Post translational modifications of Rab GTPases

References

• Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009; 10:513-25; PMID:19603039; http://dx.doi.org/10.1038/nrm2728
   PubMed Web of Science ®Google Scholar
• Hutagalung AH, Novick PJ. Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev 2011; 91:119-49; PMID:21248164; http://dx.doi.org/10.1152/physrev.00059.2009
   PubMed Web of Science ®Google Scholar
• Schwartz SL, Cao C, Pylypenko O, Rak A, Wandinger-Ness A. Rab GTPases at a glance. J Cell Sci 2007; 120:3905-10; PMID:17989088; http://dx.doi.org/10.1242/jcs.015909
   PubMed Web of Science ®Google Scholar
• Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2:107-17; PMID:11252952; http://dx.doi.org/10.1038/35052055
   PubMed Web of Science ®Google Scholar
• Delprato A, Merithew E, Lambright DG. Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5. Cell 2004; 118:607-17; PMID:15339665; http://dx.doi.org/10.1016/j.cell.2004.08.009
   PubMed Web of Science ®Google Scholar
• Matsui Y, Kikuchi A, Araki S, Hata Y, Kondo J, Teranishi Y, Takai Y. Molecular cloning and characterization of a novel type of regulatory protein (GDI) for smg p25A, a ras p21-like GTP-binding protein. Mol Cell Biol 1990; 10:4116-22; PMID:2115118; http://dx.doi.org/10.1128/MCB.10.8.4116
   PubMed Web of Science ®Google Scholar
• Pan X, Eathiraj S, Munson M, Lambright DG. TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 2006; 442:303-6; PMID:16855591; http://dx.doi.org/10.1038/nature04847
   PubMed Web of Science ®Google Scholar
• Soldati T, Shapiro AD, Svejstrup AB, Pfeffer SR. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature 1994; 369:76-8; PMID:8164745; http://dx.doi.org/10.1038/369076a0
   PubMed Web of Science ®Google Scholar
• Seabra MC, Goldstein JL, Sudhof TC, Brown MS. Rab geranylgeranyl transferase. A multisubunit enzyme that prenylates GTP-binding proteins terminating in Cys-X-Cys or Cys-Cys. J Biol Chem 1992; 267:14497-503; PMID:1321151
   PubMed Web of Science ®Google Scholar
• Andres DA, Seabra MC, Brown MS, Armstrong SA, Smeland TE, Cremers FP, Goldstein JL. cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein. Cell 1993; 73:1091-9; PMID:8513495; http://dx.doi.org/10.1016/0092-8674(93)90639-8
   PubMed Web of Science ®Google Scholar
• Pylypenko O, Rak A, Reents R, Niculae A, Sidorovitch V, Cioaca MD, Bessolitsyna E, Thomä NH, Waldmann H, Schlichting I, et al. Structure of Rab escort protein-1 in complex with Rab geranylgeranyltransferase. Mol Cell 2003; 11:483-94; PMID:12620235; http://dx.doi.org/10.1016/S1097-2765(03)00044-3
   PubMed Web of Science ®Google Scholar
• Rak A, Pylypenko O, Niculae A, Pyatkov K, Goody RS, Alexandrov K. Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease. Cell 2004; 117:749-60; PMID:15186776; http://dx.doi.org/10.1016/j.cell.2004.05.017
   PubMed Web of Science ®Google Scholar
• Guo Z, Wu YW, Das D, Delon C, Cramer J, Yu S, Thuns S, Lupilova N, Waldmann H, Brunsveld L, et al. Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation. EMBO J 2008; 27:2444-56; PMID:18756270; http://dx.doi.org/10.1038/emboj.2008.164
   PubMed Web of Science ®Google Scholar
• Wu YW, Goody RS, Abagyan R, Alexandrov K. Structure of the disordered C terminus of Rab7 GTPase induced by binding to the Rab geranylgeranyl transferase catalytic complex reveals the mechanism of Rab prenylation. J Biol Chem 2009; 284:13185-92; PMID:19240028; http://dx.doi.org/10.1074/jbc.M900579200
   PubMed Web of Science ®Google Scholar
• Leung KF, Baron R, Ali BR, Magee AI, Seabra MC. Rab GTPases containing a CAAX motif are processed post-geranylgeranylation by proteolysis and methylation. J Biol Chem 2007; 282:1487-97; PMID:17114793; http://dx.doi.org/10.1074/jbc.M605557200
   PubMed Web of Science ®Google Scholar
• Derre I, Isberg RR. Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect Immun 2004; 72:3048-53; PMID:15102819; http://dx.doi.org/10.1128/IAI.72.5.3048-3053.2004
   PubMed Web of Science ®Google Scholar
• Kagan JC, Stein MP, Pypaert M, Roy CR. Legionella subvert the functions of Rab1 and Sec 22b to create a replicative organelle. J Exp Med 2004; 199:1201-11; PMID:15117975; http://dx.doi.org/10.1084/jem.20031706
   PubMed Web of Science ®Google Scholar
• Murata T, Delprato A, Ingmundson A, Toomre DK, Lambright DG, Roy CR. The Legionella pneumophila effector protein DrrA is a Rab1 guanine nucleotide-exchange factor. Nat Cell Biol 2006; 8:971-7; PMID:16906144; http://dx.doi.org/10.1038/ncb1463
   PubMed Web of Science ®Google Scholar
• Machner MP, Isberg RR. Targeting of host Rab GTPase function by the intravacuolar pathogen Legionella pneumophila. Dev Cell 2006; 11:47-56; PMID:16824952; http://dx.doi.org/10.1016/j.devcel.2006.05.013
   PubMed Web of Science ®Google Scholar
• Muller MP, Peters H, Blumer J, Blankenfeldt W, Goody RS, Itzen A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 2010; 329:946-9; PMID:20651120; http://dx.doi.org/10.1126/science.1192276
   PubMed Web of Science ®Google Scholar
• Neunuebel MR, Chen Y, Gaspar AH, Backlund PS, Jr, Yergey A, Machner MP. De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila. Science 2011; 333:453-6; PMID:21680813; http://dx.doi.org/10.1126/science.1207193
   PubMed Web of Science ®Google Scholar
• Tan Y, Luo ZQ. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 2011; 475:506-9; PMID:21734656; http://dx.doi.org/10.1038/nature10307
   PubMed Web of Science ®Google Scholar
• Mukherjee S, Liu X, Arasaki K, McDonough J, Galan JE, Roy CR. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 2011; 477:103-6; PMID:21822290; http://dx.doi.org/10.1038/nature10335
   PubMed Web of Science ®Google Scholar
• Goody PR, Heller K, Oesterlin LK, Muller MP, Itzen A, Goody RS. Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins. EMBO J 2012; 31:1774-84; PMID:22307087; http://dx.doi.org/10.1038/emboj.2012.16
   PubMed Web of Science ®Google Scholar
• Tan Y, Arnold RJ, Luo ZQ. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc Natl Acad Sci U S A 2011; 108:21212-7; PMID:22158903; http://dx.doi.org/10.1073/pnas.1114023109
   PubMed Web of Science ®Google Scholar
• Oesterlin LK, Goody RS, Itzen A. Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor. Proc Natl Acad Sci U S A 2012; 109:5621-6; PMID:22411835; http://dx.doi.org/10.1073/pnas.1121161109
   PubMed Web of Science ®Google Scholar
• Pylypenko O, Goud B. Posttranslational modifications of Rab GTPases help their insertion into membranes. Proc Natl Acad Sci U S A 2012; 109:5555-6; PMID:22451945; http://dx.doi.org/10.1073/pnas.1202494109
   PubMed Web of Science ®Google Scholar
• Bailly E, McCaffrey M, Touchot N, Zahraoui A, Goud B, Bornens M. Phosphorylation of two small GTP-binding proteins of the Rab family by p34cdc2. Nature 1991; 350:715-8; PMID:1902553; http://dx.doi.org/10.1038/350715a0
   PubMed Web of Science ®Google Scholar
• van der Sluijs P, Hull M, Huber LA, Male P, Goud B, Mellman I. Reversible phosphorylation–dephosphorylation determines the localization of rab4 during the cell cycle. EMBO J 1992; 11:4379-89; PMID:1425574
   PubMed Web of Science ®Google Scholar
• Fitzgerald ML, Reed GL. Rab6 is phosphorylated in thrombin-activated platelets by a protein kinase C-dependent mechanism: effects on GTP/GDP binding and cellular distribution. Biochem J 1999; 342(Pt 2):353-60; PMID:10455022; http://dx.doi.org/10.1042/bj3420353
   PubMed Web of Science ®Google Scholar
• Lai YC, Kondapalli C, Lehneck R, Procter JB, Dill BD, Woodroof HI, Gourlay R, Peggie M, Macartney TJ, Corti O, et al. Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1. EMBO J 2015; 34:2840-61; PMID:26471730; http://dx.doi.org/10.15252/embj.201591593
   PubMed Web of Science ®Google Scholar
• Steger M, Tonelli F, Ito G, Davies P, Trost M, Vetter M, Wachter S, Lorentzen E, Duddy G, Wilson S, et al. Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases. Elife 2016; 5; PMID:26824392; http://dx.doi.org/10.7554/eLife.12813
   PubMed Web of Science ®Google Scholar
• Levin RS, Hertz NT, Burlingame AL, Shokat KM, Mukherjee S. Innate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogen. Proc Natl Acad Sci U S A 2016; 113:E4776-83; PMID:27482120; http://dx.doi.org/10.1073/pnas.1608355113
   PubMed Web of Science ®Google Scholar
• Shinde SR, Maddika S. PTEN modulates EGFR late endocytic trafficking and degradation by dephosphorylating Rab7. Nat Commun 2016; 7:10689; PMID:26869029; http://dx.doi.org/10.1038/ncomms10689
   PubMed Web of Science ®Google Scholar
• Satpathy S, Wagner SA, Beli P, Gupta R, Kristiansen TA, Malinova D, Francavilla C, Tolar P, Bishop GA, Hostager BS, et al. Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation. Mol Syst Biol 2015; 11:810; PMID:26038114; http://dx.doi.org/10.15252/msb.20145880
   PubMed Web of Science ®Google Scholar
• Lachance V, Degrandmaison J, Marois S, Robitaille M, Genier S, Nadeau S, Angers S, Parent JL. Ubiquitylation and activation of a Rab GTPase is promoted by a beta(2)AR-HACE1 complex. J Cell Sci 2014; 127:111-23; PMID:24190883; http://dx.doi.org/10.1242/jcs.132944
   PubMed Web of Science ®Google Scholar
• Qiu J, Sheedlo MJ, Yu K, Tan Y, Nakayasu ES, Das C, Liu X, Luo ZQ. Ubiquitination independent of E1 and E2 enzymes by bacterial effectors. Nature 2016; 533:120-4; PMID:27049943; http://dx.doi.org/10.1038/nature17657
   PubMed Web of Science ®Google Scholar
• Walther DJ, Peter JU, Winter S, Holtje M, Paulmann N, Grohmann M, Vowinckel J, Alamo-Bethencourt V, Wilhelm CS, Ahnert-Hilger G, et al. Serotonylation of small GTPases is a signal transduction pathway that triggers platelet alpha-granule release. Cell 2003; 115:851-62; PMID:14697203; http://dx.doi.org/10.1016/S0092-8674(03)01014-6
   PubMed Web of Science ®Google Scholar
• Paulmann N, Grohmann M, Voigt JP, Bert B, Vowinckel J, Bader M, Skelin M, Jevsek M, Fink H, Rupnik M, et al. Intracellular serotonin modulates insulin secretion from pancreatic beta-cells by protein serotonylation. PLoS Biol 2009; 7:e1000229; PMID:19859528; http://dx.doi.org/10.1371/journal.pbio.1000229
   PubMed Web of Science ®Google Scholar