Gene Symbol: SEC17
Description: Sec17p
Alias: RNS3, Sec17p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Mima J, Hickey C, Xu H, Jun Y, Wickner W. Reconstituted membrane fusion requires regulatory lipids, SNAREs and synergistic SNARE chaperones. EMBO J. 2008;27:2031-42 pubmed publisher
    The homotypic fusion of yeast vacuoles, each with 3Q- and 1R-SNARE, requires SNARE chaperones (Sec17p/Sec18p and HOPS) and regulatory lipids (sterol, diacylglycerol and phosphoinositides)...
  2. Collins K, Thorngren N, Fratti R, Wickner W. Sec17p and HOPS, in distinct SNARE complexes, mediate SNARE complex disruption or assembly for fusion. EMBO J. 2005;24:1775-86 pubmed
    ..Vacuole SNARE complexes bind either Sec17p or the HOPS complex, but not both. Sec17p and its co-chaperone Sec18p disassemble SNARE complexes...
  3. Holthuis J, Nichols B, Dhruvakumar S, Pelham H. Two syntaxin homologues in the TGN/endosomal system of yeast. EMBO J. 1998;17:113-26 pubmed
    ..However, neither is required for intra-Golgi traffic. Since no further syntaxins have been identified in yeast, this implies that the Golgi apparatus can function with a single syntaxin, Sed5p. ..
  4. Peng R, Gallwitz D. Sly1 protein bound to Golgi syntaxin Sed5p allows assembly and contributes to specificity of SNARE fusion complexes. J Cell Biol. 2002;157:645-55 pubmed
    ..This indicates for the first time that a Sec1 family member contributes to the specificity of SNARE complex assembly. ..
  5. Søgaard M, Tani K, Ye R, Geromanos S, Tempst P, Kirchhausen T, et al. A rab protein is required for the assembly of SNARE complexes in the docking of transport vesicles. Cell. 1994;78:937-48 pubmed
  6. Ungermann C, Nichols B, Pelham H, Wickner W. A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion. J Cell Biol. 1998;140:61-9 pubmed
    Homotypic vacuole fusion in yeast requires Sec18p (N-ethylmaleimide-sensitive fusion protein [NSF]), Sec17p (soluble NSF attachment protein [alpha-SNAP]), and typical vesicle (v) and target membrane (t) SNAP receptors (SNAREs)...
  7. Peters C, Baars T, Buhler S, Mayer A. Mutual control of membrane fission and fusion proteins. Cell. 2004;119:667-78 pubmed
    ..This activity is independent of the SNARE coactivator Sec17p/alpha-SNAP and of the v-SNARE...
  8. Haas A, Wickner W. Homotypic vacuole fusion requires Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF). EMBO J. 1996;15:3296-305 pubmed
    ..Here we demonstrate, using affinity-purified antibodies and purified recombinant proteins, a requirement for Sec17p (yeast alpha-SNAP) and Sec18p (yeast NSF) in homotypic vacuole fusion in vitro...
  9. Rossi G, Salminen A, Rice L, Brunger A, Brennwald P. Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9. J Biol Chem. 1997;272:16610-7 pubmed
    ..recombinant forms of the yeast exocytic SNARE proteins Snc1, Sso1, and Sec9 and the yeast alpha-SNAP homolog, Sec17. Despite the low level of sequence identity, the association properties of the yeast and neuronal complexes are ..

More Information


  1. Lupashin V, Pokrovskaya I, McNew J, Waters M. Characterization of a novel yeast SNARE protein implicated in Golgi retrograde traffic. Mol Biol Cell. 1997;8:2659-76 pubmed
    ..Vti1p can bind Sec17p (yeast SNAP) and enter into a Sec18p (NSF)-sensitive complex with the cis-Golgi t-SNARE Sed5p...
  2. Ungermann C, Wickner W. Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion. EMBO J. 1998;17:3269-76 pubmed
    The vacuole v-t-SNARE complex is disassembled by Sec17p/alpha-SNAP and Sec18p/NSF prior to vacuole docking and fusion. We now report a functional characterization of the vacuolar SNARE Vam7p, a SNAP-25 homolog...
  3. Sato K, Wickner W. Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex. Science. 1998;281:700-2 pubmed
    ..Thus, solubilized integral membrane components can be reconstituted for priming, docking, and fusion steps of organelle trafficking. ..
  4. Xu H, Jun Y, Thompson J, Yates J, Wickner W. HOPS prevents the disassembly of trans-SNARE complexes by Sec17p/Sec18p during membrane fusion. EMBO J. 2010;29:1948-60 pubmed publisher
    ..complex disassembly and assembly might be thought to be opposing reactions, the proteins promoting disassembly (Sec17p/Sec18p) and assembly (the HOPS complex) work synergistically to support fusion...
  5. Ungermann C, von Mollard G, Jensen O, Margolis N, Stevens T, Wickner W. Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion. J Cell Biol. 1999;145:1435-42 pubmed
    ..Our data show that vacuole-vacuole fusion requires a cis-SNARE complex of five SNAREs, the t-SNAREs Vam3p and Vam7p and the v-SNAREs Nyv1p, Vti1p, and Ykt6p. ..
  6. Jackson C, Kepes F. BFR1, a multicopy suppressor of brefeldin A-induced lethality, is implicated in secretion and nuclear segregation in Saccharomyces cerevisiae. Genetics. 1994;137:423-37 pubmed
    ..BFR1, that, in addition, partially suppresses the growth and secretion defects of the ER-to-Golgi secretion mutant sec17. A bfr1-delta 1::URA3 deletion strain is viable, but has defects in cell morphology and nuclear segregation, and ..
  7. Lupashin V, Hamamoto S, Schekman R. Biochemical requirements for the targeting and fusion of ER-derived transport vesicles with purified yeast Golgi membranes. J Cell Biol. 1996;132:277-89 pubmed
    ..A model for the sequential involvement of these components in the targeting and fusion reaction is proposed. ..
  8. Xu H, Wickner W. Bem1p is a positive regulator of the homotypic fusion of yeast vacuoles. J Biol Chem. 2006;281:27158-66 pubmed
    ..2005) Genes Dev. 19, 2606-2618), we did not find phosphorylation of Bem1p at Ser-72 to be required for Bem1p-stimulated fusion. Taken together, Bem1p is a positive regulator of lipid mixing during vacuole hemifusion and fusion. ..
  9. Gerst J. Conserved alpha-helical segments on yeast homologs of the synaptobrevin/VAMP family of v-SNAREs mediate exocytic function. J Biol Chem. 1997;272:16591-8 pubmed
    ..and to interact genetically with components of the proposed fusion complex: the Sec9 and Sso2 t-SNAREs and the Sec17 alpha-SNAP homolog...
  10. McNew J, Coe J, Søgaard M, Zemelman B, Wimmer C, Hong W, et al. Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport. FEBS Lett. 1998;435:89-95 pubmed
    ..Close examination of the secretory phenotype of GOS1-disrupted cells suggests that Gos1p may play a role in multiple transport steps, specifically ER-Golgi and/or intra-Golgi transport. ..
  11. Burri L, Varlamov O, Doege C, Hofmann K, Beilharz T, Rothman J, et al. A SNARE required for retrograde transport to the endoplasmic reticulum. Proc Natl Acad Sci U S A. 2003;100:9873-7 pubmed
    ..We suggest that Slt1 is a component of the SNAREpin required for retrograde traffic to the ER. Based on the previously reported association with Ufe1 and Sec22, Sec20 likely contributes the fourth SNARE to the SNAREpin. ..
  12. Kim D, Sacher M, Scarpa A, Quinn A, Ferro Novick S. High-copy suppressor analysis reveals a physical interaction between Sec34p and Sec35p, a protein implicated in vesicle docking. Mol Biol Cell. 1999;10:3317-29 pubmed
    ..Sec34p and Sec35p stably associate with each other to form a multiprotein complex of approximately 480 kDa. These data indicate that Sec34p acts in conjunction with Sec35p to mediate a common step in vesicular traffic. ..
  13. Dietrich L, LaGrassa T, Rohde J, Cristodero M, Meiringer C, Ungermann C. ATP-independent control of Vac8 palmitoylation by a SNARE subcomplex on yeast vacuoles. J Biol Chem. 2005;280:15348-55 pubmed
    ..We speculate that during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a novel function in Vac8 palmitoylation. ..
  14. Desfougères Y, Neumann H, Mayer A. Organelle size control - increasing vacuole content activates SNAREs to augment organelle volume through homotypic fusion. J Cell Sci. 2016;129:2817-28 pubmed publisher
    ..These results suggest that cells can adapt the volume of vacuoles to their content through feedback from the vacuole lumen to the SNAREs on the cytosolic surface of the organelle. ..
  15. Schindler C, Spang A. Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF. Mol Biol Cell. 2007;18:2852-63 pubmed
    ..of alpha-soluble N-ethylmaleimide-sensitive factor attachment protein and N-ethylmaleimide-sensitive factor, Sec17p and Sec18p, respectively...
  16. Wiederhold E, Gandhi T, Permentier H, Breitling R, Poolman B, Slotboom D. The yeast vacuolar membrane proteome. Mol Cell Proteomics. 2009;8:380-92 pubmed publisher
    ..Our work provides a wealth of information on vacuolar biology and a solid basis for further characterization of vacuolar functions. ..
  17. Wang C, Stromhaug P, Kauffman E, Weisman L, Klionsky D. Yeast homotypic vacuole fusion requires the Ccz1-Mon1 complex during the tethering/docking stage. J Cell Biol. 2003;163:973-85 pubmed
    ..Accordingly, we propose that the Ccz1-Mon1 complex is critical for the Ypt7-dependent tethering/docking stage leading to the formation of a trans-SNARE complex and subsequent vacuole fusion. ..
  18. Mima J, Wickner W. Phosphoinositides and SNARE chaperones synergistically assemble and remodel SNARE complexes for membrane fusion. Proc Natl Acad Sci U S A. 2009;106:16191-6 pubmed publisher
    Yeast vacuole fusion requires 4 SNAREs, 2 SNARE chaperone systems (Sec17p/Sec18p/ATP and the HOPS complex), and 2 phosphoinositides, phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 4,5-bisphosphate [PI(4,5)P(2)]...
  19. Chang H, Jesch S, Gaspar M, Henry S. Role of the unfolded protein response pathway in secretory stress and regulation of INO1 expression in Saccharomyces cerevisiae. Genetics. 2004;168:1899-913 pubmed
    ..Indeed, many of the Sec(-) mutants that had elevated UPR expression at semipermissive growth temperatures failed to achieve wild-type levels of INO1 expression under these same conditions. ..
  20. Steel G, Laude A, Boojawan A, Harvey D, Morgan A. Biochemical analysis of the Saccharomyces cerevisiae SEC18 gene product: implications for the molecular mechanism of membrane fusion. Biochemistry. 1999;38:7764-72 pubmed
    ..If so, the crucial biochemical properties of NSF and SNAPs should be shared by their yeast homologues, Sec18p and Sec17p. Using purified recombinant proteins, we report here that Sec18p can specifically interact not only with Sec17p ..
  21. Legesse Miller A, Sagiv Y, Glozman R, Elazar Z. Aut7p, a soluble autophagic factor, participates in multiple membrane trafficking processes. J Biol Chem. 2000;275:32966-73 pubmed
    ..We suggest that, in addition to its role in autophagocytosis, Aut7p has pleiotropic effects and participates in at least two membrane traffic events. ..
  22. Zick M, Orr A, Schwartz M, Merz A, Wickner W. Sec17 can trigger fusion of trans-SNARE paired membranes without Sec18. Proc Natl Acad Sci U S A. 2015;112:E2290-7 pubmed publisher
    b>Sec17 [soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein; α-SNAP] and Sec18 (NSF) perform ATP-dependent disassembly of cis-SNARE complexes, liberating SNAREs for subsequent assembly of trans-complexes for fusion...
  23. Ziv I, Matiuhin Y, Kirkpatrick D, Erpapazoglou Z, Leon S, Pantazopoulou M, et al. A perturbed ubiquitin landscape distinguishes between ubiquitin in trafficking and in proteolysis. Mol Cell Proteomics. 2011;10:M111.009753 pubmed publisher
    ..We conclude that despite the shared use of the ubiquitin molecule, the two branches of the ubiquitin machinery--the ubiquitin-proteasome system and the ubiquitin trafficking system--were unevenly perturbed by expression of K0 ubiquitin. ..
  24. Kaiser C, Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell. 1990;61:723-33 pubmed
    ..By electron microscopy three of the mutants, sec18, sec17, and sec22, accumulate 50 nm vesicles at the nonpermissive temperature...
  25. Meiringer C, Rethmeier R, Auffarth K, Wilson J, Perz A, Barlowe C, et al. The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J Biol Chem. 2011;286:25039-46 pubmed publisher
    ..Our data support a model, in which a tethering complex is stabilized at the organelle membrane by binding to SNAREs, recognizes the incoming vesicle via its coat and then promotes its SNARE-mediated fusion. ..
  26. Starita L, Lo R, Eng J, von Haller P, Fields S. Sites of ubiquitin attachment in Saccharomyces cerevisiae. Proteomics. 2012;12:236-40 pubmed publisher
    ..However, such peptides with GG shifts have been difficult to discover. We identify 870 unique sites of ubiquitin attachment on 438 different proteins of the yeast Saccharomyces cerevisiae. ..
  27. Ishihara N, Hamasaki M, Yokota S, Suzuki K, Kamada Y, Kihara A, et al. Autophagosome requires specific early Sec proteins for its formation and NSF/SNARE for vacuolar fusion. Mol Biol Cell. 2001;12:3690-702 pubmed
    ..This evidence demonstrating the involvement of Sec proteins in the mechanism of autophagosome formation is crucial for understanding membrane flow during the process. ..
  28. Schwartz M, Nickerson D, Lobingier B, Plemel R, Duan M, Angers C, et al. Sec17 (?-SNAP) and an SM-tethering complex regulate the outcome of SNARE zippering in vitro and in vivo. elife. 2017;6: pubmed publisher
    ..Operating independently of Sec18 (NSF) catalysis, Sec17 (?-SNAP) either inhibits or stimulates SNARE-mediated fusion...
  29. Griff I, Schekman R, Rothman J, Kaiser C. The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein. J Biol Chem. 1992;267:12106-15 pubmed
    ..Immunoblotting indicates that Sec17p fractionates as a peripheral membrane protein and is mostly soluble when overexpressed, suggesting the presence of ..
  30. Veit M, Laage R, Dietrich L, Wang L, Ungermann C. Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO J. 2001;20:3145-55 pubmed
    ..During or after SNARE complex disassembly, palmitoylation occurs and anchors Vac8p to the vacuolar membrane. We propose that palmitoylation of Vac8p is regulated by the same machinery that controls membrane fusion. ..
  31. Alpadi K, Kulkarni A, Namjoshi S, Srinivasan S, Sippel K, Ayscough K, et al. Dynamin-SNARE interactions control trans-SNARE formation in intracellular membrane fusion. Nat Commun. 2013;4:1704 pubmed publisher
    ..Our findings provide new insight into the role of dynamins in membrane fusion by directly acting on SNARE proteins. ..
  32. Cleves A, Novick P, Bankaitis V. Mutations in the SAC1 gene suppress defects in yeast Golgi and yeast actin function. J Cell Biol. 1989;109:2939-50 pubmed
    ..On this basis, we suggest that SAC1p may represent one aspect of the mechanism whereby secretory and cytoskeletal activities are coordinated, so that proper spatial regulation of secretion might be achieved. ..
  33. Lobingier B, Nickerson D, Lo S, Merz A. SM proteins Sly1 and Vps33 co-assemble with Sec17 and SNARE complexes to oppose SNARE disassembly by Sec18. elife. 2014;3:e02272 pubmed publisher
    Secretory and endolysosomal fusion events are driven by SNAREs and cofactors, including Sec17/?-SNAP, Sec18/NSF, and Sec1/Munc18 (SM) proteins. SMs are essential for fusion in vivo, but the basis of this requirement is enigmatic...
  34. Rossi G, Kolstad K, Stone S, Palluault F, Ferro Novick S. BET3 encodes a novel hydrophilic protein that acts in conjunction with yeast SNAREs. Mol Biol Cell. 1995;6:1769-80 pubmed
    ..These findings support the hypothesis that Bet3p may act before the assembly of the SNARE complex. ..
  35. Kosodo Y, Noda Y, Adachi H, Yoda K. Cooperation of Sly1/SM-family protein and sec18/NSF of Saccharomyces cerevisiae in disassembly of cis-SNARE membrane-protein complexes. Biosci Biotechnol Biochem. 2003;67:448-50 pubmed
    ..These results suggest that Slyl and Sec18 proteins work cooperatively and that the binding of Slyl to Sed5 stimulates the disassembly of the cis-SNARE complex by Sec18 ATPase. ..
  36. Munson M, Hughson F. Conformational regulation of SNARE assembly and disassembly in vivo. J Biol Chem. 2002;277:9375-81 pubmed
    ..Our findings indicate that elevated levels of SNARE complexes can be toxic and that these levels are normally controlled by the SNARE disassembly machinery, by the limited availability of Sec9p, and by the closed conformation of Sso1p. ..
  37. Wilson Zbinden C, Dos Santos A, Stoffel Studer I, van der Vaart A, Hofmann K, Reggiori F, et al. Autophagy competes for a common phosphatidylethanolamine pool with major cellular PE-consuming pathways in Saccharomyces cerevisiae. Genetics. 2015;199:475-85 pubmed publisher
  38. Coe J, Lim A, Xu J, Hong W. A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae. Mol Biol Cell. 1999;10:2407-23 pubmed
    ..Tlg1p is able to bind His6-tagged Sec17p (yeast alpha-SNAP) in a dose-dependent manner and enters into a SNARE complex with Vti1p, Tlg2p, and Vps45p...