Rab proteins as major determinants of the Golgi complex structure

References

• 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. doi:10.1074/jbc.M115.669242. PMID:26209634.
   PubMed Web of Science ®Google Scholar
• Allan BB, Moyer BD, Balch WE. Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COPII vesicles for fusion. Science. 2000;289(5478):444–8. doi:10.1126/science.289.5478.444. PMID:10903204.
   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. doi:10.1136/jmedgenet-2011-100666. PMID:22652534.
   PubMed Web of Science ®Google Scholar
• Alvarez C, Garcia-Mata R, Brandon E, Sztul E. COPI recruitment is modulated by a Rab1b-dependent mechanism. Mol Biol Cell. 2003;14(5):2116–27. doi:10.1091/mbc.E02-09-0625. PMID:12802079.
   PubMed Web of Science ®Google Scholar
• Bard F, Casano L, Mallabiabarrena A, Wallace E, Saito K, Kitayama H, Guizzunti G, Hu Y, Wendler F, Dasgupta R, et al. Functional genomics reveals genes involved in protein secretion and Golgi organization. Nature. 2006;439(7076):604–7. doi:10.1038/nature04377. PMID:16452979.
   PubMed Web of Science ®Google Scholar
• Bardin S, Miserey-Lenkei S, Hurbain I, Garcia-Castillo D, Raposo G, Goud B. Phenotypic characterisation of RAB6A knockout mouse embryonic fibroblasts. Biol Cell. 2015;107(12):427–39. doi:10.1111/boc.201400083. PMID:26304202.
   PubMed Web of Science ®Google Scholar
• Barnekow A, Thyrock A, Kessler D. Chapter 5: rab proteins and their interaction partners. Int Rev Cell Mol Biol. 2009;274:235–74. doi:10.1016/S1937-6448(08)02005-4. PMID:19349039.
   PubMed Web of Science ®Google Scholar
• Barr FA. A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr Biol. 1999;9(7):381–4. doi:10.1016/S0960-9822(99)80167-5. PMID:10209123.
   PubMed Web of Science ®Google Scholar
• Bhuin T, Roy JK. Rab proteins: the key regulators of intracellular vesicle transport. Exp Cell Res. 2014;328(1):1–19. doi:10.1016/j.yexcr.2014.07.027. PMID:25088255.
   PubMed Web of Science ®Google Scholar
• Burguete AS, Fenn TD, Brunger AT, Pfeffer SR. Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. Cell. 2008;132(2):286–98. doi:10.1016/j.cell.2007.11.048. PMID:18243103.
   PubMed Web of Science ®Google Scholar
• Cheung PY, Limouse C, Mabuchi H, Pfeffer SR. Protein flexibility is required for vesicle tethering at the Golgi. Elife. 2015;4:e12790. doi:10.7554/eLife.12790. PMID:26653856.
   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. doi:10.1091/mbc.E15-03-0123. PMID:27053659.
   PubMed Web of Science ®Google Scholar
• Cuif MH, Possmayer F, Zander H, Bordes N, Jollivet F, Couedel-Courteille A, Janoueix-Lerosey I, Langsley G, Bornens M, Goud B. Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome. EMBO J. 1999;18(7):1772–82. doi:10.1093/emboj/18.7.1772. PMID:10202141.
   PubMed Web of Science ®Google Scholar
• Dejgaard SY, Murshid A, Erman A, Kizilay O, Verbich D, Lodge R, Dejgaard K, Ly-Hartig TB, Pepperkok R, Simpson JC, et al. Rab18 and Rab43 have key roles in ER-Golgi trafficking. J Cell Sci. 2008;121(Pt 16):2768–81. doi:10.1242/jcs.021808. PMID:18664496.
   PubMed Web of Science ®Google Scholar
• Diao A, Rahman D, Pappin DJ, Lucocq J, Lowe M. The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J Cell Biol. 2003;160(2):201–12. doi:10.1083/jcb.200207045. PMID:12538640.
   PubMed Web of Science ®Google Scholar
• Distefano MB, Kjos I, Bakke O, Progida C. Rab7b at the intersection of intracellular trafficking and cell migration. Commun Integr Biol. 2015;8(6):e1023492. doi:10.1080/19420889.2015.1023492. PMID:27066171.
   PubMedGoogle 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. doi:10.1111/cmi.12398. PMID:25439980.
   PubMed Web of Science ®Google Scholar
• Dupuis N, Lebon S, Kumar M, Drunat S, Graul-Neumann LM, Gressens P, El Ghouzzi V. A novel RAB33B mutation in Smith-McCort dysplasia. Hum Mutat. 2013;34(2):283–6. doi:10.1002/humu.22235. PMID:23042644.
   PubMed Web of Science ®Google Scholar
• Echard A, Jollivet F, Martinez O, Lacapère JJ, Rousselet A, Janoueix-Lerosey I, Goud B. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science. 1998;279(5350):580–5. doi:10.1126/science.279.5350.580. PMID:9438855.
   PubMed Web of Science ®Google Scholar
• Echard A, Opdam FJ, de Leeuw HJ, Jollivet F, Savelkoul P, Hendriks W, Voorberg J, Goud B, Fransen JA. Alternative splicing of the human Rab6A gene generates two close but functionally different isoforms. Mol Biol Cell. 2000;11(11):3819–33. doi:10.1091/mbc.11.11.3819. PMID:11071909.
   PubMed Web of Science ®Google Scholar
• Fernandes H, Franklin E, Recacha R, Houdusse A, Goud B, Khan AR. Structural aspects of Rab6-effector complexes. Biochem Soc Trans. 2009;37(Pt 5):1037–41. doi:10.1042/BST0371037. PMID:19754447.
   PubMedGoogle Scholar
• Fridmann-Sirkis Y, Siniossoglou S, Pelham HR. TMF is a golgin that binds Rab6 and influences Golgi morphology. BMC Cell Biol. 2004;5:18. doi:10.1186/1471-2121-5-18. PMID:15128430.
   PubMed Web of Science ®Google Scholar
• Fuchs E, Haas, AK, Spooner RK, Yoshimura S, Lord JM, Barr FA. Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways. J Cell Biol. 2007;177:1133–43. doi:10.1083/jcb.200612068. PMID:17562788.
   PubMed Web of Science ®Google Scholar
• Fukuda M, Itoh T. Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals. Autophagy. 2008;4(6):824–6. doi:10.4161/auto.6542. PMID:18670194.
   PubMed Web of Science ®Google Scholar
• Galea G, Simpson JC. High-content analysis of Rab protein function at the ER-Golgi interface. Bioarchitecture. 2015;5(3–4):44–53. doi:10.1080/19490992.2015.1102826. PMID:26693811.
   PubMedGoogle Scholar
• Gerondopoulos A, Bastos RN, Yoshimura S, Anderson R, Carpanini S, Aligianis I, Handley MT, Barr FA. Rab18 and a Rab18 GEF complex are required for normal ER structure. J Cell Biol. 2014;205(5):707–20. doi:10.1083/jcb.201403026. PMID:24891604.
   PubMed Web of Science ®Google Scholar
• Giannandrea M, Bianchi V, Mignogna ML, Sirri A, Carrabino S, D'Elia E, Vecellio M, Russo S, Cogliati F, Larizza L, 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. doi:10.1016/j.ajhg.2010.01.011. PMID:20159109.
   PubMed Web of Science ®Google Scholar
• Gilchrist A, Au CE, Hiding J, Bell AW, Fernandez-Rodriguez J, Lesimple S, Nagaya H, Roy L, Gosline SJ, Hallett M, et al. Quantitative proteomics analysis of the secretory pathway. Cell. 2006;127(6):1265–81. doi:10.1016/j.cell.2006.10.036. PMID:17174899.
   PubMed Web of Science ®Google Scholar
• Goud B, Zahraoui A, Tavitian A, Saraste J. Small GTP-binding protein associated with Golgi cisternae. Nature. 1990;345(6275):553–6. doi:10.1038/345553a0. PMID:2112230.
   PubMed Web of Science ®Google Scholar
• Goud B, Akhmanova A. Rab6 GTPase. In: Guangpu L and Segev N, editors. Rab GTPases and membrane trafficking; 2012. p. 34–46. ebooks.benthamscience.com/.
   Google Scholar
• Grigoriev I, Splinter D, Keijzer N, Wulf PS, Demmers J, Ohtsuka T, Modesti M, Maly IV, Grosveld F, Hoogenraad CC, et al. Rab6 regulates transport and targeting of exocytotic carriers. Dev Cell. 2007;13(2):305–14. doi:10.1016/j.devcel.2007.06.010. PMID:17681140.
   PubMed Web of Science ®Google Scholar
• Haas AK, Yoshimura S, Stephens DJ, Preisinger C, Fuchs E, Barr FA. 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. doi:10.1242/jcs.014225. PMID:17684057.
   PubMed Web of Science ®Google Scholar
• Hayes GL, Brown FC, Haas AK, Nottingham RM, Barr FA, Pfeffer SR. Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi. Mol Biol Cell. 2009;20(1):209–17. doi:10.1091/mbc.E08-07-0740. PMID:18946081.
   PubMed Web of Science ®Google Scholar
• Hutagalung AH, Novick PJ. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev. 2011;91(1):119–49. doi:10.1152/physrev.00059.2009. PMID:21248164.
   PubMed Web of Science ®Google Scholar
• Ishida M, Ohbayashi N, Fukuda M. Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP. Sci Rep. 2015;5:8238. doi:10.1038/srep08238. PMID:25649263.
   PubMed Web of Science ®Google Scholar
• Jiang S, Storrie B. Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress. Mol Biol Cell. 2005;16(5):2586–96. doi:10.1091/mbc.E04-10-0861. PMID:15758030.
   PubMed Web of Science ®Google Scholar
• Kamena F, Diefenbacher M, Kilchert C, Schwarz H, Spang A. Ypt1p is essential for retrograde Golgi-ER transport and for Golgi maintenance in S. cerevisiae. J Cell Sci. 2008;121(Pt 8):1293–302. doi:10.1242/jcs.016998. PMID:18388317.
   PubMed Web of Science ®Google Scholar
• Kelly EE, Giordano F, Horgan CP, Jollivet F, Raposo G, McCaffrey MW. Rab30 is required for the morphological integrity of the Golgi apparatus. Biol Cell. 2012;104(2):84–101. doi:10.1111/boc.201100080. PMID:22188167.
   PubMed Web of Science ®Google Scholar
• Lee PL, Ohlson MB, Pfeffer SR. Rab6 regulation of the kinesin family KIF1C motor domain contributes to Golgi tethering. Elife. 2015;4. doi:10.7554/eLife.06029.
   Web of Science ®Google Scholar
• Levivier E, Goud B, Souchet M, Calmels TP, Mornon JP, Callebaut I. uDENN, DENN, and dDENN: indissociable domains in Rab and MAP kinases signaling pathways. Biochem Biophys Res Commun. 2001;287(3):688–95. doi:10.1006/bbrc.2001.5652. PMID:11563850.
   PubMed Web of Science ®Google Scholar
• Liewen H, Meinhold-Heerlein I, Oliveira V, Schwarzenbacher R, Luo G, Wadle A, Jung M, Pfreundschuh M, Stenner-Liewen F. Characterization of the human GARP (Golgi associated retrograde protein) complex. Exp Cell Res. 2005;306(1):24–34. doi:10.1016/j.yexcr.2005.01.022. PMID:15878329.
   PubMed Web of Science ®Google Scholar
• Liu S, Storrie B. Are Rab proteins the link between Golgi organization and membrane trafficking? Cell Mol Life Sci. 2012;69(24):4093–106. doi:10.1007/s00018-012-1021-6. PMID:22581368.
   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. doi:10.1371/journal.pone.0071886. PMID:23936529.
   PubMed Web of Science ®Google Scholar
• Liu S, Storrie B. How Rab proteins determine Golgi structure. Int Rev Cell Mol Biol. 2015;315:1–22. doi:10.1016/bs.ircmb.2014.12.002. PMID:25708460.
   PubMed Web of Science ®Google Scholar
• Liu S, Majeed W, Kudlyk T, Lupashin V, Storrie B. Identification of Rab41/6d effectors provides an explanation for the differential effects of Rab41/6d and Rab6a/a' on golgi organization. Front Cell Dev Biol. 2016;4:13. doi:10.3389/fcell.2016.00013. PMID:26973836.
   PubMedGoogle Scholar
• Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L. Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J Cell Biol. 2002;156(4):653–64. doi:10.1083/jcb.200110081. PMID:11839770.
   PubMed Web of Science ®Google Scholar
• Martin S, Driessen K, Nixon SJ, Zerial M, Parton RG. Regulated localization of Rab18 to lipid droplets. J Biol Chem. 2005;280:42325–35. doi:10.1074/jbc.M506651200. PMID:16207721.
   PubMed Web of Science ®Google Scholar
• Martinez O, Schmidt A, Salaméro J, Hoflack B, Roa M, Goud B. The small GTP-binding protein rab6 functions in intra-Golgi transport. J Cell Biol. 1994;127(6 Pt 1):1575–88. doi:10.1083/jcb.127.6.1575. PMID:7798313.
   PubMed Web of Science ®Google Scholar
• Martinez O, Antony C, Pehau-Arnaudet G, Berger EG, Salamero J, Goud B. GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum. Proc Natl Acad Sci U S A. 1997;94(5):1828–33. doi:10.1073/pnas.94.5.1828. PMID:9050864.
   PubMed Web of Science ®Google Scholar
• Matanis T, Akhmanova A, Wulf P, Del Nery E, Weide T, Stepanova T, Galjart N, Grosveld F, Goud B, De Zeeuw CI, et al. Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex. Nat Cell Biol. 2002;4(12):986–92. doi:10.1038/ncb891. PMID:12447383.
   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. doi:10.1074/jbc.M112.370544. PMID:22740695.
   PubMed Web of Science ®Google Scholar
• Mignogna ML, Giannandrea M, Gurgone A, Fanelli F, Raimondi F, Mapelli L, Bassani S, Fang H, Van Anken E, Alessio M, et al. The intellectual disability protein RAB39B selectively regulates GluA2 trafficking to determine synaptic AMPAR composition. Nat Commun. 2015;6:6504. doi:10.1038/ncomms7504. PMID:25784538.
   PubMed Web of Science ®Google Scholar
• Miserey-Lenkei S, Chalancon G, Bardin S, Formstecher E, Goud B, Echard A. Rab and actomyosin-dependent fission of transport vesicles at the Golgi complex. Nat Cell Biol. 2010;12(7):645–54. doi:10.1038/ncb2067. PMID:20562865.
   PubMed Web of Science ®Google Scholar
• Miserey-Lenkei S, Dimitrov A, Bardin A, Pylypenko O, Bressanelli G, Fraisier V, Houdusse A, Echard A, Goud B. Coupling generation and exit of RAB6 vesicles at Golgi fission hot spots through kinesin-myosin interactions. Nat Commun. 2017;8(1):1254. doi:10.1038/s41467-017-01266-0
   PubMedGoogle Scholar
• Mizuno-Yamasaki E, Rivera-Molina F, Novick P. GTPase networks in membrane traffic. Annu Rev Biochem. 2012;81:637–59. doi:10.1146/annurev-biochem-052810-093700. PMID:22463690.
   PubMed Web of Science ®Google Scholar
• Monetta P, Slavin I, Romero N, Alvarez C. Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association. Mol Biol Cell. 2007;18(7):2400–10. doi:10.1091/mbc.E06-11-1005. PMID:17429068.
   PubMed Web of Science ®Google Scholar
• Monier S, Jollivet F, Janoueix-Lerosey I, Johannes L, Goud B. Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport. Traffic. 2002;3(4):289–97. doi:10.1034/j.1600-0854.2002.030406.x. PMID:11929610.
   PubMed Web of Science ®Google Scholar
• Moyer BD, Allan BB, Balch WE. Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis–Golgi tethering. Traffic. 2001;2(4):268–76. doi:10.1034/j.1600-0854.2001.1o007.x. PMID:11285137.
   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. doi:10.1016/j.bbrc.2007.07.076. PMID:17678623.
   PubMed Web of Science ®Google Scholar
• Ng EL, Gan BQ, Ng F, Tang BL. Rab GTPases regulating receptor trafficking at the late endosome-lysosome membranes. Cell Biochem Funct. 2012;30(6):515–23. doi:10.1002/cbf.2827. PMID:22473705.
   PubMed Web of Science ®Google Scholar
• Nuoffer C, Davidson HW, Matteson J, Meinkoth J, Balch WE. A GDP-bound of rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments. J Cell Biol. 1994;125(2):225–37. doi:10.1083/jcb.125.2.225. PMID:8163542.
   PubMed Web of Science ®Google Scholar
• Opdam FJ, Echard A, Croes HJ, van den Hurk JA, van de Vorstenbosch RA, Ginsel LA, Goud B, Fransen JA. 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. PMID:10893188.
   PubMed Web of Science ®Google Scholar
• Ozeki S, Cheng J, Tauchi-Sato K, Hatano N, Taniguchi H, Fujimoto T. Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane. J Cell Sci. 2005;118(Pt 12):2601–11. doi:10.1242/jcs.02401. PMID:15914536.
   PubMed Web of Science ®Google Scholar
• Papanikou E, Glick BS. Golgi compartmentation and identity. Curr Opin Cell Biol. 2014;29:74–81. doi:10.1016/j.ceb.2014.04.010. PMID:24840895.
   PubMed Web of Science ®Google Scholar
• Pfeffer SR. How the Golgi works: a cisternal progenitor model. Proc Natl Acad Sci U S A. 2010;107(46):19614–8. doi:10.1073/pnas.1011016107. PMID:21045128.
   PubMed Web of Science ®Google Scholar
• Plutner H, Cox AD, Pind S, Khosravi-Far R, Bourne JR, Schwaninger R, Der CJ, Balch WE. Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. J Cell Biol. 1991;115(1):31–43. doi:10.1083/jcb.115.1.31. PMID:1918138.
   PubMed Web of Science ®Google Scholar
• Romero N, Dumur CI, Martinez H, García IA, Monetta P, Slavin I, Sampieri L, Koritschoner N, Mironov AA, De Matteis MA, Alvarez C. Rab1b overexpression modifies Golgi size and gene expression in HeLa cells and modulates the thyrotrophin response in thyroid cells in culture. Mol Biol Cell. 2013;24(5):617–32. doi:10.1091/mbc.E12-07-0530. PMID:23325787.
   PubMed Web of Science ®Google Scholar
• Rosing M, Ossendorf E, Rak A, Barnekow A. Giantin interacts with both the small GTPase Rab6 and Rab1. Exp Cell Res. 2007;313(11):2318–25. doi:10.1016/j.yexcr.2007.03.031. PMID:17475246.
   PubMed Web of Science ®Google Scholar
• Russo AJ, Mathiowetz AJ, Hong S, Welch MD, Campellone KG. Rab1 recruits WHAMM during membrane remodeling but limits actin nucleation. Mol Biol Cell. 2016;27(6):967–78. doi:10.1091/mbc.E15-07-0508. PMID:26823012.
   PubMed Web of Science ®Google Scholar
• Salian S, Cho TJ, Phadke SR, Gownshankar K, Bhavani GS, Shukla A, Jagadeesh S, Kim OH, Nishimura G, Ginsha KM. Aditional three patients with Smith-McCort dysplasia due to novel RAB33B mutations. Am J Med Genet A. 2017;173(3):588–595. doi:10.1002/ajmg.a.38064. PMID:28127940.
   PubMed Web of Science ®Google Scholar
• Sannerud R, Marie M, Nizak C, Dale HA, Pernet-Gallay K, Perez F, Goud B, Saraste J. Rab1 defines a novel pathway connecting the pre-Golgi intermediate compartment with the cell periphery. Mol Biol Cell. 2006;17(4):1514–26. doi:10.1091/mbc.E05-08-0792. PMID:16421253.
   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. PMID:7615674.
   PubMedGoogle Scholar
• Saraste J. Spatial and Functional Aspects of ER-Golgi Rabs and Tethers. Front Cell Dev Biol. 2016;4:28. doi:10.3389/fcell.2016.00028. PMID:27148530.
   PubMed Web of Science ®Google Scholar
• Sato K, Roboti P, Mironov AA, Lowe M. Coupling of vesicle tethering and Rab binding is required for in vivo functionality of the golgin GMAP-210. Mol Biol Cell. 2015;26(3):537–53. doi:10.1091/mbc.E14-10-1450. PMID:25473115.
   PubMed Web of Science ®Google Scholar
• Sengupta P, Satpute-Krishnan P, Seo AY, Burnette DT, Patterson GH, Lippincott-Schwartz J. ER trapping reveals Golgi enzymes continually revisit the ER through a recycling pathway that controls Golgi organization. Proc Natl Acad Sci U S A. 2015;112(49):E6752–61. doi:10.1073/pnas.1520957112. PMID:26598700.
   PubMed Web of Science ®Google Scholar
• Schlager MA, Kapitein LC, Grigoriev I, Burzynski GM, Wulf PS, Keijzer N, de Graaff E, Fukuda M, Shepherd IT, Akhmanova A, 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. doi:10.1038/emboj.2010.51. PMID:20360680.
   PubMed Web of Science ®Google Scholar
• Shafaq-Zadah M, Gomes-Santos CS, Bardin S, Maiuri P, Maurin M, Iranzo J, Gautreau A, Lamaze C, Caswell P, Goud B, et al. Persistent cell migration and adhesion rely on retrograde transport of β(1) integrin. Nat Cell Biol. 2016;18(1):54–64. doi:10.1038/ncb3287. PMID:26641717.
   PubMed Web of Science ®Google Scholar
• Short B, Preisinger C, Körner R, Kopajtich R, Byron O, Barr FA. A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J Cell Biol. 2001;155(6):877–83. doi:10.1083/jcb.200108079. PMID:11739401.
   PubMed Web of Science ®Google Scholar
• Short B, Haas A, Barr FA. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim Biophys Acta. 2005;1744(3):383–95. doi:10.1016/j.bbamcr.2005.02.001. PMID:15979508.
   PubMed Web of Science ®Google Scholar
• Sinka R, Gillingham AK, Kondylis V, Munro S. Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins. J Cell Biol. 2008;183(4):607–15. doi:10.1083/jcb.200808018. PMID:19001129.
   PubMed Web of Science ®Google Scholar
• Starr T, Sun Y, Wilkins N, Storrie B. Rab33b and Rab6 are functionally overlapping regulators of Golgi homeostasis and trafficking. Traffic. 2010;11(5):626–36. doi:10.1111/j.1600-0854.2010.01051.x. PMID:20163571.
   PubMed Web of Science ®Google Scholar
• Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol. 2009;10(8):513–25. doi:10.1038/nrm2728. PMID:19603039.
   PubMed Web of Science ®Google Scholar
• Storrie B, White J, Röttger S, Stelzer EH, Suganuma T, Nilsson T. Recycling of golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering. J Cell Biol. 1998;143(6):1505–21. doi:10.1083/jcb.143.6.1505. PMID:9852147.
   PubMed Web of Science ®Google Scholar
• Storrie B, Micaroni M, Morgan GP, Jones N, Kamykowski JA, Wilkins N, Pan TH, Marsh BJ. Electron tomography reveals Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number. Traffic. 2012;13(5):727–44. doi:10.1111/j.1600-0854.2012.01343.x. PMID:22335553.
   PubMed Web of Science ®Google Scholar
• Sun Y, Shestakova A, Hunt L, Sehgal S, Lupashin V, Storrie B. Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis. Mol Biol Cell. 2007;18(10):4129–42. doi:10.1091/mbc.E07-01-0080. PMID:17699596.
   PubMed Web of Science ®Google Scholar
• Teber I, Nagano F, Kremerskothen J, Bilbilis K, Goud B, Barnekow A. Rab6 interacts with the mint3 adaptor protein. Biol Chem. 2005;386(7):671–7. doi:10.1515/BC.2005.078. PMID:16207088.
   PubMed Web of Science ®Google Scholar
• Tisdale EJ, Artalejo CR. A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated events. Traffic. Biol Chem. 2007;8(6):733–41.
   Google Scholar
• Tisdale EJ, Bourne JR, Khosravi-Far R, Der CJ, Balch WE. 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. doi:10.1083/jcb.119.4.749. PMID:1429835.
   PubMed Web of Science ®Google Scholar
• Tisdale EJ. Rab2 interacts directly with atypical protein kinase C (aPKC) iota/lambda and inhibits aPKCiota/lambda-dependent glyceraldehyde-3-phosphate dehydrogenase phosphorylation. J Biol Chem. 2003;278(52):52524–30. doi:10.1074/jbc.M309343200. PMID:14570876.
   PubMed Web of Science ®Google Scholar
• Valente C, Polishchuk R, De Matteis MA. Rab6 and myosin II at the cutting edge of membrane fission. Nat Cell Biol. 2010;12(7):635–8. doi:10.1038/ncb0710-635. PMID:20596045.
   PubMed Web of Science ®Google Scholar
• Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T. Identification of rabaptin-5, rabex-5, and GM130 as putative effectors of rab33b, a regulator of retrograde traffic between the Golgi apparatus and ER. FEBS Lett. 2001;508(2):201–9. doi:10.1016/S0014-5793(01)02993-3. PMID:11718716.
   PubMed Web of Science ®Google Scholar
• Wang S, Ma Z, Xu X, Wang Z, Sun L, Zhou Y, Lin X, Hong W, Wang T. 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. doi:10.1371/journal.pone.0096242. PMID:24788816.
   PubMed Web of Science ®Google Scholar
• Wanschers B, van de Vorstenbosch R, Wijers M, Wieringa B, King SM, Fransen J. Rab6 family proteins interact with the dynein light chain protein DYNLRB1. Cell Motil Cytoskeleton. 2008;65(3):183–96. doi:10.1002/cm.20254. PMID:18044744.
   PubMed Web of Science ®Google Scholar
• Weide T, Bayer M, Köster M, Siebrasse JP, Peters R, Barnekow A. The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b. EMBO Rep. 2001;2(4):336–41. doi:10.1093/embo-reports/kve065. PMID:11306556.
   PubMed Web of Science ®Google Scholar
• White J, Johannes L, Mallard F, Girod A, Grill S, Reinsch S, Keller P, Tzschaschel B, Echard A, Goud B, et al. Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J Cell Biol. 1999;147(4):743–60. doi:10.1083/jcb.147.4.743. PMID:10562278.
   PubMed Web of Science ®Google Scholar
• Wilson BS, Nuoffer C, Meinkoth JL, McCaffery M, Feramisco JR, Balch WE, Farquhar MG. A Rab1 mutant affecting guanine nucleotide exchange promotes disassembly of the Golgi apparatus. J Cell Biol. 1994;125(3):557–71. doi:10.1083/jcb.125.3.557. PMID:8175881.
   PubMed Web of Science ®Google Scholar
• Wong M, Munro S. Membrane trafficking. The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins. Science. 2014;346(6209):1256898. doi:10.1126/science.1256898. PMID:25359980.
   PubMedGoogle Scholar
• Young J, Stauber T, del Nery E, Vernos I, Pepperkok R, Nilsson T. Regulation of microtubule-dependent recycling at the trans-Golgi network by Rab6A and Rab6A'. Mol Biol Cell. 2005;16(1):162–77. doi:10.1091/mbc.E04-03-0260. PMID:15483056.
   PubMed Web of Science ®Google Scholar
• Young J, Ménétrey 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. doi:10.1016/j.jmb.2010.01.009. PMID:20064528.
   PubMed Web of Science ®Google Scholar
• Zahraoui A, Touchot N, Chardin P, Tavitian A. The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion. J Biol Chem. 1989;264(21):12394–401. PMID:2501306.
   PubMed Web of Science ®Google Scholar
• Zheng JY, Koda T, Fujiwara T, Kishi M, Ikehara Y, Kakinuma M. A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae. J Cell Sci. 1998;111(Pt 8):1061–69. PMID:9512502.
   PubMedGoogle Scholar