0854.2010.01051.x
   PubMed Web of Science ®Google Scholar
• Zheng JY, Koda T, Fujiwara T, et al. A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae. J Cell Sci. 1998;111(Pt 8):1061–9.
   PubMedGoogle Scholar
• Goldenberg NM, Grinstein S, Silverman M. Golgi-bound Rab34 is a novel member of the secretory pathway. Mol Biol Cell. 2007;18(12):4762–71. https://doi.org/10.1091/mbc.E06-11-0991
   PubMed Web of Science ®Google Scholar
• Kasmapour B, Gronow A, Bleck CK, et al. Size-dependent mechanism of cargo sorting during lysosome-phagosome fusion is controlled by Rab34. Proc Natl Acad Sci U S A. 2012;109(50):20485–90. https://doi.org/10.1073/pnas.1206811109
   PubMed Web of Science ®Google Scholar
• Wang HJ, Gao Y, Chen L, et al. RAB34 was a progression- and prognosis-associated biomarker in gliomas. Tumour Biol. 2015;36(3):1573–8. https://doi.org/10.1007/s13277-014-2732-0
   PubMedGoogle Scholar
• Zougman A, Mann M, Wisniewski JR. Identification and characterization of a novel ubiquitous nucleolar protein ‘NARR’ encoded by a gene overlapping the rab34 oncogene. Nucleic Acids Res. 2011;39(16):7103–13. https://doi.org/10.1093/nar/gkr273
   PubMed Web of Science ®Google Scholar
• Chen L, Hu J, Yun Y, et al. Rab36 regulates the spatial distribution of late endosomes and lysosomes through a similar mechanism to Rab34. Mol Membr Biol. 2010;27(1):23–30. https://doi.org/10.3109/09687680903417470
   PubMed Web of Science ®Google Scholar
• Matsui T, Ohbayashi N, Fukuda M. The Rab interacting lysosomal protein (RILP) homology domain functions as a novel effector domain for small GTPase Rab36: Rab36 regulates retrograde melanosome transport in melanocytes. J Biol Chem. 2012;287(34):28619–31. https://doi.org/10.1074/jbc.M112.370544
   PubMed Web of Science ®Google Scholar
• Mori T, Fukuda Y, Kuroda H, et al. Cloning and characterization of a novel Rab-family gene, Rab36, within the region at 22q11.2 that is homozygously deleted in malignant rhabdoid tumors. Biochem Biophys Res Commun. 1999;254(3):594–600. https://doi.org/10.1006/bbrc.1998.9968
   PubMed Web of Science ®Google Scholar
• Ljubicic S, Bezzi P, Brajkovic S, et al. The GTPase Rab37 Participates in the Control of Insulin Exocytosis. PLoS One. 2013;8(6):e68255. https://doi.org/10.1371/journal.pone.0068255
   PubMed Web of Science ®Google Scholar
• Masuda ES, Luo Y, Young C, et al. Rab37 is a novel mast cell specific GTPase localized to secretory granules. FEBS Lett. 2000;470(1):61–4. https://doi.org/10.1016/S0014-5793(00)01288-6
   PubMed Web of Science ®Google Scholar
• Mori R, Ikematsu K, Kitaguchi T, et al. Release of TNF-alpha from macrophages is mediated by small GTPase Rab37. Eur J Immunol. 2011;41(11):3230–9. https://doi.org/10.1002/eji.201141640
   PubMed Web of Science ®Google Scholar
• Tsai CH, Cheng HC, Wang YS, et al. Small GTPase Rab37 targets tissue inhibitor of metalloproteinase 1 for exocytosis and thus suppresses tumour metastasis. Nat Commun. 2014;5:4804. https://doi.org/10.1038/ncomms5804
   PubMed Web of Science ®Google Scholar
• Xu X, Guan X, Tao H, et al. An association study on genetic polymorphisms of Rab37 gene with the risk of esophageal squamous cell carcinoma in a Chinese Han population. Int J Med Sci. 2013;10(3):235–42. https://doi.org/10.7150/ijms.5524
   PubMed Web of Science ®Google Scholar
• Di Pietro SM, Dell'Angelica EC. The cell biology of Hermansky-Pudlak syndrome: recent advances. Traffic. 2005;6(7):525–33. https://doi.org/10.1111/j.1600-0854.2005.00299.x
   PubMed Web of Science ®Google Scholar
• Osanai K, Higuchi J, Oikawa R, et al. Altered lung surfactant system in a Rab38-deficient rat model of Hermansky-Pudlak syndrome. Am J Physiol Lung Cell Mol Physiol. 2010;298(2):L243–51. https://doi.org/10.1152/ajplung.00242.2009
   PubMed Web of Science ®Google Scholar
• Becker CE, Creagh EM, O'Neill LA. Rab39a binds caspase-1 and is required for caspase-1-dependent interleukin-1beta secretion. J Biol Chem. 2009;284(50):34531–7. https://doi.org/10.1074/jbc.M109.046102
   PubMed Web of Science ®Google Scholar
• Chen T, Han Y, Yang M, et al. Rab39, a novel Golgi-associated Rab GTPase from human dendritic cells involved in cellular endocytosis. Biochem Biophys Res Commun. 2003;303(4):1114–20. https://doi.org/10.1016/S0006-291X(03)00482-0
   PubMed Web of Science ®Google Scholar
• Gambarte Tudela J, Capmany A, Romao M, et al. The late endocytic Rab39a GTPase regulates the interaction between multivesicular bodies and chlamydial inclusions. J Cell Sci. 2015;128(16):3068–81. https://doi.org/10.1242/jcs.170092
   PubMed Web of Science ®Google Scholar
• Seto S, Sugaya K, Tsujimura K, et al. Rab39a interacts with phosphatidylinositol 3-kinase and negatively regulates autophagy induced by lipopolysaccharide stimulation in macrophages. PLoS One. 2013;8(12):e83324. https://doi.org/10.1371/journal.pone.0083324
   PubMed Web of Science ®Google Scholar
• Cheng H, Ma Y, Ni X, et al. Isolation and characterization of a human novel RAB (RAB39B) gene. Cytogenet Genome Res. 2002;97(1-2):72–5. https://doi.org/10.1159/000064047
   PubMed Web of Science ®Google Scholar
• Corbier C, Sellier C. C9ORF72 is a GDP/GTP exchange factor for Rab8 and Rab39 and regulates autophagy. Small GTPases. 2016;1–6.
   Google Scholar
• Lesage S, Bras J, Cormier-Dequaire F, et al. Loss-of-function mutations in RAB39B are associated with typical early-onset Parkinson disease. Neurol Genet. 2015;1(1):e9. https://doi.org/10.1212/NXG.0000000000000009
   PubMedGoogle Scholar
• Tang BL. Rabs, Membrane Dynamics, and Parkinson's Disease. J Cell Physiol. 2017;232(7):1626–33. https://doi.org/10.1002/jcp.25713
   PubMed Web of Science ®Google Scholar
• Wilson GR, Sim JC, McLean C, et al. Mutations in RAB39B cause X-linked intellectual disability and early-onset Parkinson disease with alpha-synuclein pathology. Am J Hum Genet. 2014;95(6):729–35. https://doi.org/10.1016/j.ajhg.2014.10.015
   PubMed Web of Science ®Google Scholar
• Lee RH, Iioka H, Ohashi M, et al. XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway. EMBO J. 2007;26(15):3592–606. https://doi.org/10.1038/sj.emboj.7601781
   PubMed Web of Science ®Google Scholar
• Pereira-Leal JB, Seabra MC. The mammalian Rab family of small GTPases: definition of family and subfamily sequence motifs suggests a mechanism for functional specificity in the Ras superfamily. J Mol Biol. 2000;301(4):1077–87. https://doi.org/10.1006/jmbi.2000.4010
   PubMed Web of Science ®Google Scholar
• Bedoyan JK, Schaibley VM, Peng W, et al. Disruption of RAB40AL function leads to Martin–Probst syndrome, a rare X-linked multisystem neurodevelopmental human disorder. J Med Genet. 2012;49(5):332–40. https://doi.org/10.1136/jmedgenet-2011-100575
   PubMed Web of Science ®Google Scholar
• Oldak M, Ruszkowska E, Pollak A, et al. A note of caution on the diagnosis of Martin-Probst syndrome by the detection of the p.D59G mutation in the RAB40AL gene. Eur J Pediatr. 2015;174(5):693–6. https://doi.org/10.1007/s00431-014-2452-x
   PubMed Web of Science ®Google Scholar
• Jacob A, Jing J, Lee J, et al. Rab40b regulates trafficking of MMP2 and MMP9 during invadopodia formation and invasion of breast cancer cells. J Cell Sci. 2013;126(Pt 20):4647–58. https://doi.org/10.1242/jcs.126573
   PubMed Web of Science ®Google Scholar
• Jacob A, Linklater E, Bayless BA, et al. The role and regulation of Rab40b-Tks5 complex during invadopodia formation and cancer cell invasion. J Cell Sci. 2016;129(23):4341–53. https://doi.org/10.1242/jcs.193904
   PubMed Web of Science ®Google Scholar
• Li Y, Jia Q, Wang Y, et al. Rab40b upregulation correlates with the prognosis of gastric cancer by promoting migration, invasion, and metastasis. Med Oncol. 2015;32(4):126. https://doi.org/10.1007/s12032-015-0562-6
   PubMed Web of Science ®Google Scholar
• Rodriguez-Gabin AG, Almazan G, Larocca JN. Vesicle transport in oligodendrocytes: probable role of Rab40c protein. J Neurosci Res. 2004;76(6):758–70. https://doi.org/10.1002/jnr.20121
   PubMed Web of Science ®Google Scholar
• Tan R, Wang W, Wang S, et al. Small GTPase Rab40c associates with lipid droplets and modulates the biogenesis of lipid droplets. PLoS One. 2013;8(4):e63213. https://doi.org/10.1371/journal.pone.0063213
   PubMed Web of Science ®Google Scholar
• Yang Q, Jie Z, Cao H, et al. Low-level expression of let-7a in gastric cancer and its involvement in tumorigenesis by targeting RAB40C. Carcinogenesis. 2011;32(5):713–22. https://doi.org/10.1093/carcin/bgr035
   PubMed Web of Science ®Google Scholar
• Liu S, Hunt L, Storrie B. Rab41 is a novel regulator of Golgi apparatus organization that is needed for ER-to-Golgi trafficking and cell growth. PLoS One. 2013;8(8):e71886. https://doi.org/10.1371/journal.pone.0071886
   PubMed Web of Science ®Google Scholar
• Kohnke M, Delon C, Hastie ML, et al. Rab GTPase prenylation hierarchy and its potential role in choroideremia disease. PLoS One. 2013;8(12):e81758. https://doi.org/10.1371/journal.pone.0081758
   PubMed Web of Science ®Google Scholar
• Cox JV, Kansal R, Whitt MA. Rab43 regulates the sorting of a subset of membrane protein cargo through the medial Golgi. Mol Biol Cell. 2016;27(11):1834–44. https://doi.org/10.1091/mbc.E15-03-0123
   PubMed Web of Science ®Google Scholar
• Dejgaard SY, Murshid A, Erman A, et al. Rab18 and Rab43 have key roles in ER-Golgi trafficking. J Cell Sci. 2008;121(Pt 16):2768–81. https://doi.org/10.1242/jcs.021808
   PubMed Web of Science ®Google Scholar
• Haas AK, Yoshimura S, Stephens DJ, et al. Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J Cell Sci. 2007;120(Pt 17):2997–3010. https://doi.org/10.1242/jcs.014225
   PubMed Web of Science ®Google Scholar
• Han MZ, Huang B, Chen AJ, et al. High expression of RAB43 predicts poor prognosis and is associated with epithelial-mesenchymal transition in gliomas. Oncol Rep. 2017;37(2):903–12. https://doi.org/10.3892/or.2017.5349
   PubMed Web of Science ®Google Scholar
• Kretzer NM, Theisen DJ, Tussiwand R, et al. RAB43 facilitates cross-presentation of cell-associated antigens by CD8alpha+ dendritic cells. J Exp Med. 2016;213(13):2871–83. https://doi.org/10.1084/jem.20160597
   PubMed Web of Science ®Google Scholar
• Srikanth S, Woo JS, Gwack Y. A large Rab GTPase family in a small GTPase world. Small GTPases. 2017;8(1):43–8. https://doi.org/10.1080/21541248.2016.1192921
   PubMedGoogle Scholar
• Nakamura S, Takemura T, Tan L, et al. Small GTPase RAB45-mediated p38 activation in apoptosis of chronic myeloid leukemia progenitor cells. Carcinogenesis. 2011;32(12):1758–72. https://doi.org/10.1093/carcin/bgr205
   PubMed Web of Science ®Google Scholar
• Shintani M, Tada M, Kobayashi T, et al. Characterization of Rab45/RASEF containing EF-hand domain and a coiled-coil motif as a self-associating GTPase. Biochem Biophys Res Commun. 2007;357(3):661–7. https://doi.org/10.1016/j.bbrc.2007.03.206
   PubMed Web of Science ®Google Scholar
• Liew GM, Ye F, Nager AR, et al. The intraflagellar transport protein IFT27 promotes BBSome exit from cilia through the GTPase ARL6/BBS3. Dev Cell. 2014;31(3):265–78. https://doi.org/10.1016/j.devcel.2014.09.004
   PubMed Web of Science ®Google Scholar