Are Rab proteins the link between Golgi organization and membrane trafficking?

详细信息    查看全文

• 作者：Shijie Liu (1)
  Brian Storrie (1)
  
• 关键词：Rab proteins ; Golgi apparatus ; Membrane trafficking ; Golgi organization
• 刊名：Cellular and Molecular Life Sciences (CMLS)
• 出版年：2012
• 出版时间：December 2012
• 年：2012
• 卷：69
• 期：24
• 页码：4093-4106
• 全文大小：508KB
• 参考文献：1. Farquhar MG, Palade GE (1998) The Golgi apparatus: 100聽years of progress and controversy. Trends Cell Biol 8:2鈥?0
  2. Emr S, Glick BS, Linstedt AD, Lippincott-Schwartz J, Luini A, Malhotra V, Marsh BJ, Nakano A, Pfeffer SR, Rabouille C et al (2009) Journeys through the Golgi-taking stock in a new era. J Cell Biol 187:449鈥?53
  3. Wilson C, Venditti R, Rega LR, Colanzi A, D鈥橝ngelo G, De Matteis MA (2011) The Golgi apparatus: an organelle with multiple complex functions. Biochem J 433(1):1鈥?
  4. Tamaki H, Yamashina S (2002) The stack of the Golgi apparatus. Arch Histol Cytol 65(3):209鈥?18
  5. Lowe M (2011) Structure organization of the Golgi apparatus. Curr Opin Cell Biol 23:85鈥?3
  6. Shorter J, Warren G (2002) Golgi architecture and inheritance. Annu Rev Cell Biol 18:379鈥?20
  7. Marra P, Salvatore L, Mironov A Jr, Di Campli A, Di Tullio G, Trucco A, Beznoussenko G, Mironov A, De Matteis MA (2007) The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130. Mol Biol Cell 18:1595鈥?608
  8. Drickamer K, Taylor ME (1998) Evolving views of protein glycosylation. Trends Biochem Sci 23:321鈥?24
  9. F眉llekrug J, Nilsson T (1998) Protein sorting in the Golgi complex. Biochim Biophys Acta 1404(1鈥?):77鈥?4
  10. Preuss D, Mulholland J, Franzusoff A, Segev N, Botstein D (1992) Characterization of the / Saccharomyces Golgi complex through the cell cycle by immunoelectron microscopy. Mol Biol Cell 3(7):789鈥?03
  11. Suda Y, Nakano A (2011) The yeast Golgi apparatus. Traffic. doi:10.1111/j.1600-0854.2011.01316.x
  12. Dupree P, Sherrier DJ (1998) The plant Golgi apparatus. Biochim Biophys Acta 1404(1鈥?):259鈥?70
  13. Nickel W, Wieland FT (1998) Biosynthetic protein transport through the early secretory pathway. Histochem Cell Biol 109(5鈥?):477鈥?86
  14. Aridor M, Bannykh SI, Rowe T, Balch WE (1995) Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J Cell Biol 131(4):875鈥?93
  15. Weidman PJ (1995) Anterograde transport through the Golgi complex: do Golgi tubules hold the key? Trends Cell Biol 5(8):302鈥?05
  16. Lorente-Rodr铆guez A, Barlowe C (2011) Requirement for Golgi-localized PI(4)P in fusion of COPII vesicles with Golgi compartments. Mol Biol Cell 22(2):216鈥?29
  17. Miesenb枚ck G, Rothman JE (1995) The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack. J Cell Biol 129:309鈥?19
  18. Ganley IG, Espinosa E, Pfeffer SR (2008) A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J Cell Biol 180(1):159鈥?72
  19. Lee MC, Miller EA, Goldberg J, Orci L, Schekman R (2004) Bi-directional protein transport between the ER and Golgi. Annu Rev Cell Dev Biol 20:87鈥?23
  20. Tarrag贸-Trani MT, Storrie B (2007) Alternate routes for drug delivery to the cell interior: pathways to the Golgi apparatus and endoplasmic reticulum. Adv Drug Deliv Rev 59(8):782鈥?97
  21. Cosson P, Amherdt M, Rothman JE, Orci L (2002) A resident Golgi protein is excluded from peri-Golgi vesicles in NRK cells. Proc Natl Acad Sci USA 99(20):12831鈥?2834
  22. Storrie B (2005) Maintenance of Golgi apparatus structure in the face of continuous protein recycling to the endoplasmic reticulum: making ends meet. Int Rev Cytol 244:69鈥?4
  23. Glick BS (2000) Organization of the Golgi apparatus. Curr Opin Cell Biol 12(4):450鈥?56
  24. Hutagalung AH, Novick PJ (2011) Role of Rab GTPases in membrane traffic and cell physiology. Physiol Rev 91(1):119鈥?49
  25. Goud B, Gleeson PA (2010) TGN golgins, Rabs and cytoskeleton: regulating the Golgi trafficking highways. Trends Cell Biol 20(6):329鈥?36
  26. Barr FA (2009) Rab GTPase function in Golgi trafficking. Semin Cell Dev Biol 20(7):780鈥?83
  27. Jordens I, Marsman M, Kuijl C, Neefjes J (2005) Rab proteins, connecting transport and vesicle fusion. Traffic 6(12):1070鈥?077
  28. Stenmark H (2009) Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 10(8):513鈥?25
  29. Bock JB, Matern HT, Peden AA, Scheller RH (2001) A genomic perspective on membrane compartment organization. Nature 409(6822):839鈥?41
  30. Bucci C, Parton RG, Mather IH, Stunnenberg H, Simons K, Hoflack B, Zerial M (1992) The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway. Cell 70(5):715鈥?28
  31. McBride HM, Rybin V, Murphy C, Giner A, Teasdale R, Zerial M (1999) Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 98(3):377鈥?86
  32. Guo W, Roth D, Walch-Solimena C, Novick P (1999) The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18(4):1071鈥?080
  33. Dumas JJ, Zhu Z, Connolly JL, Lambright DG (1999) Structural basis of activation and GTP hydrolysis in Rab proteins. Structure聽7(4):413鈥?23
  34. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, Ferrin TE (2004) UCSF Chimera鈥攁 visualization system for exploratory research and analysis. J Comput Chem 25(13):1605鈥?612
  35. Pfeffer SR (2005) Structural clues to Rab GTPase functional diversity. J Biol Chem 280(16):15485鈥?5488
  36. Lee M, Mishra A, Lambright D (2009) Structural mechanisms for regulation of membrane traffic by Rab GTPases. Traffic 10:1377鈥?389
  37. Aivazian D, Serrano R, Pfeffer S (2006) TIP47 is a key effector for Rab9 localization. J Cell Biol 173:917鈥?26
  38. Ali B, Seabra M (2005) Targeting of Rab GTPases to cellular membranes. Biochem Soc Trans 33:652鈥?56
  39. Chavrier P, Gorvel JP, Stelzer E, Simons K, Gruenberg J, Zerial M (1991) Hypervariable C-terminal domain of rab proteins acts as a targeting signal. Nature 353:769鈥?72
  40. Pereira-Leal J, Seabra M (2000) 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 301:1077鈥?087
  41. Moore I, Schell J, Palme K (1995) Subclass-specific sequence motifs identified in Rab GTPases. Trends Biochem Sci 20:10鈥?2
  42. Ostermeier C, Brunger AT (1999) Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A. Cell 96:363鈥?74
  43. Schlichting I, Almo SC, Rapp G, Wilson K, Petratos K, Lentfer A, Wittinghofer A, Kabsch W, Pai EF, Petsko GA, Goody RS (1990) Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis. Nature 345:309鈥?15
  44. Stroupe C, Brunger AT (2000) Crystal structures of a Rab protein in its inactive and active conformations. J Mol Biol 304(4):585鈥?98
  45. Brennwald P, Novick P (1993) Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362:560鈥?63
  46. Pfeffer SR (2001) Rab GTPases: specifying and deciphering organelle identity and function. Trends Cell Biol 11(12):487鈥?91
  47. Alexandrov K, Horiuchi H, Steele-Mortimer O, Seabra M, Zerial M (1994) Rab escort protein-1 is a multifunctional protein that accompanies newly prenylated rab proteins to their target membranes. EMBO J 13:5262鈥?273
  48. Andres D, Seabra M, Brown M, Armstrong S, Smeland T, Cremers F, Goldstein J (1993) cDNA cloning of component A of Rab geranylgeranyl transferase and demonstration of its role as a Rab escort protein. Cell 73:1091鈥?099
  49. Ullrich O, Stenmark H, Alexandrov K, Huber LA, Kaibuchi K, Sasaki T, Takai Y, Zerial M (1993) Rab GDP dissociation inhibitor as a general regulator for the membrane association of rab proteins. J Biol Chem 268:18143鈥?8150
  50. Dirac-Svejstrup AB, Sumizawa T, Pfeffer SR (1997) Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J 16:465鈥?72
  51. Collins R (2003) 鈥淕etting it on鈥?GDI displacement and small GTPase membrane recruitment. Mol Cell 12:1064鈥?066
  52. Bos J, Rehmann H, Wittinghofer A (2007) GEFs and GAPs: critical elements in the control of small G proteins. Cell 129:865鈥?77
  53. Alory C, Balch WE (2001) Organization of the Rab-GDI/CHM superfamily: the functional basis for choroideremia disease. Traffic 2(8):532鈥?43
  54. Garrett MD, Zahner JE, Cheney CM, Novick PJ (1994) GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway. EMBO J 13(7):1718鈥?728
  55. Grosshans BL, Ortiz D, Novick P (2006) Rabs and their effectors: achieving specificity in membrane traffic. Proc Natl Acad Sci USA 103(32):11821鈥?1827
  56. Kishida S, Shirataki H, Sasaki T, Kato M, Kaibuchi K, Takai Y (1993) Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein. J Biol Chem 268(30):22259鈥?2261
  57. Wang X, Hu B, Zimmermann B, Kilimann MW (2001) Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal alpha -helix motifs. J Biol Chem 276(35):32480鈥?2488
  58. Handley MT, Burgoyne RD (2008) The Rab27 effector Rabphilin, unlike Granuphilin and Noc2, rapidly exchanges between secretory granules and cytosol in PC12 cells. Biochem Biophys Res Commun 373(2):275鈥?81
  59. Fukuda M (2005) Versatile role of Rab27 in membrane trafficking: focus on the Rab27 effector families. J Biochem 137(1):9鈥?6
  60. D铆az E, Pfeffer SR (1998) TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking. Cell 93(3):433鈥?43
  61. Bahadoran P, Aberdam E, Mantoux F, Busc脿 R, Bille K, Yalman N, de Saint-Basile G, Casaroli-Marano R, Ortonne JP, Ballotti R (2001) Rab27a: a key to melanosome transport in human melanocytes. J Cell Biol 152(4):843鈥?50
  62. Hume AN, Collinson LM, Rapak A, Gomes AQ, Hopkins CR, Seabra MC (2001) Rab27a regulates the peripheral distribution of melanosomes in melanocytes. J Cell Biol 152(4):795鈥?08
  63. Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC (2002) A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J Biol Chem 277(28):25423鈥?5430
  64. Matanis T, Akhmanova A, Wulf P, Del Nery E, Weide T, Stepanova T, Galjart N, Grosveld F, Goud B, De Zeeuw CI, Barnekow A, Hoogenraad CC (2002) Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex. Nat Cell Biol 4(12):986鈥?92
  65. Moyer BD, Allan BB, Balch WE (2001) Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis鈥擥olgi tethering. Traffic 2(4):268鈥?76
  66. TerBush DR, Maurice T, Roth D, Novick P (1996) The exocyst is a multiprotein complex required for exocytosis in / Saccharomyces cerevisiae. EMBO J 15(23):6483鈥?494
  67. Lehman K, Rossi G, Adamo JE, Brennwald P (1999) Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J Cell Biol 146(1):125鈥?40
  68. Grosshans BL, Andreeva A, Gangar A, Niessen S, Yates JR 3rd, Brennwald P, Novick P (2006) The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p. J Cell Biol 172(1):55鈥?6
  69. Weide T, Teuber J, Bayer M, Barnekow A (2003) MICAL-1 isoforms, novel rab1 interacting proteins. Biochem Biophys Res Commun 306(1):79鈥?6
  70. Fischer J, Weide T, Barnekow A (2005) The MICAL proteins and rab1: a possible link to the cytoskeleton? Biochem Biophys Res Commun 328(2):415鈥?23
  71. Ooms LM, Horan KA, Rahman P, Seaton G, Gurung R, Kethesparan DS, Mitchell CA (2009) The role of the inositol polyphosphate 5-phosphatases in cellular function and human disease. Biochem J 419(1):29鈥?9
  72. Hyvola N, Diao A, McKenzie E, Skippen A, Cockcroft S, Lowe M (2006) Membrane targeting and activation of the Lowe syndrome protein OCRL1 by rab GTPases. EMBO J 25(16):3750鈥?761
  73. Laufman O, Hong W, Lev S (2011) The COG complex interacts directly with Syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. J Cell Biol 194(3):459鈥?72
  74. Alvarez C, Garcia-Mata R, Hauri HP, Sztul E (2001) The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic. J Biol Chem 276(4):2693鈥?700
  75. Weide T, Bayer M, K枚ster M, Siebrasse JP, Peters R, Barnekow A (2001) The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b. EMBO Rep 2(4):336鈥?41
  76. Diao A, Rahman D, Pappin DJC, Lucocq J, Lowe M (2003) The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J Cell Biol 160:201鈥?12
  77. Satoh A, Wang Y, Malsam J, Beard MB, Warren G (2003) Golgin-84 is a rab1 binding partner involved in Golgi structure. Traffic 4(3):153鈥?61
  78. Fukuda M, Kanno E, Ishibashi K, Itoh T (2008) Large scale screening for novel rab effectors reveals unexpected broad Rab binding specificity. Mol Cell Proteomics 7(6):1031鈥?042
  79. Duran JM, Kinseth M, Bossard C, Rose DW, Polishchuk R, Wu CC, Yates J, Zimmerman T, Malhotra V (2008) The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis. Mol Biol Cell 19(6):2579鈥?587
  80. Short B, Preisinger C, K枚rner R, Kopajtich R, Byron O, Barr FA (2001) A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J Cell Biol 155(6):877鈥?83
  81. Fernandes H, Franklin E, Recacha R, Houdusse A, Goud B, Khan AR (2009) Structural aspects of Rab6-effector complexes. Biochem Soc Trans 37(5):1037鈥?041
  82. Antony C, Cibert C, G茅raud G, Santa Maria A, Maro B, Mayau V, Goud B (1992) The small GTP-binding protein rab6p is distributed from medial Golgi to the trans-Golgi network as determined by a confocal microscopic approach. J Cell Sci 103:785鈥?96
  83. Opdam FJ, Echard A, Croes HJ, van den Hurk JA, van de Vorstenbosch RA, Ginsel LA, Goud B, Fransen JA (2000) The small GTPase Rab6B, a novel Rab6 subfamily member, is cell-type specifically expressed and localised to the Golgi apparatus. J Cell Sci 113:2725鈥?735
  84. Young J, M茅n茅trey J, Goud B (2010) RAB6C is a retrogene that encodes a centrosomal protein involved in cell cycle progression. J Mol Biol 397(1):69鈥?8
  85. Schlager MA, Kapitein LC, Grigoriev I, Burzynski GM, Wulf PS, Keijzer N, de Graaff E, Fukuda M, Shepherd IT, Akhmanova A, Hoogenraad CC (2010) Pericentrosomal targeting of Rab6 secretory vesicles by Bicaudal-D-related protein 1 (BICDR-1) regulates neuritogenesis. EMBO J 29(10):1637鈥?651
  86. Barbero P, Bittova L, Pfeffer SR (2002) Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol 156(3):511鈥?18
  87. D铆az E, Schimm枚ller F, Pfeffer SR (1997) A novel Rab9 effector required for endosome-to-TGN transport. J Cell Biol 138(2):283鈥?90
  88. Reddy JV, Burguete AS, Sridevi K, Ganley IG, Nottingham RM, Pfeffer SR (2006) A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling. Mol Biol Cell 17(10):4353鈥?363
  89. Schuck S, Gerl MJ, Ang A, Manninen A, Keller P, Mellman I, Simons K (2007) Rab10 is involved in basolateral transport in polarized Madin-Darby canine kidney cells. Traffic 8(1):47鈥?0
  90. Ullrich O, Reinsch S, Urb茅 S, Zerial M, Parton RG (1996) Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol 135(4):913鈥?24
  91. Lindsay AJ, McCaffrey MW (2002) Rab11-FIP2 functions in transferrin recycling and associates with endosomal membranes via its COOH-terminal domain. J Cell Chem 277(30):27193鈥?7199
  92. Schonteich E, Wilson GM, Burden J, Hopkins CR, Anderson K, Goldenring JR, Prekeris R (2008) The Rip11/Rab11-FIP5 and kinesin II complex regulates endocytic protein recycling. J Cell Sci 121(22):3824鈥?833
  93. Mammoto A, Ohtsuka T, Hotta I, Sasaki T, Takai Y (1999) Rab11BP/Rabphilin-11, a downstream target of rab11 small G protein implicated in vesicle recycling. J Cell Chem 274(36):25517鈥?5524
  94. Lindsay AJ, Marie N, McCaffrey MW (2005) Functional properties of the Rab-binding domain of Rab coupling protein. Methods Enzymol 403:481鈥?91
  95. Olkkonen VM, Dupree P, Killisch I, L眉tcke A, Zerial M, Simons K (1993) Molecular cloning and subcellular localization of three GTP-binding proteins of the rab subfamily. J Cell Sci 106(4):1249鈥?261
  96. Iida H, Wang L, Nishii K, Ookuma A, Shibata Y (1996) Identification of rab12 as a secretory granule-associated small GTP-binding protein in atrial myocytes. Circ Res 78(2):343鈥?47
  97. Nokes RL, Fields IC, Collins RN, F枚lsch H (2008) Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells. J Cell Biol 182(5):845鈥?53
  98. Zahraoui A, Joberty G, Arpin M, Fontaine JJ, Hellio R, Tavitian A, Louvard D (1994) 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 124(1鈥?):101鈥?15
  99. Junutula JR, De Mazi茅re AM, Peden AA, Ervin KE, Advani RJ, van Dijk SM, Klumperman J, Scheller RH (2004) Rab14 is involved in membrane trafficking between the Golgi complex and endosomes. Mol Biol Cell 15(5):2218鈥?229
  100. Proikas-Cezanne T, Gaugel A, Frickey T, Nordheim A (2006) Rab14 is part of the early endosomal clathrin-coated TGN microdomain. FEBS Lett 580(22):5241鈥?246
  101. Kelly EE, Horgan CP, Adams C, Patzer TM, N铆 Sh煤illeabh谩in DM, Norman JC, McCaffrey MW (2009) Class I Rab11-family interacting proteins are binding targets for the Rab14 GTPase. Biol Cell 102(1):51鈥?2
  102. Yamamoto H, Koga H, Katoh Y, Takahashi S, Nakayama K, Shin HW (2010) Functional cross-talk between Rab14 and Rab4 through a dual effector, RUFY1/Rabip4. Mol Biol Cell 21(15):2746鈥?755
  103. Dejgaard SY, Murshid A, Erman A, Kizilay O, Verbich D, Lodge R, Dejgaard K, Ly-Hartig TB, Pepperkok R, Simpson JC, Presley JF (2008) Rab18 and Rab43 have key roles in ER-Golgi trafficking. J Cell Sci 121:2768鈥?781
  104. L眉tcke A, Parton RG, Murphy C, Olkkonen VM, Dupree P, Valencia A, Simons K, Zerial M (1994) Cloning and subcellular localization of novel rab proteins reveals polarized and cell type-specific expression. J Cell Sci 107:3437鈥?448
  105. Brasaemle DL, Dolios G, Shapiro L, Wang R (2004) Proteomic analysis of proteins associated with lipid droplets of basal and lipolytically stimulated 3T3-L1 adipocytes. J Biol Chem 279(45):46835鈥?6842
  106. Ozeki S, Cheng J, Tauchi-Sato K, Hatano N, Taniguchi H, Fujimoto T (2005) Rab18 localizes to lipid droplets and induces their close apposition to the endoplasmic reticulum-derived membrane. J Cell Sci 118:2601鈥?611
  107. Martin S, Driessen K, Nixon SJ, Zerial M, Parton RG (2005) Regulated localization of Rab18 to lipid droplets: effects of lipolytic stimulation and inhibition of lipid droplet catabolism. J Biol Chem 280(51):42325鈥?2335
  108. Gilchrist A, Au CE, Hiding J, Bell AW, Fernandez-Rodriguez J, Lesimple S, Nagaya H, Roy L, Gosline SJ, Hallett M, Paiement J, Kearney RE, Nilsson T, Bergeron JJ (2006) Quantitative proteomics analysis of the secretory pathway. Cell 127(6):1265鈥?281
  109. L眉tcke A, Olkkonen VM, Dupree P, L眉tcke H, Simons K, Zerial M (1995) Isolation of a murine cDNA clone encoding Rab19, a novel tissue-specific small GTPase. Gene 155(2):257鈥?60
  110. Amillet JM, Ferbus D, Real FX, Antony C, Muleris M, Gress TM, Goubin G (2006) Characterization of human Rab20 overexpressed in exocrine pancreatic carcinoma. Hum Pathol 37(3):256鈥?63
  111. Chen D, Guo J, Miki T, Tachibana M, Gahl WA (1996) Molecular cloning of two novel rab genes from human melanocytes. Gene 174(1):129鈥?34
  112. de Leeuw HP, Wijers-Koster PM, van Mourik JA, Voorberg J (1999) Small GTP-binding protein RalA associates with Weibel-Palade bodies in endothelial cells. Thromb Haemost 82(3):1177鈥?181
  113. Kelly EE, Giordano F, Horgan CP, Jollivet F, Raposo G, McCaffrey MW (2011) Rab30 is required for the morphological integrity of the Golgi apparatus. Biol Cell. doi:10.1111/boc.201100080
  114. Fukuda M, Itoh T (2008) Direct link between Atg protein and small GTPase Rab: Atg16L functions as a potential Rab33 effector in mammals. Autophagy 4(6):824鈥?26
  115. Mallard F, Tang BL, Galli T, Tenza D, Saint-Pol A, Yue X, Antony C, Hong W, Goud B, Johannes L (2002) Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J Cell Biol 156(4):653鈥?64
  116. Valsdottir R, Hashimoto H, Ashman K, Koda T, Storrie B, Nilsson T (2001) 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 508(2):201鈥?09
  117. Starr T, Sun Y, Wilkins N, Storrie B (2010) Rab33b and Rab6 are functionally overlapping regulators of Golgi homeostasis and trafficking. Traffic 11(5):626鈥?36
  118. Plutner H, Cox AD, Pind S, Khosravi-Far R, Bourne JR, Schwaninger R, Der CJ, Balch WE (1991) Rab1b regulates vesicular transport between the endoplasmic reticulum and successive Golgi compartments. J Cell Biol 115(1):31鈥?3
  119. Goldenberg NM, Grinstein S, Silverman M (2007) Golgi-bound Rab34 is a novel member of the secretory pathway. Mol Biol Cell 18(12):4762鈥?771
  120. Song Y, Ailenberg M, Silverman M (1998) Cloning of a novel gene in the human kidney homologous to rat munc13s: its potential role in diabetic nephropathy. Kidney Int 53(6):1689鈥?695
  121. Colucci AM, Campana MC, Bellopede M, Bucci C (2005) The Rab-interacting lysosomal protein, a Rab7 and Rab34 effector, is capable of self-interaction. Biochem Biophys Res Commun 334(1):128鈥?33
  122. Mori T, Fukuda Y, Kuroda H, Matsumura T, Ota S, Sugimoto T, Nakamura Y, Inazawa J (1999) 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 254(3):594鈥?00
  123. Chen L, Hu J, Yun Y, Wang T (2010) Rab36 regulates the spatial distribution of late endosomes and lysosomes through a similar mechanism to Rab34. Mol Membr Biol 27(1):24鈥?1
  124. Chen T, Han Y, Yang M, Zhang W, Li N, Wan T, Guo J, Cao X (2003) Rab39, a novel Golgi-associated Rab GTPase from human dendritic cells involved in cellular endocytosis. Biochem Biophys Res Commun 303(4):1114鈥?120
  125. Becker CE, Creagh EM, O鈥橬eill LA (2009) Rab39a binds caspase-1 and is required for caspase-1-dependent interleukin-1beta secretion. J Biol Chem 284(50):34531鈥?4537
  126. Lee RH, Iioka H, Ohashi M, Iemura S, Natsume T, Kinoshita N (2007) XRab40 and XCullin5 form a ubiquitin ligase complex essential for the noncanonical Wnt pathway. EMBO J 26(15):3592鈥?606
  127. Kanno E, Ishibashi K, Kobayashi H, Matsui T, Ohbayashi N, Fukuda M (2010) Comprehensive screening for novel rab-binding proteins by GST pull-down assay using 60 different mammalian Rabs. Traffic 11(4):491鈥?07
  128. Haas AK, Yoshimura S, Stephens DJ, Preisinger C, Fuchs E, Barr FA (2007) Analysis of GTPase-activating proteins: Rab1 and Rab43 are key Rabs required to maintain a functional Golgi complex in human cells. J Cell Sci 120:2997鈥?010
  129. Bard F, Casano L, Mallabiabarrena A, Wallace E, Saito K, Kitayama H, Guizzunti G, Hu Y, Wendler F, Dasgupta R, Perrimon N, Malhotra V (2006) Functional genomics reveals genes involved in protein secretion and Golgi organization. Nature 439(7076):604鈥?07
  130. Echard A, Opdam FJ, de Leeuw HJ, Jollivet F, Savelkoul P, Hendriks W, Voorberg J, Goud B, Fransen JA (2000) Alternative splicing of the human Rab6A gene generates two close but functionally different isoforms. Mol Biol Cell 11(11):3819鈥?833
  131. Goud B, Zahraoui A, Tavitian A, Saraste J (1990) Small GTP-binding protein associated with Golgi cisternae. Nature 345(6275):553鈥?56
  132. Martinez O, Schmidt A, Salam茅ro J, Hoflack B, Roa M, Goud B (1994) The small GTP-binding protein rab6 functions in intra-Golgi transport. J Cell Biol 127:1575鈥?588
  133. Martinez O, Antony C, Pehau-Arnaudet G, Berger EG, Salamero J, Goud B (1997) GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum. Proc Natl Acad Sci USA 94(5):1828鈥?833
  134. White J, Johannes L, Mallard F, Girod A, Grill S, Reinsch S, Keller P, Tzschaschel B, Echard A, Goud B, Stelzer EH (1999) Rab6 coordinates a novel Golgi to ER retrograde transport pathway in live cells. J Cell Biol 147(4):743鈥?60
  135. Girod A, Storrie B, Simpson JC, Johannes L, Goud B, Roberts LM, Lord JM, Nilsson T, Pepperkok R (1999) Evidence for a COP-I-independent transport route from the Golgi complex to the endoplasmic reticulum. Nat Cell Biol 1(7):423鈥?30
  136. Kano F, Yamauchi S, Yoshida Y, Watanabe-Takahashi M, Nishikawa K, Nakamura N, Murata M (2009) Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER. J Cell Sci 122:2218鈥?227
  137. Sannerud R, Saraste J, Goud B (2003) Retrograde traffic in the biosynthetic-secretory route: pathways and machinery. Curr Opin Cell Biol 15(4):438鈥?45
  138. Del Nery E, Miserey-Lenkei S, Falgui猫res T, Nizak C, Johannes L, Perez F, Goud B (2006) Rab6A and Rab6A鈥?GTPases play non-overlapping roles in membrane trafficking. Traffic 7(4):394鈥?07
  139. Monier S, Jollivet F, Janoueix-Lerosey I, Johannes L, Goud B (2002) Characterization of novel Rab6-interacting proteins involved in endosome-to-TGN transport. Traffic 3(4):289鈥?97
  140. Utskarpen A, Slagsvold HH, Iversen TG, W盲lchli S, Sandvig K (2006) Transport of ricin from endosomes to the Golgi apparatus is regulated by Rab6A and Rab6A鈥? Traffic 7(6):663鈥?72
  141. Young J, Stauber T, del Nery E, Vernos I, Pepperkok R, Nilsson T (2005) Regulation of microtubule-dependent recycling at the trans-Golgi network by Rab6A and Rab6A鈥? Mol Biol Cell 16(1):162鈥?77
  142. Miserey-Lenkei S, Chalancon G, Bardin S, Formstecher E, Goud B, Echard A (2010) Rab and actomyosin-dependent fission of transport vesicles at the Golgi complex. Nat Cell Biol 12(7):645鈥?54
  143. Valente C, Polishchuk R, De Matteis MA (2010) Rab6 and myosin II at the cutting edge of membrane fission. Nat Cell Biol 12(7):635鈥?38
  144. De Matteis MA, Luini A (2008) Exiting the Golgi complex. Nat Rev Mol Cell Biol 9(4):273鈥?84
  145. Grigoriev I, Splinter D, Keijzer N, Wulf PS, Demmers J, Ohtsuka T, Modesti M, Maly IV, Grosveld F, Hoogenraad CC, Akhmanova A (2007) Rab6 regulates transport and targeting of exocytotic carriers. Dev Cell 13(2):305鈥?14
  146. Grigoriev I, Yu KL, Martinez-Sanchez E, Serra-Marques A, Smal I, Meijering E, Demmers J, Per盲nen J, Pasterkamp RJ, van der Sluijs P, Hoogenraad CC, Akhmanova A (2011) Rab6, Rab8, and MICAL3 cooperate in controlling docking and fusion of exocytotic carriers. Curr Biol 21(11):967鈥?74
  147. Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K (1993) Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol 123(1):35鈥?5
  148. Sun Y, Shestakova A, Hunt L, Sehgal S, Lupashin V, Storrie B (2007) Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis. Mol Biol Cell 18(10):4129鈥?142
  149. Storrie B, Micaroni M, Morgan GP, Jones N, Kamykowski JA, Wilkins N, Pan TH, Marsh BJ (2012) Electron tomography reveals that Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number. Traffic 13(5):727鈥?44
  150. Karess R (2005) Rod-Zw10-Zwilch: a key player in the spindle checkpoint. Trends Cell Biol 15(7):386鈥?92
  151. Hirose H, Arasaki K, Dohmae N, Takio K, Hatsuzawa K, Nagahama M, Tani K, Yamamoto A, Tohyama M, Tagaya M (2004) Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi. EMBO J 23(6):1267鈥?278
  152. Arasaki K, Taniguchi M, Tani K, Tagaya M (2006) RINT-1 regulates the localization and entry of ZW10 to the syntaxin 18 complex. Mol Biol Cell 17(6):2780鈥?788
  153. Zolov SN, Lupashin VV (2005) Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. J Cell Biol 168(5):747鈥?59
  154. Shestakova A, Zolov S, Lupashin V (2006) COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation. Traffic 7(2):191鈥?04
  155. Wanschers BF, van de Vorstenbosch R, Schlager MA, Splinter D, Akhmanova A, Hoogenraad CC, Wieringa B, Fransen JA (2007) A role for the Rab6B Bicaudal-D1 interaction in retrograde transport in neuronal cells. Exp Cell Res 313(16):3408鈥?420
  156. Hoogenraad CC, Akhmanova A, Howell SA, Dortland BR, De Zeeuw CI, Willemsen R, Visser P, Grosveld F, Galjart N (2001) Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes. EMBO J 20(15):4041鈥?054
  157. Koda T, Kakinuma M (1993) Molecular cloning of a cDNA encoding a novel small GTP-binding protein. FEBS Lett 328:21鈥?4
  158. Zheng JY, Koda T, Arimura Y, Kishi M, Kakinuma M (1997) Structure and expression of the mouse S10 gene. Biochim Biophys Acta 1351(1鈥?):47鈥?0
  159. Zheng JY, Koda T, Fujiwara T, Kishi M, Ikehara Y, Kakinuma M (1998) A novel Rab GTPase, Rab33B, is ubiquitously expressed and localized to the medial Golgi cisternae. J Cell Sci 111:1061鈥?069
  160. Jiang S, Storrie B (2005) Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress. Mol Biol Cell 16(5):2586鈥?596
  161. Saraste J, Lahtinen U, Goud B (1995) Localization of the small GTP-binding protein rab1p to early compartments of the secretory pathway. J Cell Sci 108:1541鈥?552
  162. Nuoffer C, Davidson HW, Matteson J, Meinkoth J, Balch WE (1994) A GDP-bound form of Rab1 inhibits protein export from the endoplasmic reticulum and transport between Golgi compartments. J Cell Biol 125(2):225鈥?37
  163. Tisdale EJ, Balch WE (1996) Rab2 is essential for the maturation of pre-Golgi intermediates. J Biol Chem 271(46):29372鈥?9379
  164. Tisdale EJ, Bourne JR, Khosravi-Far R, Der CJ, Balch WE (1992) GTP-binding mutants of rab1 and rab2 are potent inhibitors of vesicular transport from the endoplasmic reticulum to the Golgi complex. J Cell Biol 119(4):749鈥?61
  165. Fuchs E, Haas AK, Spooner RA, Yoshimura S, Lord JM, Barr FA (2007) Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways. J Cell Biol 177(6):1133鈥?143
  166. Luo Z, Gallwitz D (2003) Biochemical and genetic evidence for the involvement of yeast Ypt6-GTPase in protein retrieval to different Golgi compartments. J Biol Chem 278(2):791鈥?99
  167. Tsukada M, Gallwitz D (1996) Isolation and characterization of SYS genes from yeast, multicopy suppressors of the functional loss of the transport GTPase Ypt6p. J Cell Sci 109:2471鈥?481
  168. Bensen ES, Yeung BG, Payne GS (2001) Ric1p and the Ypt6p GTPase function in a common pathway required for localization of trans-Golgi network membrane proteins. Mol Biol Cell 12(1):13鈥?6
  169. Siniossoglou S (2005) Affinity purification of Ypt6 effectors and identification of TMF/ARA160 as a Rab6 interactor. Methods Enzymol 403:599鈥?07
  170. Tsukada M, Will E, Gallwitz D (1999) Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast. Mol Biol Cell 10(1):63鈥?5
  171. Touchot N, Zahraoui A, Vielh E, Tavitian A (1989) Biochemical properties of the YPT-related rab1B protein. Comparison with rab1A. FEBS Lett 256(1鈥?):79鈥?4
  172. Vielh E, Touchot N, Zahraoui A, Tavitian A (1989) Nucleotide sequence of a rat cDNA: rab1B, encoding a rab1-YPT related protein. Nucleic Acids Res 17(4):1770
  173. Ferro-Novick S, Novick P (1993) The role of GTP-binding proteins in transport along the exocytic pathway. Annu Rev Cell Biol 9:575鈥?99
  174. Hanbruck H, Prange R, Vorgias C, Gallwitz D (1989) The / ras-related mouse ypt 1 protein can functionally replace the / YPT1 gene product in yeast. EMBO J 8:1427鈥?432
  175. Cao X, Ballew N, Barlowe C (1998) Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 17(8):2156鈥?165
  176. Suvorova ES, Duden R, Lupashin VV (2002) The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol 157(4):631鈥?43
  177. Jedd G, Mulholland J, Segev N (1997) Two new Ypt GTPases are required for exit from the yeast trans-Golgi compartment. J Cell Biol 137(3):563鈥?80
  178. Du LL, Novick P (2001) Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p. Mol Biol Cell 12(5):1215鈥?226
  179. Rivera-Molina FE, Novick PJ (2009) A Rab GAP cascade defines the boundary between two Rab GTPases on the secretory pathway. Proc Natl Acad Sci USA 106(34):14408鈥?4413
  180. Jones S, Newman C, Liu F, Segev N (2000) The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell 11(12):4403鈥?411
  181. Ortiz D, Medkova M, Walch-Solimena C, Novick P (2002) Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast. J Cell Biol 157(6):1005鈥?015
  182. Barr FA, Short B (2003) Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 15(4):405鈥?13
  183. Xiang Y, Wang Y (2010) GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking. J Cell Biol 188(2):237鈥?51
  
• 作者单位：Shijie Liu (1)
  Brian Storrie (1)
  
  1. Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR, 72205, USA
  
• ISSN：1420-9071

文摘

The fundamental separation of Golgi function between subcompartments termed cisternae is conserved across all eukaryotes. Likewise, Rab proteins, small GTPases of the Ras superfamily, are putative common coordinators of Golgi organization and protein transport. However, despite sequence conservation, e.g., Rab6 and Ypt6 are conserved proteins between humans and yeast, the fundamental organization of the organelle can vary profoundly. In the yeast Saccharomyces cerevisiae, the Golgi cisternae are physically separated from one another, while in mammalian cells, the cisternae are stacked one upon the other. Moreover, in mammalian cells, many Golgi stacks are typically linked together to generate a ribbon structure. Do evolutionarily conserved Rab proteins regulate secretory membrane trafficking and diverse Golgi organization in a common manner? In mammalian cells, some Golgi-associated Rab proteins function in coordination of protein transport and maintenance of Golgi organization. These include Rab6, Rab33B, Rab1, Rab2, Rab18, and Rab43. In yeast, these include Ypt1, Ypt32, and Ypt6. Here, based on evidence from both yeast and mammalian cells, we speculate on the essential role of Rab proteins in Golgi organization and protein transport.