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Regulation of Protein Trafficking by GTP-Binding Proteins

  • Michel Franco
  • Philippe Chavrier
  • Florence Niedergang
Part of the Molecular Biology Intelligence Unit book series (MBIU)

Abstract

In eukaryotic cells, specific mechanisms allow selective packaging of proteins and lipids into transport vesicles, which can then specifically recognize the membrane of the acceptor compartment and fuse with it to deliver their cargo. Formation, transport and docking of vesicles are based on a complex network of interactions between regulatory molecules and structural components. Small GTP-binding proteins have emerged as master regulators of all steps of vesicle trafficking. In this chapter, we will first present the general mechanisms of GTP-binding protein function that are based on their ability to bind to and hydrolyze GTP. Specific methods commonly used to study GTP-binding protein activation will be briefly de- scribed. The last section will then review, through selected examples, the different ways by which proteins belonging to the different families of small GTP-binding proteins control various aspects of intracellular vesicle trafficking.

Keywords

Coat Protein Fluorescence Resonance Energy Transfer Recombinant Antibody Golgi Membrane Exocyst Complex 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    De Vries L, Zheng B, Fischer T et al. The regulator of G protein signaling family. Annu Rev Pharmacol Toxicol 2000; 40:235–21.PubMedGoogle Scholar
  2. 2.
    Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature 2002; 420(6916):629–35.PubMedGoogle Scholar
  3. 3.
    Zerial M, McBride H. Rab proteins as membrane organizers. Nat Rev Mol Cell Biol 2001; 2(2):107–17.PubMedGoogle Scholar
  4. 4.
    Chavrier P, Goud B. The role of ARF and rab GTPases in membrane transport. Curr Opin Cell Biol 1999; 11:466–75.PubMedGoogle Scholar
  5. 5.
    Pasqualato S, Renault L, Cherfils J. Arf, Arl, Arp and Sar proteins: A family of GTP-binding proteins with a structural device for ‘front-back’ communication. EMBO Rep 2002; 3(11):1035–41.PubMedGoogle Scholar
  6. 6.
    Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: Conserved structure and molecular mechanism. Nature 1991; 349:117–27.PubMedGoogle Scholar
  7. 7.
    Corbett KD, Alber T. The many faces of Ras: Recognition of small GTP-binding proteins. Trends Biochem Sci 2001; 26(12):710–6.PubMedGoogle Scholar
  8. 8.
    Cherfils J, Chardin P. GEFs: Structural basis for their activation of small GTP-binding proteins. Trends Biochem Sci 1999; 24(8):306–11.PubMedGoogle Scholar
  9. 9.
    Boguski MS, McCormick F. Proteins regulating Ras and its relatives. Nature 1993; 366:643–654.PubMedGoogle Scholar
  10. 10.
    Scheffzek K, Ahmadian MR, Wittinghofer A. GTPase-activating proteins: Helping hands to complement an active site. Trends Biochem Sci 1998; 23(7):257–62.PubMedGoogle Scholar
  11. 11.
    Bernards A. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim Biophys Acta 2003; 1603(2):47–82.PubMedGoogle Scholar
  12. 12.
    Horiuchi H, Lippe R, McBride HM et al. A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function. Cell 1997; 90(6): 1149–59.PubMedGoogle Scholar
  13. 13.
    Wada M, Nakanishi H, Satoh A et al. Isolation and characterization of a GDP/GTP exchange protein specific for the Rab3 subfamily small G proteins. J Biol Chem 1997; 272(7):3875–8.PubMedGoogle Scholar
  14. 14.
    Walch-Solimena C, Collins RN, Novick PJ. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J Cell Biol 1997; 137(7): 1495–509.PubMedGoogle Scholar
  15. 15.
    Jones S, Richardson CJ, Litt RJ et al. Identification of regulators for Yptl GTPase nucleotide cy-cling. Mol Biol Cell 1998; 9(10):2819–37.PubMedGoogle Scholar
  16. 16.
    Donaldson JG, Jackson CL. Regulators and effectors of the ARF GTPases. Curr Opin Cell Biol 2000; 12:475–82.PubMedGoogle Scholar
  17. 17.
    Rossman KL, Der CJ, Sondek J. GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors. Nat Rev Mol Cell Biol 2005; 6(2): 167–80.PubMedGoogle Scholar
  18. 18.
    Ogasawara M, Kim SC, Adamik R et al. Similarities in function and gene structure of cytohesin-4 and cytohesin-1, guanine nucleotide-exchange proteins for ADP-ribosylation factors. J Biol Chem 2000; 275:3221–30.PubMedGoogle Scholar
  19. 19.
    Franco M, Peters PJ, Boretto J et al. EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J 1999; 18:1480–1491.PubMedGoogle Scholar
  20. 20.
    Hoffman GR, Cerione RA. Signaling to the Rho GTPases: Networking with the DH domain. FEBS Lett 2002; 513(1):85–91.PubMedGoogle Scholar
  21. 21.
    Cherfils J, Menetrey J, Mathieu M et al. Structure of the Sec7 domain of the Arf exchange factor ARNO. Nature 1998; 392:101–5.PubMedGoogle Scholar
  22. 22.
    Goldberg J. Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide ex-change and GTP-myristoyl switching. Cell 1998; 95(2):237–48.PubMedGoogle Scholar
  23. 23.
    Bernards A, Settleman J. GAP control: Regulating the regulators of small GTPases. Trends Cell Biol 2004; l4(7):377–85.Google Scholar
  24. 24.
    Alory C, Balch WE. Organization of the Rab-GDI/CHM superfamily: The functional basis for choroideremia disease. Traffic 2001; 2(8):532–43.PubMedGoogle Scholar
  25. 25.
    Olofsson B. Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling. Cell Signal 1999; ll(8):545–54.Google Scholar
  26. 26.
    Robbe K, Otto-Bruc A, Chardin P et al. Dissociation of GDP dissociation inhibitor and membrane translocation are required for efficient activation of Rac by the Dbl homology-pleckstrin homology region of Tiam. J Biol Chem 2003; 278(7):4756–62.PubMedGoogle Scholar
  27. 27.
    Hirao M, Sato N, Kondo T et al. Regulation mechanism of ERM (Ezrin/Radixin/Moesin) protein/ plasma membrane association: Possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. J Cell Biol 1996; 135:37–51.PubMedGoogle Scholar
  28. 28.
    Bretscher A. Regulation of cortical structure by the ezrin-radixin-moesin protein family. Curr Opin Cell Biol 1999; 11:109–16.PubMedGoogle Scholar
  29. 29.
    Del Pozo MA, Kiosses WB, Alderson NB et al. Integrins regulate GTP-Rac localized effector interactions through dissociation of Rho-GDI. Nat Cell Biol 2002; 4(3):232–9.PubMedGoogle Scholar
  30. 30.
    Dirac-Svejstrup AB, Sumizawa T, Pfeffer SR. Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J 1997; 16(3):465–72.PubMedGoogle Scholar
  31. 31.
    Sivars U, Aivazian D, Pfeffer SR. Yip3 catalyses the dissociation of endosomal Rab-GDI com-plexes. Nature 2003; 425(6960):856–9.PubMedGoogle Scholar
  32. 32.
    Feig LA. Tools of the trade: Use of dominant-inhibitory mutants of Ras-family GTPases. Nat Cell Biol 1999; l(2):E25–7.Google Scholar
  33. 33.
    Macia E, Luton F, Partisani M et al. The GDP-bound form of Arf6 is located at the plasma membrane. J Cell Sci 2004; 117(Pt ll):2389–98.PubMedGoogle Scholar
  34. 34.
    Mochizuki N, Yamashita S, Kurokawa K et al. Spatio-temporal images of growth-factor-induced activation of Ras and Rapl. Nature 2001; 4ll(684l):1065–8.Google Scholar
  35. 35.
    Kraynov VS, Chamberlain C, Bokoch GM et al. Localized rac activation dynamics visualized in living cells. Science 2000; 290:333–7.PubMedGoogle Scholar
  36. 36.
    Nizak C, Monier S, del Nery E et al. Recombinant antibodies to the small GTPase Rab6 as conformation sensors. Science 2003; 300(5621):984–7.PubMedGoogle Scholar
  37. 37.
    Bonifacino JS, Lippincott-Schwartz J. Coat proteins: Shaping membrane transport. Nat Rev Mol Cell Biol 2003; 4(5):409–14.PubMedGoogle Scholar
  38. 38.
    Antonny B, Schekman R. ER export: Public transportation by the COPII coach. Curr Opin Cell Biol 2001; 13(4):438–43.PubMedGoogle Scholar
  39. 39.
    Aridor M, Balch WE. Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. J Biol Chem 2000; 275(46):35673–6.PubMedGoogle Scholar
  40. 40.
    Bi X, Corpina RA, Goldberg J. Structure of the Sec23/24-Sarl prebudding complex of the COPII vesicle coat. Nature 2002; 419(6904):271–7.PubMedGoogle Scholar
  41. 41.
    Antonny B, Gounon P, Schekman R et al. Self-assembly of minimal COPII cages. EMBO Rep 2003; 4(4):4l9–24.Google Scholar
  42. 42.
    Barlowe C, Orci L, Yeung T et al. COPII: A membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum. Cell 1994; 77(6):895–907.PubMedGoogle Scholar
  43. 43.
    Matsuoka K, Orci L, Amherdt M et al. COPII-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell 1998; 93:263–75.PubMedGoogle Scholar
  44. 44.
    Oka T, Nakano A. Inhibition of GTP hydrolysis by Sarlp causes accumulation of vesicles that are a functional intermediate of the ER-to-Golgi transport in yeast. J Cell Biol 1994; 124(4):425–34.PubMedGoogle Scholar
  45. 45.
    Antonny B, Madden D, Hamamoto S et al. Dynamics of the COPII coat with GTP and stable analogues. Nat Cell Biol 2001; 3(6):531–7.PubMedGoogle Scholar
  46. 46.
    Yoshihisa T, Barlowe C, Schekman R. Requirement for a GTPase-activating protein in vesicle budding from the endoplasmic reticulum. Science 1993; 259(5100): 1466–8.PubMedGoogle Scholar
  47. 47.
    Springer S, Schekman R. Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs. Science 1998; 281:698–700.PubMedGoogle Scholar
  48. 48.
    Miller E, Antonny B, Hamamoto S et al. Cargo selection into COPII vesicles is driven by the Sec24p subunit. EMBO J 2002; 21(22):6105–13.PubMedGoogle Scholar
  49. 49.
    Aridor M, Fish KN, Bannykh S et al. The Sari GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly. J Cell Biol 2001; 152(l):213–29.PubMedGoogle Scholar
  50. 50.
    Waters MG, Serafini T, Rothman JE. ‘Coatomer’: A cytosolic protein complex containing subunits of nonclathrin-coated Golgi transport vesicles. Nature 1991; 349(6306):248–51.PubMedGoogle Scholar
  51. 51.
    Spang A, Matsuoka K, Hamamoto S et al. Coatomer, Arflp, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes. Proc Natl Acad Sci USA 1998; 95(19):11199–204.PubMedGoogle Scholar
  52. 52.
    Zhao L, Helms JB, Brugger B et al. Direct and GTP-dependent interaction of ADP ribosylation factor 1 with coatomer subunit beta. Proc Natl Acad Sci USA 1997; 94(9):44l8–23.Google Scholar
  53. 53.
    Franco M, Chardin P, Chabre M et al. Myristoylation of ADP-ribosylation factor 1 facilitates nucleotide exchange at physiological Mg2+ levels. J.Biol Chem 1995; 270:1337–41.PubMedGoogle Scholar
  54. 54.
    Renault L, Guibert B, Cherfils J. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 2003; 426(6966):525–30.PubMedGoogle Scholar
  55. 55.
    Kirchhausen T. Three ways to make a vesicle. Nat Rev Mol Cell Biol 2000; 1(3): 187–98.PubMedGoogle Scholar
  56. 56.
    Lanoix J, Ouwendijk J, Lin CC et al. GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles. EMBO J 1999; 18(18):4935–48.PubMedGoogle Scholar
  57. 57.
    Aoe T, Huber I, Vasudevan C et al. The KDEL receptor regulates a GTPase-activating protein for ADP-ribosylation factor 1 by interacting with its noncatalytic domain. J Biol Chem 1999; 274(29):20545–9.PubMedGoogle Scholar
  58. 58.
    Lanoix J, Ouwendijk J, Stark A et al. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAPl. J Cell Biol 2001; 155(7):1199–212.PubMedGoogle Scholar
  59. 59.
    Goldberg J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 1999; 96(6):893–902.PubMedGoogle Scholar
  60. 60.
    Bigay J, Gounon P, Robineau S et al. Lipid packing sensed by ArfGAPl couples COPI coat disassembly to membrane bilayer curvature. Nature 2003; 426(6966): 563–6.PubMedGoogle Scholar
  61. 61.
    Kirchhausen T. Clathrin. Annu Rev Biochem 2000; 69:699–727.PubMedGoogle Scholar
  62. 62.
    Robinson MS, Bonifacino JS. Adaptor-related proteins. Curr Opin Cell Biol 2001; 13(4):444–453.PubMedGoogle Scholar
  63. 63.
    Stamnes MA, Rothman JE. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 1993; 73(5):999–1005.PubMedGoogle Scholar
  64. 64.
    Ooi CE, Dell’Angelica EC, Bonifacino JS. ADP-ribosylation factor lf(ARFl) regulates recruitment of the AP-3 adaptor complex to membranes. J Cell Biol 1998; l42(2):391–402.Google Scholar
  65. 65.
    Boehm M, Aguilar RC, Bonifacino JS. Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO J 2001; 20(22):6265–76.PubMedGoogle Scholar
  66. 66.
    Nie Z, Hirsch DS, Randazzo PA. Arf and its many interactors. Curr Opin Cell Biol 2003; 15(4):396–404.PubMedGoogle Scholar
  67. 67.
    Krauss M, Kinuta M, Wenk MR et al. ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Igamma. J Cell Biol 2003; 162(1):113–24.PubMedGoogle Scholar
  68. 68.
    Robinson MS, Kreis TE. Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells: Effects of brefeldin A and G protein activators. Cell 1992; 69(1): 129–38.PubMedGoogle Scholar
  69. 69.
    Shinotsuka C, Yoshida Y, Kawamoto K et al. Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples Brefeldin A-induced adaptor protein-1 coat dissocia-tion and membrane tubulation. J Biol Chem 2002; 277(11):9468–73.PubMedGoogle Scholar
  70. 70.
    Symons M, Rusk N. Control of vesicular trafficking by rho GTPases. Curr Biol 2003; 13(19):1747.Google Scholar
  71. 71.
    Qualmann B, Mellor H. Regulation of endocytic traffic by Rho GTPases. Biochem J 2003; 371 (Pt2): 233–41.PubMedGoogle Scholar
  72. 72.
    Ridley AJ. Rho proteins: Linking signaling with membrane trafficking. Traffic 2001; 2(5):303–310.PubMedGoogle Scholar
  73. 73.
    Lamaze C, Chuang TH, Terlecky LJ et al. Regulation of receptor-mediated endocytosis by Rho and Rac. Nature 1996; 382:177–9.PubMedGoogle Scholar
  74. 74.
    Malecz N, McCabe PC, Spaargaren C et al. Synaptojanin 2, a novel Racl effector that regulates clathrin-mediated endocytosis. Curr Biol 2000; 10(21):1383–6.PubMedGoogle Scholar
  75. 75.
    Lamaze C, Dujeancourt A, Baba T et al. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol Cell 2001; 7(3):661–71.PubMedGoogle Scholar
  76. 76.
    O’Bryan JP, Mohney RP, Oldham CE. Mitogenesis and endocytosis: What’s at the INTERSECTION? Oncogene 2001; 20(44):6300–8.PubMedGoogle Scholar
  77. 77.
    Hussain NK, Jenna S, Glogauer M et al. Endocytic protein intersectin-1 regulates actin assembly via Cdc42 and N-WASP. Nat Cell Biol 2001; 3(10):927–32.PubMedGoogle Scholar
  78. 78.
    Yang W, Lo CG, Dispenza T et al. The Cdc42 target ACK2 directly interacts with clathrin and influences clathrin assembly. J Biol Chem 2001; 276(20): 17468–73.PubMedGoogle Scholar
  79. 79.
    Teo M, Tan L, Lim L et al. The tyrosine kinase ACK1 associates with clathrin-coated vesicles through a binding motif shared by arrestin and other adaptors. J Biol Chem 2001; 276(21): 18392–8.PubMedGoogle Scholar
  80. 80.
    Lin Q, Lo CG, Cerione RA et al. The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J Biol Chem 2002; 277(12):10134–8.PubMedGoogle Scholar
  81. 81.
    Ridley AJ, Paterson HF, Johnston CL et al. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 1992; 70:401–10.PubMedGoogle Scholar
  82. 82.
    West MA, Prescott AR, Eskelinen EL et al. Rac is required for constitutive macropinocytosis by dendritic cells but does not control its downregulation. Curr Biol 2000; 10(14):839–48.PubMedGoogle Scholar
  83. 83.
    Garret WS, Chen LM, Kroschewski R et al. Developmental control of endocytosis in dendritic cells by Cdc42. Cell 2000; 102:325–34.Google Scholar
  84. 84.
    Galan JE. Salmonella interactions with host cells: Type III secretion at work. Annu Rev Cell Dev Biol 2001; 17:53–86.PubMedGoogle Scholar
  85. 85.
    Stebbins CE, Galan JE. Structural mimicry in bacterial virulence. Nature 2001; 4l2(6848):701–5.Google Scholar
  86. 86.
    Boquet P, Lemichez E. Bacterial virulence factors targeting Rho GTPases: Parasitism or symbiosis? Trends Cell Biol 2003; 13(5):238–46.PubMedGoogle Scholar
  87. 87.
    McNiven MA, Cao H, Pitts KR et al. The dynamin family of mechanoenzymes: Pinching in new places. Trends Biochem Sci 2000; 25(3):115–20.PubMedGoogle Scholar
  88. 88.
    Hinshaw JE. Dynamin and its role in membrane fission. Annu Rev Cell Dev Biol 2000; 16:483–519.PubMedGoogle Scholar
  89. 89.
    Sever S. Dynamin and endocytosis. Curr Opin Cell Biol 2002; 14(4):463–7.PubMedGoogle Scholar
  90. 90.
    Song BD, Schmid SL. A molecular motor or a regulator? Dynamin’s in a class of its own. Biochemistry 2003; 42(6):1369–76.PubMedGoogle Scholar
  91. 91.
    van Dam EM, Stoorvogel W. Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol Biol Cell 2002; 13(1):169–82.PubMedGoogle Scholar
  92. 92.
    Schliwa M, Woehlke G. Molecular motors. Nature 2003; 422(6933):759–65.PubMedGoogle Scholar
  93. 93.
    Hammer IIIrd JA, Wu XS. Rabs grab motors: Defining the connections between Rab GTPases and motor proteins. Curr Opin Cell Biol 2002; 14(1):69–75.Google Scholar
  94. 94.
    Wu XS, Rao K, Zhang H et al. Identification of an organelle receptor for myosin-Va. Nat Cell Biol 2002; 4(4):271–8.PubMedGoogle Scholar
  95. 95.
    Desnos C, Schonn JS, Huet S et al. Rab27A and its effector MyRIP link secretory granules to F-actin and control their motion towards release sites. J Cell Biol 2003; 163(3):559–70.PubMedGoogle Scholar
  96. 96.
    Nielsen E, Severin F, Backer JM et al. Rab5 regulates motility of early endosomes on microtubules. Nat Cell Biol 1999; 1(6):376–82.PubMedGoogle Scholar
  97. 97.
    Echard A, Jollivet F, Martinez O et al. Interaction of a Golgi-associated kinesin-like protein with Rab6. Science 1998; 279:580–5.PubMedGoogle Scholar
  98. 98.
    Short B, Preisinger C, Schaletzky J et al. The Rab6 GTPase regulates recruitment of the dynactin complex to Golgi membranes. Curr Biol 2002; 12(20):1792–5.PubMedGoogle Scholar
  99. 99.
    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.PubMedGoogle Scholar
  100. 100.
    Cantalupo G, Alifano P, Roberti V et al. Rab-interacting lysosomal protein (RILP): The Rab7 effector required for transport to lysosomes. EMBO J 2001; 20(4):683–93.PubMedGoogle Scholar
  101. 101.
    Gasman S, Kalaidzidis Y, Zerial M. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol 2003; 5(3):195–204.PubMedGoogle Scholar
  102. 102.
    Orth JD, McNiven MA. Dynamin at the actin-membrane interface. Curr Opin Cell Biol 2003; 15(1):31–9.PubMedGoogle Scholar
  103. 103.
    Rothman JE. Mechanisms of intracellular protein transport. Nature 1994; 372(6501):55–63.PubMedGoogle Scholar
  104. 104.
    Pfeffer SR. Transport-vesicle targeting: Tethers before SNAREs. Nat Cell Biol 1999; 1(1):E17–22.PubMedGoogle Scholar
  105. 105.
    Finger FP, Novick P. Spatial regulation of exocytosis: Lessons from yeast. J Cell Biol 1998; 142:609–12.PubMedGoogle Scholar
  106. 106.
    Hsu SC, Hazuka CD, Foletti DL et al. Targeting vesicles to specific sites on the plasma membrane: The role of the sec6/8 complex. Trends Biochem Sci 1999; 9:150–3.Google Scholar
  107. 107.
    Finger FP, Hughes TE, Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 1998; 92:559–71.PubMedGoogle Scholar
  108. 108.
    Guo W, Tamanoi F, Novick P. Spatial regulation of the exocyst complex by Rhol GTPase. Nat Cell Biol 2001; 3(4):353–60.PubMedGoogle Scholar
  109. 109.
    Zhang X, Bi E, Novick P et al. Cdc42 interacts with the exocyst and regulates polarized secretion. J Biol Chem 2001; 276(50):46745–50.PubMedGoogle Scholar
  110. 110.
    Robinson NG, Guo L, Imai J et al. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol Cell Biol 1999; 19(5):3580–7.PubMedGoogle Scholar
  111. 111.
    Guo W, Roth D, Walch-Solimena C et al. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 1999; 18:1071–80.PubMedGoogle Scholar
  112. 112.
    Novick P, Guo W. Ras family therapy: Rab, Rho and Ral talk to the exocyst. Trends Cell Biol 2002; 12(6):247–9.PubMedGoogle Scholar
  113. 113.
    Hsu SC, Ting AE, Hazuka CD et al. The mammalian brain rsec6/8 complex. Neuron 1996; 17:1209–19.PubMedGoogle Scholar
  114. 114.
    Kee Y, Yoo JS, Hazuka CD et al. Subunit structure of the mammalian exocyst complex. Proc Natl Acad Sci USA 1997; 94:14438–43.PubMedGoogle Scholar
  115. 115.
    Grindstaff KK, Yeaman C, Anandasabapathy N et al. Sec6/8 complex is recruited to cell-cell con-tacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 1998; 93:731–40.PubMedGoogle Scholar
  116. 116.
    Lipschutz JH, Guo W, O’Brien LE et al. Exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins. Mol Biol Cell 2000; 11:4259–75.PubMedGoogle Scholar
  117. 117.
    Hazuka CD, Foletti DL, Hsu SC et al. The sec6/8 complex is located at neurite outgrowth and axonal synapse-assembly domains. J Neurosci 1999; 19(4): 1324–34.PubMedGoogle Scholar
  118. 118.
    Vega IE, Hsu SC. The exocyst complex associates with microtubules to mediate vesicle targeting and neurite outgrowth. J Neurosci 2001; 21(11):3839–48.PubMedGoogle Scholar
  119. 119.
    Yeaman C, Grindstaff KK, Wright JR et al. Sec6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells. J Cell Biol 2001; 155(4):593–604.PubMedGoogle Scholar
  120. 120.
    Folsch H, Pypaert M, Maday S et al. The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 2003; 163(2):351–62.PubMedGoogle Scholar
  121. 121.
    Prigent M, Dubois T, Raposo G et al. ARF6 controls post-endocytic recycling through its down-stream exocyst complex effector. J Cell Biol 2003; 163(5):11H–21.Google Scholar
  122. 122.
    Brymora A, Valova VA, Larsen MR et al. The brain exocyst complex interacts with RalA in a GTP-dependent manner: Identification of a novel mammalian Sec3 gene and a second Sec 15 gene. J Biol Chem 2001; 276(32):29792–7.PubMedGoogle Scholar
  123. 123.
    Sugihara K, Asano S, Tanaka K et al. The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat Cell Biol 2002; 4(1):73–8.PubMedGoogle Scholar
  124. 124.
    Moskalenko S, Henry DO, Rosse C et al. The exocyst is a Ral effector complex. Nat Cell Biol 2002; 4(1):66–72.PubMedGoogle Scholar
  125. 125.
    Moskalenko S, Tong C, Rosse C et al. Ral GTPases regulate exocyst assembly through dual sub-unit interactions. J Biol Chem 2003; 278(51):51743–8.PubMedGoogle Scholar
  126. 126.
    Polzin A, Shipitsin M, Goi T et al. Ral-GTPase influences the regulation of the readily releasable pool of synaptic vesicles. Mol Cell Biol 2002; 22(6): 1714–22.PubMedGoogle Scholar
  127. 127.
    Saltiel AR, Pessin JE. Insulin signaling pathways in time and space. Trends Cell Biol 2002; 12(2):65–71.PubMedGoogle Scholar
  128. 128.
    Inoue M, Chang L, Hwang J et al. The exocyst complex is required for targeting of Glut4 to the plasma membrane by insulin. Nature 2003; 422(6932):629–33.PubMedGoogle Scholar
  129. 129.
    Lipschutz JH, Mostov KE. Exocytosis: The many masters of the exocyst. Curr Biol 2002; 12(6):R212–4.PubMedGoogle Scholar
  130. 130.
    Whyte JR, Munro S. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev Cell 2001; 1(4):527–37.PubMedGoogle Scholar
  131. 131.
    Suvorova ES, Duden R, Lupashin W. The Sec34/Sec35p complex, a Yptlp effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. J Cell Biol 2002; 157(4):631–43.PubMedGoogle Scholar
  132. 132.
    Sacher M, Barrowman J, Wang W et al. TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport. Mol Cell 2001; 7(2):433–42.PubMedGoogle Scholar
  133. 133.
    Whyte JR, Munro S. Vesicle tethering complexes in membrane traffic. J Cell Sci 2002; 115(Pt13): 2627–37.Google Scholar
  134. 134.
    Allan BB, Moyer BD, Balch WE. Rabl recruitment of pi 15 into a cis-SNARE complex: Program-ming budding COPII vesicles for fusion. Science 2000; 289(5478):444–8.PubMedGoogle Scholar
  135. 135.
    Wickner W. Yeast vacuoles and membrane fusion pathways. EMBO J 2002; 21(6):1241–7.PubMedGoogle Scholar
  136. 136.
    Panic B, Whyte JR, Munro S. The ARF-like GTPases Arllp and Arl3p act in a pathway that interacts with vesicle-tethering factors at the Golgi apparatus. Curr Biol 2003; 13(5):405–10.PubMedGoogle Scholar
  137. 137.
    Panic B, Perisic O, Veprintsev DB et al. Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol Cell 2003; 12(4):863–74.PubMedGoogle Scholar
  138. 138.
    Short B, Barr FA. Membrane traffic: A glitch in the Golgi matrix. Curr Biol 2003; 13(8):R311–313.PubMedGoogle Scholar
  139. 139.
    Christoforidis S, McBride HM, Burgoyne RD et al. The Rab5 effector EEA1 is a core component of endosome docking. Nature 1999; 397:621–5.PubMedGoogle Scholar
  140. 140.
    Bourne HR. Do GTPases direct membrane traffic in secretion? Cell 1988; 53(5):669–71.PubMedGoogle Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  • Michel Franco
    • 1
  • Philippe Chavrier
    • 2
  • Florence Niedergang
    • 3
  1. 1.Institut de Pharmacologic Moleculaire et CellulaireUPR 411 CNRSValbonneFrance
  2. 2.Membrane and Cytoskeleton Dynamics Group Institut CurieCNRS UMR 144ParisFrance
  3. 3.Phagocytosis and Bacterial Invasion Group Institut Cochin INSERM U 567, CNRS UMR 8104University Paris DescartesParisFrance

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