Tethering Factors

  • Vladimir Lupashin
  • Elizabeth Sztul
Part of the Molecular Biology Intelligence Unit book series (MBIU)


The movement of proteins between compartments of the secretory and endocytic pathways occurs via vesicles and/or larger carriers. The efficacy of both pathways relies on high fidelity with which the vesicles are delivered to the appropriate target membrane. The initial recognition between a vesicle and a target membrane appears to be mediated by members of loosely related family of tethering factors. Tethering factors can be generally divided into a group of long coiled-coil proteins and a group of large multi-subunit complexes. In both cases, the tethers can span relatively long distances (>200 nm) between the vesicle and the acceptor membrane. As such, they may provide a molecular net to catch relevant vesicles and increase the possibility that they will fuse with the appropriate membrane. In addition, tethers may have additional roles in facilitating the formation of SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complexes, promoting cargo selection, and regulating the interactions of membrane carriers with the cytoskeleton. This chapter will focus on functions of tethering factors in vesicle-mediated transport. We describe the current understanding of tethering at distinct sites of the secretory and endocytic pathways.


Snare Complex Membrane Traffic Multisubunit Complex COPII Vesicle 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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  1. 1.
    Bonifacino JS, Glick BS. The mechanisms of vesicle budding and fusion. Cell 2004; 116(2):153–166.PubMedGoogle Scholar
  2. 2.
    Nie Z, Hirsch DS, Randazzo PA. Arf and its many interactors. Curr Opin Cell Biol 2003; 15(4):396–404.PubMedGoogle Scholar
  3. 3.
    Ungar D, Hughson FM. SNARE protein structure and function. Annu Rev Cell Dev Biol 2003; 19:493–517.PubMedGoogle Scholar
  4. 4.
    Pfeffer SR. Rab GTPases: Specifying and deciphering organelle identity and function. Trends Cell Biol 2001; 11(12):487–91.PubMedGoogle Scholar
  5. 5.
    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.PubMedGoogle Scholar
  6. 6.
    Nakajima H, Hirata A, Ogawa Y et al. A cytoskeleton-related gene, usol, is required for intracellular protein transport in Saccharomyces cerevisiae. J Cell Biol 1991; 113:245–60.PubMedGoogle Scholar
  7. 7.
    Sapperstein SK, Lupashin W, Schmitt HD et al. Assembly of the ER to Golgi SNARE complex requires Usolp. Journal of Cell Biology 1996; 132(5):755–67.PubMedGoogle Scholar
  8. 8.
    Segev N, Mulholland J, Botstein D. The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery. Cell 1988; 52(6):915–24.PubMedGoogle Scholar
  9. 9.
    Cao X, Ballew N, Barlowe C. Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J 1998; 17(8):2156–65.PubMedGoogle Scholar
  10. 10.
    Barlowe C. Coupled ER to Golgi transport reconstituted with purified cytosolic proteins. J Cell Biol 1997; 139(5):1097–108.PubMedGoogle Scholar
  11. 11.
    Waters MG, Clary DO, Rothman JE. A novel 115-kD peripheral membrane protein is required for intercisternal transport in the Golgi stack. J Cell Biol 1992; 118(5):1015–26.PubMedGoogle Scholar
  12. 12.
    Sapperstein SK, Walter DM, Grosvenor AR et al. p115 is a general vesicular transport factor related to the yeast endoplasmic reticulum to Golgi transport factor Usolp. Proc Natl Acad Sci USA 1995; 92(2):522–6.PubMedGoogle Scholar
  13. 13.
    Alvarez C, Fujita H, Hubbard A et al. ER to Golgi transport: Requirement for p115 at a pre-Golgi VTC stage. J Cell Biol 1999; 147(6):1205–22.PubMedGoogle Scholar
  14. 14.
    Alvarez C, Garcia-Mata R, Hauri HP et al. The p115-interactive proteins GM130 and giantin participate in endoplasmic reticulum-Golgi traffic. J Biol Chem 2001; 276(4):2693–700.PubMedGoogle Scholar
  15. 15.
    Shorter J, Warren G. A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J Cell Biol 1999; l46(1):57–70.Google Scholar
  16. 16.
    Sohda M, Misumi Y, Yoshimura S et al. Depletion of vesicle-tethering factor p115 causes mini-stacked Golgi fragments with delayed protein transport. Biochem Biophys Res Commun 2005; 338(2):1268–74.PubMedGoogle Scholar
  17. 17.
    Yamakawa H, Seog DH, Yoda K et al. Usol protein is a dimer with two globular heads and a long coiled-coil tail. J Struct Biol 1996; 116(3):356–65.PubMedGoogle Scholar
  18. 18.
    Brandon E, Szul T, Alvarez C et al. On and off membrane dynamics of the endoplasmic reticulum-golgi tethering factor p115 in vivo. Mol Biol Cell 2006; 17(7):2996–3008.PubMedGoogle Scholar
  19. 19.
    Beard M, Satoh A, Shorter J et al. A cryptic Rab1-binding site in the p115 tethering protein. J Biol Chem 2005; 280(27):25840–8.PubMedGoogle Scholar
  20. 20.
    Shorter J, Beard MB, Seemann J et al. Sequential tethering of Golgins and catalysis of SNARE-pin assembly by the vesicle-tethering protein p115. J Cell Biol 2002; 157(1):45–62.PubMedGoogle Scholar
  21. 21.
    Puthenveedu MA, Linstedt AD. Gene replacement reveals that p115/SNARE interactions are essential for Golgi biogenesis. Proc Natl Acad Sci USA 2004; 101(5):1253–6.PubMedGoogle Scholar
  22. 22.
    Gillingham AK, Pfeifer AC, Munro S. GASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin. Mol Biol Cell 2002; 13(11):376l–74.Google Scholar
  23. 23.
    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.PubMedGoogle Scholar
  24. 24.
    Nakamura N, Rabouille C, Watson R et al. Characterization of a cis-Golgi matrix protein, GM130. J Cell Biol 1995; 131(6 Pt 2):1715–26.PubMedGoogle Scholar
  25. 25.
    Sonnichsen B, Lowe M, Levine T et al. A role for giantin in docking COPI vesicles to Golgi membranes. J Cell Biol 1998; 140(5):1013–21.PubMedGoogle Scholar
  26. 26.
    Kingsley DM, Kozarsky KF, Segal M et al. Three types of low density lipoprotein receptor-deficient mutant have pleiotropic defects in the synthesis of N-linked, O-linked, and lipid-linked carbohydrate chains. J Cell Biol 1986; 102(5):1576–85.PubMedGoogle Scholar
  27. 27.
    Vasile E, Perez T, Nakamura N et al. Structural integrity of the Golgi is temperature sensitive in conditional-lethal mutants with no detectable GM130. Traffic 2003; 4(4):254–72.PubMedGoogle Scholar
  28. 28.
    Kondylis V, Rabouille C. A novel role for dp115 in the organization of tER sites in Drosophila. J Cell Biol 2003; 162(2):185–98.PubMedGoogle Scholar
  29. 29.
    Linstedt AD, Hauri HP. Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol Biol Cell 1993; 4(7):679–93.PubMedGoogle Scholar
  30. 30.
    Misumi Y, Sohda M, Tashiro A et al. An essential cytoplasmic domain for the Golgi localization of coiled-coil proteins with a COOH-terminal membrane anchor. J Biol Chem 2001; 276(9):6867–73.PubMedGoogle Scholar
  31. 31.
    Malsam J, Satoh A, Pelletier L et al. Golgin tethers define subpopulations of COPI vesicles. Science 2005; 307(5712):1095–8.PubMedGoogle Scholar
  32. 32.
    Lesa GM, Seemann J, Shorter J et al. The amino-terminal domain of the golgi protein giantin interacts directly with the vesicle-tethering protein p115. J Biol Chem 2000; 275(4):2831–6.PubMedGoogle Scholar
  33. 33.
    Rabouille C, Misteli T, Watson R et al. Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J. Cell Biol 1995; 129(3):605–18.PubMedGoogle Scholar
  34. 34.
    Linstedt AD, Jesch SA, Mehta A et al. Binding relationships of membrane tethering components. The giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus. J Biol Chem 2000; 275(14):10196–201.PubMedGoogle Scholar
  35. 35.
    Puthenveedu MA, Linstedt AD. Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components giantin and GM130. J Cell Biol 2001; 155(2):227–38.PubMedGoogle Scholar
  36. 36.
    Short B, Haas A, Barr FA. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochimica Et Biophysica Acta-Molecular Cell Research 2005; 1744(3):383–95.Google Scholar
  37. 37.
    Bascom RA, Srinivasan S, Nussbaum RL. Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain. J Biol Chem 1999; 274(5):2953–62.PubMedGoogle Scholar
  38. 38.
    Satoh A, Wang Y, Malsam J et al. Golgin-84 is a rab1 binding partner involved in Golgi structure. Traffic 2003; 4(3):153–61.PubMedGoogle Scholar
  39. 39.
    Diao A, Rahman D, Pappin DJ et al. 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.PubMedGoogle Scholar
  40. 40.
    Wu M, Lu L, Hong W et al. Structural basis for recruitment of GRIP domain golgin-245 by small GTPase Aril. Nat Struct Mol Biol 2004; 11(1):86–94.PubMedGoogle Scholar
  41. 41.
    Yoshino A, Setty SR, Poynton C et al. tGolgin-1 (p230, golgin-245) modulates Shigatoxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre. J Cell Sci 2005; 118(Pt 10):2279–93.PubMedGoogle Scholar
  42. 42.
    Dumas JJ, Merithew E, Sudharshan E et al. Multivalent endosome targeting by homodimeric EEA1. Mol Cell 2001; 8(5):947–58.PubMedGoogle Scholar
  43. 43.
    Simonsen A, Lippe R, Christoforidis S et al. EEA1 links PI(3)K function to Rab5 regulation of endosome fusion [see comments]. Nature 1998; 394(6692):494–8.PubMedGoogle Scholar
  44. 44.
    Stenmark H, Aasland R, Driscoll PC. The phosphatidylinositol 3-phosphate-binding FYVE finger. FEBS Lett 2002; 513(1):77–84.PubMedGoogle Scholar
  45. 45.
    Wilson JM, de Hoop M, Zorzi N et al. EEA1, a tethering protein of the early sorting endosome, shows a polarized distribution in hippocampal neurons, epithelial cells, and fibroblasts. Mol Biol Cell 2000; 11(8):2657–71.PubMedGoogle Scholar
  46. 46.
    Christoforidis S, McBride HM, Burgoyne RD et al. The Rab5 effector EEA1 is a core component of endosome docking. Nature 1999; 397(6720):621–5.PubMedGoogle Scholar
  47. 47.
    Rubino M, Miaczynska M, Lippe R et al. Selective membrane recruitment of EEA1 suggests a role in directional transport of clathrin-coated vesicles to early endosomes. J Biol Chem 2000; 275(6):3745–8.PubMedGoogle Scholar
  48. 48.
    Simonsen A, Gaullier JM, D’Arrigo A et al. The Rab5 effector EEA1 interacts directly with syntaxin-6. J Biol Chem 1999; 274(41):28857–60.PubMedGoogle Scholar
  49. 49.
    Merithew E, Stone C, Eathiraj S et al. Determinants of Rab5 interaction with the N terminus of early endosome antigen 1. J Biol Chem 2003; 278(10):8494–500.PubMedGoogle Scholar
  50. 50.
    Haas AK, Fuchs E, Kopajtich R et al. A GTPase-activating protein controls Rab5 function in endocytic trafficking. Nat Cell Biol 2005; 7(9):887–93.PubMedGoogle Scholar
  51. 51.
    Webb GC, Zhang J, Garlow SJ et al. Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome. Molecular Biology Of The Cell 1997; 8(5):871–95.PubMedGoogle Scholar
  52. 52.
    Tall GG, Hama H, DeWald DB et al. The phosphatidylinositol 3-phosphate binding protein Vaclp interacts with a Rab GTPase and a Seclp homologue to facilitate vesicle-mediated vacuolar protein sorting. Mol Biol Cell 1999; 10(6):1873–89.PubMedGoogle Scholar
  53. 53.
    Peterson MR, Burd CG, Emr SD. Vac1p coordinates Rab and phosphatidylinositol 3-kinase signaling in Vps45p-dependent vesicle docking/fusion at the endosome. Curr Biol 1999; 9(3):159–62.PubMedGoogle Scholar
  54. 54.
    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. Developmental Cell 2001; 1(4):527–37.PubMedGoogle Scholar
  55. 55.
    Sacher M, Jiang Y, Barrowman J et al. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. EMBO J 1998; 17(9):2494–503.PubMedGoogle Scholar
  56. 56.
    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
  57. 57.
    Sacher M, Barrowman J, Schieltz D et al. Identification and characterization of five new subunits of TRAPP. Eur J Cell Biol 2000; 79(2):71–80.PubMedGoogle Scholar
  58. 58.
    Barrowman J, Sacher M, Ferro-Novick S. TRAPP stably associates with the Golgi and is required for vesicle docking. EMBO J 2000; 19(5):862–9.PubMedGoogle Scholar
  59. 59.
    Wang W, Sacher M, Ferro-Novick S. TRAPP stimulates guanine nucleotide exchange on Ypt1p. J Cell Biol 2000; 151(2):289–96.PubMedGoogle Scholar
  60. 60.
    Jones S, Newman C, Liu F et al. The TRAPP complex is a nucleotide exchanger for Ypt1 and Ypt31/32. Mol Biol Cell 2000; 11(12):4403–11.PubMedGoogle Scholar
  61. 61.
    Cai H, Zhang Y, Pypaert M et al. Mutants in trsl20 disrupt traffic from the early endosome to the late Golgi. J Cell Biol 2005; 171(5):823–33.PubMedGoogle Scholar
  62. 62.
    Sacher M, Ferro-Novick S. Purification of TRAPP from Saccharomyces cerevisiae and identification of its mammalian counterpart. Methods Enzymol 2001; 329:234–41.PubMedGoogle Scholar
  63. 63.
    Kim MS, Yi MJ, Lee KH et al. Biochemical and crystallographic studies reveal a specific interaction between TRAPP subunits Trs33p and Bet3p. Traffic 2005; 6(12):1183–95.PubMedGoogle Scholar
  64. 64.
    Kummel D, Muller JJ, Roske Y et al. The structure of the TRAPP subunit TPC6 suggests a model for a TRAPP subcomplex. EMBO Rep 2005; 6(8):787–93.PubMedGoogle Scholar
  65. 65.
    Kim YG, Sohn EJ, Seo J et al. Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP. Nat Struct Mol Biol 2005; 12(1):38–45.PubMedGoogle Scholar
  66. 66.
    Gecz J, Shaw MA, Bellon JR et al. Human wild-type SEDL protein functionally complements yeast Trs20p but some naturally occurring SEDL mutants do not. Gene 2003; 320:137–44.PubMedGoogle Scholar
  67. 67.
    Jang SB, Kim YG, Cho YS et al. Crystal structure of SEDL and its implications for a genetic disease spondyloepiphyseal dysplasia tarda. J Biol Chem 2002; 277(51):49863–9.PubMedGoogle Scholar
  68. 68.
    Suvorova ES, Kurten RC, Lupashin W. Identification of a human orthologue of Sec34p as a component of the cis-Golgi vesicle tethering machinery. J Biol Chem 2001; 276(25):22810–8.PubMedGoogle Scholar
  69. 69.
    Ungar D, Oka T, Brittle EE et al. Characterization of a mammalian Golgi-localized protein complex, COG, that is required for normal Golgi morphology and function. J Cell Biol 2002; 157(3):405–15.PubMedGoogle Scholar
  70. 70.
    Ram RJ, Li B, Kaiser CA. Identification of sec36p, sec37p, and sec38p: Components of yeast complex that contains sec34p and sec35p. Mol Biol Cell 2002; 13(5):1484–500.PubMedGoogle Scholar
  71. 71.
    Fotso P, Koryakina Y, Pavliv O et al. Coglp plays a central role in the organization of the yeast conserved oligomeric golgi complex. J Biol Chem 2005; 280(30):27613–23.PubMedGoogle Scholar
  72. 72.
    Oka T, Vasile E, Penman M et al. Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: Studies of COG5-and COG7-deficient mammalian cells. J Biol Chem 2005; 280(38):32736–45.PubMedGoogle Scholar
  73. 73.
    Ungar D, Oka T, Vasile E et al. Subunit architecture of the conserved oligomeric golgi complex. J Biol Chem 2005; 280(38):32729–35.PubMedGoogle Scholar
  74. 74.
    Fotso P, Koriakina Y, Lupashin V. Coglp plays a central role in the organization of the yeast Conserved Oligomeric Golgi (COG) complex. Mol Biol Cell 2004; 15:460A–461A.Google Scholar
  75. 75.
    VanRheenen SM, Cao X, Lupashin W et al. Sec35p, a novel peripheral membrane protein, is required for ER to Golgi vesicle docking. J Cell Biol 1998; 141(5):1107–19.PubMedGoogle Scholar
  76. 76.
    VanRheenen SM, Cao X, Sapperstein SK et al. Sec34p, a protein required for vesicle tethering to the yeast Golgi apparatus, is in a complex with Sec35p. J Cell Biol 1999; 147(4):729–42.PubMedGoogle Scholar
  77. 77.
    Suvorova ES, Duden R, Lupashin W. The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteins. Journal of Cell Biology 2002; 157(4):631–43.PubMedGoogle Scholar
  78. 78.
    Walter DM, Paul KS, Waters MG. Purification and characterization of a novel 13 S hetero-oligomeric protein complex that stimulates in vitro Golgi transport. J Biol Chem 1998; 273(45):29565–76.PubMedGoogle Scholar
  79. 79.
    Kim DW, Massey T, Sacher M et al. Sgf1p, a new component of the Sec34p/Sec35p complex. Traffic 2001; 2(11):820–30.PubMedGoogle Scholar
  80. 80.
    Zolov SN, Lupashin W. Cog3p depletion blocks vesicle-mediated Golgi retrograde trafficking in HeLa cells. Journal of Cell Biology 2005; 168(5):747–59.PubMedGoogle Scholar
  81. 81.
    Wuestehube LJ, Duden R, Eun A et al. New mutants of Saccharomyces cerevisiae affected in the transport of proteins from the endoplasmic reticulum to the Golgi complex. Genetics 1996; 142:393–406.PubMedGoogle Scholar
  82. 82.
    Spelbrink RG, Nothwehr SF. The yeast GRD20 gene is required for protein sorting in the trans-Golgi network/endosomal system and for polarization of the actin cytoskeleton. Mol Biol Cell 1999; 10(12):4263–81.PubMedGoogle Scholar
  83. 83.
    Morsomme P, Riezman H. The Rab GTPase Yptlp and tethering factors couple protein sorting at the ER to vesicle targeting to the Golgi apparatus. Dev Cell 2002; 2(3):307–17.PubMedGoogle Scholar
  84. 84.
    Ungar D, Oka T, Krieger M et al. Retrograde transport on the COG railway. Trends Cell Biol 2006; 16(2): 113–20.PubMedGoogle Scholar
  85. 85.
    Farkas RM, Giansanti MG, Gatti M et al. The Drosophila Cog5 homologue is required for cytokinesis, cell elongation, and assembly of specialized Golgi architecture during spermatogenesis. Mol Biol Cell 2003; l4(l):190–200.Google Scholar
  86. 86.
    Podos SD, Reddy P, Ashkenas J et al. LDLC encodes a brefeldin A-sensitive, peripheral Golgi protein required for normal Golgi function. J Cell Biol 1994; 127(3):679–91.PubMedGoogle Scholar
  87. 87.
    Wu X, Steet RA, Bohorov O et al. Mutation of the COG complex subunit gene COG7 causes a lethal congenital disorder. Nat Med 2004; 10(5):518–23.PubMedGoogle Scholar
  88. 88.
    Foulquier F, Vasile E, Schollen E et al. Conserved oligomeric Golgi complex subunit 1 deficiency reveals a previously uncharacterized congenital disorder of glycosylation type II. Proc Natl Acad Sci USA 2006; 103(10):3764–9.PubMedGoogle Scholar
  89. 89.
    Harris SL, Waters MG. Localization of a yeast early Golgi mannosyltransferase, Ochlp, involves retrograde transport. J Cell Biol 1996; 132:985–98.PubMedGoogle Scholar
  90. 90.
    Opat AS, Houghton F, Gleeson PA. Steady-state localization of a medial-Golgi glycosyltransferase involves transit through the trans-Golgi network. Biochem J 2001; 358(Pt l):33–40.PubMedGoogle Scholar
  91. 91.
    Shestakova A, Zolov S, Lupashin V. COG complex-mediated recycling of Golgi glycosyltransferases is essential for normal protein glycosylation. Traffic 2006; 7(2): 191–204.PubMedGoogle Scholar
  92. 92.
    Oka T, Ungar D, Hughson FM et al. The COG and COPI complexes interact to control the abundance of GEARs, a subset of Golgi integral membrane proteins. Mol Biol Cell 2004; 15(5):2423–35.PubMedGoogle Scholar
  93. 93.
    Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 1980; 21(1):205–15.Google Scholar
  94. 94.
    TerBush DR, Maurice T, Roth D et al. The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 1996; 15:6483–94.PubMedGoogle Scholar
  95. 95.
    Hamburger ZA, Hamburger AE, West Jr AP et al. Crystal structure of the S.cerevisiae exocyst component Exo70p. J Mol Biol 2006; 356(1):9–21.PubMedGoogle Scholar
  96. 96.
    Dong G, Hutagalung AH, Fu C et al. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol 2005; 12(12): 1094–100.PubMedGoogle Scholar
  97. 97.
    Finger FP, Hughes TE, Novick P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 1998; 92(4):559–71.PubMedGoogle Scholar
  98. 98.
    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(4):1071–80.PubMedGoogle Scholar
  99. 99.
    Boyd C, Hughes T, Pypaert M et al. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J Cell Biol 2004; 167(5):889–901.PubMedGoogle Scholar
  100. 100.
    France YE, Boyd C, Coleman J et al. The polarity-establishment component Bemlp interacts with the exocyst complex through the Secl5p subunit. J Cell Sci 2006; 119(Pt 5):876–88.PubMedGoogle Scholar
  101. 101.
    Rogers KK, Wilson PD, Snyder RW et al. The exocyst localizes to the primary cilium in MDCK cells. Biochem Biophys Res Commun 2004; 319(1): 138–43.PubMedGoogle Scholar
  102. 102.
    Wang L, Li G, Sugita S. RalA-exocyst interaction mediates GTP-dependent exocytosis. J Biol Chem 2004; 279(19):19875–81.PubMedGoogle Scholar
  103. 103.
    Shin DM, Zhao XS, Zeng W et al. The mammalian Sec6/8 complex interacts with Ca(2+) signaling complexes and regulates their activity. J Cell Biol 2000; 150(5): 1101–12.PubMedGoogle Scholar
  104. 104.
    Hsu SC, Hazuka CD, Roth R et al. Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments. Neuron 1998; 20(6): 1111–22.PubMedGoogle Scholar
  105. 105.
    Grindstaff KK, Yeaman C, Anandasabapathy N et al. Sec6/8 complex is recruited to cell-cell contacts and specifies transport vesicle delivery to the basal-lateral membrane in epithelial cells. Cell 1998; 93(5):731–40.PubMedGoogle Scholar
  106. 106.
    Yeaman C, Grindstaff KK, Nelson WJ. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J Cell Sci 2004; 117(Pt 4):559–70.PubMedGoogle Scholar
  107. 107.
    Murthy M, Garza D, Scheller RH et al. Mutations in the exocyst component sec5 disrupt neu-ronal membrane traffic, but neurotransmitter release persists. Neuron 2003; 37(3):433–47.PubMedGoogle Scholar
  108. 108.
    Murthy M, Schwarz TL. The exocyst component Sec5 is required for membrane traffic and polarity in the Drosophila ovary. Development 2004; 131(2):377–88.PubMedGoogle Scholar
  109. 109.
    Wu SY, Mehta SQ, Pichaud F et al. Sec 15 interacts with Rab 11 via a novel domain and affects Rabll localization in vivo. Nature Structural and Molecular Biology 2005; 12(10):879–85.Google Scholar
  110. 110.
    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
  111. 111.
    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
  112. 112.
    Moskalenko S, Henry DO, Rosse C et al. The exocyst is a Ral effector complex. Nat Cell Biol 2002; 4(l):66–72.PubMedGoogle Scholar
  113. 113.
    Medkova M, France YE, Coleman J et al. The rab exchange factor Sec2p reversibly associates with the exocyst. Mol Biol Cell 2006; 17(6):2757–69.PubMedGoogle Scholar
  114. 114.
    Fukai S, Matern HT, Jagath JR et al. Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. EMBO J 2003; 22(13):3267–78.PubMedGoogle Scholar
  115. 115.
    Moskalenko S, Tong C, Rosse C et al. Ral GTPases regulate exocyst assembly through dual subunit interactions. J Biol Chem 2003; 278(51):51743–8.PubMedGoogle Scholar
  116. 116.
    Peterson MR, Emr SD. The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic 2001; 2(7):476–86.PubMedGoogle Scholar
  117. 117.
    Rieder SE, Banta LM, Kohrer K et al. Multilamellar endosome-like compartment accumulates in the yeast vps28 vacuolar protein sorting mutant. Mol Biol Cell 1996; 7(6):985–99.PubMedGoogle Scholar
  118. 118.
    Srivastava A, Woolford CA, Jones EW. Pep3p/Pep5p complex: A putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae. Genetics 2000; 156(l):105–22.PubMedGoogle Scholar
  119. 119.
    Raymond CK, Howald-Stevenson I, Vater CA et al. Morphological classification of the yeast vacuolar protein sorting mutants: Evidence for a prevacuolar compartment in class E vps mutants. Mol Biol Cell 1992; 3(12):1389–402.PubMedGoogle Scholar
  120. 120.
    Rieder SE, Emr SD. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol Biol Cell 1997; 8(ll):2307–27.PubMedGoogle Scholar
  121. 121.
    Sevrioukov EA, He JP, Moghrabi N et al. A role for the deep orange and carnation eye color genes in lysosomal delivery in Drosophila. Mol Cell 1999; 4(4):479–86.PubMedGoogle Scholar
  122. 122.
    Caplan S, Hartnell LM, Aguilar RC et al. Human Vam6p promotes lysosome clustering and fusion in vivo. J Cell Biol 2001; 154(l):109–22.PubMedGoogle Scholar
  123. 123.
    Kim BY, Kramer H, Yamamoto A et al. Molecular characterization of mammalian homologues of class C Vps proteins that interact with syntaxin-7. J Biol Chem 2001; 276(31):29393–402.PubMedGoogle Scholar
  124. 124.
    Robinson JS, Graham TR, Emr SD. A putative zinc finger protein, Saccharomyces cerevisiae Vpsl8p, affects late Golgi functions required for vacuolar protein sorting and efficient alpha-factor prohormone maturation. Mol Cell Biol 1991; ll(12):5813–24.Google Scholar
  125. 125.
    Ybe JA, Brodsky FM, Hofmann K et al. Clathrin self-assembly is mediated by a tandemly repeated superhelix. Nature 1999; 399(6734):371–5.PubMedGoogle Scholar
  126. 126.
    Wurmser AE, Sato TK, Emr SD. New component of the vacuolar class C-Vps complex couples nucleotide exchange on the Ypt7 GTPase to SNARE-dependent docking and fusion. J Cell Biol 2000; 151(3):551–62.PubMedGoogle Scholar
  127. 127.
    Seals DF, Eitzen G, Margolis N et al. A Ypt/Rab effector complex containing the Seel homolog Vps33p is required for homotypic vacuole fusion. Proc Natl Acad Sci USA 2000; 97(17):9402–7.PubMedGoogle Scholar
  128. 128.
    Banta LM, Vida TA, Herman PK et al. Characterization of yeast Vps33p, a protein required for vacuolar protein sorting and vacuole biogenesis. Mol Cell Biol 1990; 10(9):4638–49.Google Scholar
  129. 129.
    Stroupe C, Collins KM, Fratti RA et al. Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p. EMBO J 2006; 25(8): 1579–89.PubMedGoogle Scholar
  130. 130.
    Laage R, Ungermann C. The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion. Mol Biol Cell 2001; 12(ll):3375–85.PubMedGoogle Scholar
  131. 131.
    Wang L, Merz AJ, Collins KM et al. Hierarchy of protein assembly at the vertex ring domain for yeast vacuole docking and fusion. J Cell Biol 2003; 160(3):365–74.PubMedGoogle Scholar
  132. 132.
    Collins KM, Thorngren NL, Fratti RA et al. Secl7p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J 2005; 24(10): 1775–86.PubMedGoogle Scholar
  133. 133.
    Conibear E, Stevens TH. Vps52p, Vps53p, and Vps54p form a novel multisubunit complex required for protein sorting at the yeast late Golgi. Mol Biol Cell 2000; ll(l):305–23.Google Scholar
  134. 134.
    Liewen H, Meinhold-Heerlein I, Oliveira V et al. Characterization of the human GARP (Golgi associated retrograde protein) complex. Exp Cell Res 2005; 306(1 ):24–34.PubMedGoogle Scholar
  135. 135.
    Siniossoglou S, Pelham HR. An effector of Ypt6p binds the SNARE Tlglp and mediates selective fusion of vesicles with late Golgi membranes. EMBO J 2001; 20(21):5991–8.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.
    Conibear E, Cleck JN, Stevens TH. Vps51p mediates the association of the GARP (Vps52/53/54) complex with the late Golgi t-SNARE Tlglp. Mol Biol Cell 2003; l4(4):1610–23.Google Scholar
  138. 138.
    Kim KA, von Zastrow M. Neurotrophin-regulated sorting of opioid receptors in the biosynthetic pathway of neurosecretory cells. J Neurosci 2003; 23(6):2075–85.Google Scholar
  139. 139.
    Barr FA, Puype M, Vandekerckhove J et al. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 1997; 91(2):253–62.Google Scholar
  140. 140.
    Barr FA, Nakamura N, Warren G. Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J 1998; 17(12):3258–68.Google Scholar
  141. 141.
    Puthenveedu MA, Bachert C, Puri S et al. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat Cell Biol 2006; 8(3):238–48.PubMedGoogle Scholar
  142. 142.
    Kim DW. Characterization of Grplp, a novel cis-Golgi matrix protein. Biochem Biophys Res Commun 2003; 303(l):370–8.PubMedGoogle Scholar
  143. 143.
    Kim DW, Sacher M, Scarpa A et al. High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p> a protein implicated in vesicle docking. Mol Biol Cell 1999; 10(10):3317–29.PubMedGoogle Scholar
  144. 144.
    Short B, Preisinger C, Korner R et al. A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J Cell Biol 2001; 155(6):877–83.PubMedGoogle Scholar
  145. 145.
    Derby MC, van Vilet C, Brown D et al. Mammalian GRIP domain proteins differ in their membrane binding properties and are recruited to distinct domains of the TGN. J Cell Sci 2004; 117(24):5865–74.PubMedGoogle Scholar
  146. 146.
    Lu L, Tai G, Hong W. Autoantigen Golgin-97, an effector of Aril GTPase, participates in traffic from the endosome to the trans-golgi network. Mol Biol Cell 2004; 15(10):4426–43.PubMedGoogle Scholar
  147. 147.
    Reilly BA, Kraynack BA, VanRheenen SM et al. Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsllp, a component of the ER target site that interacts with a COPI coat subunit. Mol Biol Cell 2001; 12(12):3783–96.PubMedGoogle Scholar
  148. 148.
    Kraynack BA, Chan A, Rosenthal E et al. Dsllp, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol Biol Cell 2005; l6(9):3963–77.Google Scholar
  149. 149.
    Vanrheenen SM, Reilly BA, Chamberlain SJ et al. Dsllp, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast. Traffic 2001; 2(3):212–31.PubMedGoogle Scholar
  150. 150.
    Andag U, Neumann T, Schmitt HD. The coatomer-interacting protein dsllp is required for golgi-to-endoplasmic reticulum retrieval in yeast. J Biol Chem 2001; 276(42):39150–60.PubMedGoogle Scholar
  151. 151.
    Andag U, Schmitt HD. Dsllp, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J Biol Chem 2003; 278(51):51722–34.PubMedGoogle Scholar
  152. 152.
    Hirose H, Arasaki K, Dohmae N et al. Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi. EMBO J 2004; 23(6): 1267–78.PubMedGoogle Scholar
  153. 153.
    Arasaki K, Taniguchi M, Tani K et al. RINT-1 regulates the localization and entry of ZW10 to the syntaxin 18 complex. Mol Biol Cell 2006.Google Scholar
  154. 154.
    Orci L, Perrelet A, Rothman JE. Vesicles on strings: Morphological evidence for processive transport within the Golgi stack. Proc Natl Acad Sci USA 1998; 95(5):2279–83.PubMedGoogle Scholar
  155. 155.
    Marra P, Maffucci T, Daniele T et al. The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment. Nat Cell Biol 2001; 3(12):1101–13.PubMedGoogle Scholar
  156. 156.
    Darsow T, Rieder SE, Emr SD. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Cell Biol 1997; 138(3):517–29.PubMedGoogle Scholar
  157. 157.
    Sato TK, Rehling P, Peterson MR et al. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol Cell 2000; 6(3):661–71.PubMedGoogle Scholar
  158. 158.
    Roti EC, Myers CD, Ayers RA et al. Interaction with GM130 during HERG ion channel trafficking. Disruption by type 2 congenital long QT syndrome mutations. Human Ether-a-go-go-Related Gene. J Biol Chem 2002; 277(49):47779–85.Google Scholar
  159. 159.
    Kuo A, Zhong C, Lane WS et al. Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. EMBO J 2000; 19(23):6427–39.PubMedGoogle Scholar
  160. 160.
    Hoogenraad CC, Akhmanova A, Howell SA et al. Mammalian Golgi-associated Bicaudal-D2 functions in the dynein-dynactin pathway by interacting with these complexes. EMBO J 2001 20(15):404l–54.Google Scholar
  161. 161.
    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
  162. 162.
    Matanis T, Akhmanova A, Wulf P 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.Google Scholar
  163. 163.
    Young J, Stauber T, del Nery E et al. Regulation of microtubule-dependent recycling at the trans-Golgi network by Rab6A and Rab6A Mol Biol Ceil 2005; 16(l):l62–77.Google Scholar
  164. 164.
    Barr FA. A novel Rab6-interacting domain defines a family of Golgi-targeted coiled-coil proteins. Curr Biol 1999; 9(7):381–4.PubMedGoogle Scholar
  165. 165.
    Fritzler MJ, Hamel JC, Ochs RL et al. Molecular characterization of two human autoantigens: Unique cDNAs encoding 95-and 160-kD proteins of a putative family in the Golgi complex. J Exp Med 1993; 178(l):49–62.PubMedGoogle Scholar
  166. 166.
    Nakamura N, Lowe M, Levine TP et al. The vesicle docking protein pi 15 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 1997; 89:445–55.PubMedGoogle Scholar
  167. 167.
    Preisinger C, Short B, De Corte V et al. YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate l4-3-3zeta. J Cell Biol 2004; 164(7): 1009–20.PubMedGoogle Scholar
  168. 168.
    Valsdottir R, Hashimoto H, Ashman K et al. 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.PubMedGoogle Scholar
  169. 169.
    Rios RM, Sanchis A, Tassin AM et al. GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation. Cell 2004; 118(3):323–35.Google Scholar
  170. 170.
    Abe A, Emi N, Tanimoto M et al. Fusion of the platelet-derived growth factor receptor beta to a novel gene CEV14 in acute myelogenous leukemia after clonal evolution. Blood 1997; 90(11):4271–7.PubMedGoogle Scholar
  171. 171.
    Gillingham AK, Tong AH, Boone C et al. The GTPase Arflp and the ER to Golgi cargo receptor Ervl4p cooperate to recruit the golgin Rud3p to the cis-Golgi. J Cell Biol 2004; l67(2):281–92.Google Scholar
  172. 172.
    Barr FA, Short B. Golgins in the structure and dynamics of the Golgi apparatus. Curr Opin Cell Biol 2003; 15(4):405–13.Google Scholar
  173. 173.
    Lu L, Hong W. Interaction of Arll-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol Biol Cell 2003; 14(9):3767–81.PubMedGoogle Scholar
  174. 174.
    Luke MR, Kjer-Nielsen L, Brown DL et al. GRIP domain-mediated targeting of two new coiled-coil proteins, GCC88 and GCC185, to subcompartments of the trans-Golgi network. J Biol Chem 2003; 278(6):4216–26.PubMedGoogle Scholar
  175. 175.
    Munro S, Nichols BJ. The GRIP domain — A novel Golgi-targeting domain found in several coiled-coil proteins. Curr Biol 1999; 9(7):377–80.PubMedGoogle Scholar
  176. 176.
    Gleeson PA, Anderson TJ, Stow JL et al. p230 is associated with vesicles budding from the trans-Golgi network. J Cell Sci 1996; 109(Pt 12):2811–21.PubMedGoogle Scholar
  177. 177.
    Van Valkenburgh H, Shern JF, Sharer JD et al. ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific and shared effectors: Characterizing ARL1-binding proteins. J Biol Chem 2001; 276(25):22826–37.PubMedGoogle Scholar
  178. 178.
    Kjer-Nielsen L, Teasdale RD, van Vliet C et al. A novel Golgi-localisation domain shared by a class of coiled-coil peripheral membrane proteins. Curr Biol 1999; 9(7):385–8.PubMedGoogle Scholar
  179. 179.
    Siniossoglou S, Peak-Chew SY, Pelham HR. Riclp and Rgplp form a complex that catalyses nucleotide exchange on Ypt6p. EMBO J 2000; 19(18):4885–94.Google Scholar
  180. 180.
    Tsukada M, Will E, Gallwitz D. Structural and functional analysis of a novel coiled-coil protein involved in Ypt6 GTPase-regulated protein transport in yeast. Mol Biol Cell 1999; 10(l):63–75.PubMedGoogle Scholar
  181. 181.
    Shorter J, Watson R, Giannakou ME et al. GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J 1999; 18(18):4949–60.Google Scholar
  182. 182.
    Barr FA, Preisinger C, Kopajtich R et al. Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J Cell Biol 2001; 155(6):885–91.PubMedGoogle Scholar
  183. 183.
    Yoshimura S, Yamamoto A, Misumi Y et al. Dynamics of golgi matrix proteins after the blockage of ER to golgi transport. J Biochem (Tokyo) 2004; 135(2):201–16.Google Scholar
  184. 184.
    Jesch SA, Lewis TS, Ahn NG et al. Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2. Mol Biol Cell 2001; 12(6):1811–7.PubMedGoogle Scholar
  185. 185.
    Brandon E, Gao Y, Garcia-Mata R et al. Membrane targeting of pi 15 phosphorylation mutants and their effects on Golgi integrity and secretory traffic. Eur J Cell Biol 2003; 82(8):4ll–20.Google Scholar
  186. 186.
    Garcia-Mata R, Sztul E. The membrane-tethering protein pi 15 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. EMBO Rep 2003; 4(3):320–5.PubMedGoogle Scholar
  187. 187.
    Lupashin W, Hamamoto S, Schekman RW. Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J Cell Biol 1996; 132(3):277–89.PubMedGoogle Scholar
  188. 188.
    Chatterton JE, Hirsch D, Schwartz JJ et al. Expression cloning of LDLB, a gene essential for normal Golgi function and assembly of the ldlCp complex. Proc Natl Acad Sci USA 1999; 96(3):915–20.PubMedGoogle Scholar
  189. 189.
    Cosson P, Schroder-Kohne S, Sweet DS et al. The Sec20/Tip20p complex is involved in ER retrieval of dilysine-tagged proteins. Eur J Cell Biol 1997; 73(2):93–7.PubMedGoogle Scholar
  190. 190.
    Nakajima K, Hirose H, Taniguchi M et al. Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion. EMBO J 2004; 23(l6):3216–26.PubMedGoogle Scholar
  191. 191.
    TerBush DR, Novick P. Sec6, Sec8, and Seel 5 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J Cell Biol 1995; 130:299–312.PubMedGoogle Scholar
  192. 192.
    Kee Y, Yoo JS, Hazuka CD et al. Subunit structure of the mammalian exocyst complex. Proc Natl Acad Sci USA 1997; 94(26): 14438–43.PubMedGoogle Scholar
  193. 193.
    Matern HT, Yeaman C, Nelson WJ et al. The Sec6/8 complex in mammalian cells: Characterization of mammalian Sec3, subunit interactions, and expression of subunits in polarized cells. Proc Natl Acad Sci USA 2001; 98(17):9648–53.PubMedGoogle Scholar
  194. 194.
    Guo W, Roth D, Gatti E et al. Identification and characterization of homologues of the Exocyst component SeclOp. Febs Letters 1997; 404(2-3): 135–9.PubMedGoogle Scholar
  195. 195.
    Siniossoglou S, Pelham HR. Vps51p links the VFT complex to the SNARE Tlglp. J Biol Chem 2002; 277(50):48318–24.PubMedGoogle Scholar
  196. 196.
    Walter L, Stark S, Helou K et al. Identification, characterization and cytogenetic mapping of a yeast Vps54 homolog in rat and mouse. Gene 2002; 285(l-2):213–20.PubMedGoogle Scholar
  197. 197.
    Preston RA, Manolson MF, Becherer K et al. Isolation and characterization of PEP3, a gene required for vacuolar biogenesis in Saccharomyces cerevisiae. Mol Cell Biol 1991; 11(12):5801–12.Google Scholar
  198. 198.
    Preston RA, Reinagel PS, Jones EW. Genes required for vacuolar acidity in Saccharomyces cerevisiae. Genetics 1992; 131(3):551–8.Google Scholar
  199. 199.
    Nakamura N, Hirata A, Ohsumi Y et al. Vam2/Vps4lp and Vam6/Vps39p are components of a protein complex on the vacuolar membranes and involved in the vacuolar assembly in the yeast Saccharomyces cerevisiae. J Biol Chem 1997; 272(17):11344–9.PubMedGoogle Scholar
  200. 200.
    Horazdovsky BF, Emr SD. The VPS 16 gene product associates with a sedimentable protein complex and is essential for vacuolar protein sorting in yeast. J Biol Chem 1993; 268(7):4953–62.PubMedGoogle Scholar
  201. 201.
    Rossi G, Kolstad K, Stone S et al. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Mol Biol Cell 1995; 6:1769–80.PubMedGoogle Scholar
  202. 202.
    Jiang Y, Scarpa A, Zhang L et al. A high copy suppressor screen reveals genetic interactions between BET3 and a new gene. Evidence for a novel complex in ER-to-Golgi transport. Genetics 1998; 149(2):833–41.PubMedGoogle Scholar
  203. 203.
    Kauppi M, Simonsen A, Bremnes B et al. The small GTPase Rab22 interacts with EEA1 and controls endosomal membrane trafficking. J Cell Sci 2002; 115(Pt 5):899–911.PubMedGoogle Scholar
  204. 204.
    Frigerio G. The Saccharomyces cerevisiae early secretion mutant tip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufelp. Yeast 1998; l4(7):633–46.Google Scholar
  205. 205.
    Lewis MJ, Rayner JC, Pelham HR. A novel SNARE complex implicated in vesicle fusion with the endoplasmic reticulum. EMBO Journal 1997; 16(ll):3017–24.PubMedGoogle Scholar
  206. 206.
    McBride HM, Rybin V, Murphy C et al. Oligomeric complexes link Rab5 effectors with NSF and drive membrane fusion via interactions between EEA1 and syntaxin 13. Cell 1999; 98(3):377–86.PubMedGoogle Scholar
  207. 207.
    Sivaram MV, Saporita JA, Furgason ML et al. Dimerization of the exocyst protein Sec6p and its interaction with the t-SNARE Sec9p. Biochemistry 2005; 44(16):6302–11.PubMedGoogle Scholar
  208. 208.
    Price A, Seals D, Wickner W et al. The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein. J Cell Biol 2000; 148(6): 1231–8.PubMedGoogle Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  1. 1.Department of Cell BiologyUniversity of Alabama at BirminghamBirminghamUSA
  2. 2.Department of Physiology and BiophysicsUniversity of Arkansas for Medical SciencesLittle RockUSA

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