Gene Symbol: VTI1
Description: v-SNARE protein VTI1
Alias: v-SNARE protein VTI1
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Fischer von Mollard G, Stevens T. The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Mol Biol Cell. 1999;10:1719-32 pubmed
    ..Certain vti1-ts yeast mutants are defective in alkaline phosphatase transport from the Golgi to the vacuole and in targeting of ..
  2. 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
    ..This ternary synergy of phosphoinositides and 2 SNARE chaperone systems is required for rapid fusion. ..
  3. Karunakaran V, Wickner W. Fusion proteins and select lipids cooperate as membrane receptors for the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) Vam7p. J Biol Chem. 2013;288:28557-66 pubmed publisher
    ..Acidic lipids allow low concentrations of Vam7p to suffice for fusion; without acidic lipids, the block to fusion is partially bypassed by high concentrations of Vam7p. ..
  4. Tsui M, Tai W, Banfield D. Selective formation of Sed5p-containing SNARE complexes is mediated by combinatorial binding interactions. Mol Biol Cell. 2001;12:521-38 pubmed
    ..Rather our data are consistent with the existence of multiple (perhaps parallel) trafficking pathways where Sed5p-containing SNARE complexes play overlapping and/or distinct functional roles. ..
  5. 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
    ..Sec17p may displace HOPS from SNAREs to permit subsequent rounds of fusion. ..
  6. 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;12:3375-85 pubmed
    ..We conclude that the N-terminus of Vam3p is required for coordination of priming and docking during homotypic vacuole fusion. ..
  7. 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. ..
  8. 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
    ..Overexpression of Tlg1p complements the growth defect of vti1-11 at the nonpermissive temperature, whereas incomplete complementation was observed with vti1-1, further ..
  9. 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
    ..The temperature-sensitive vti1 growth defect can be rescued by the overexpression of the v-SNARE, Ykt6p, which physically interacts with Vti1p...

More Information


  1. Fukuda R, McNew J, Weber T, Parlati F, Engel T, Nickel W, et al. Functional architecture of an intracellular membrane t-SNARE. Nature. 2000;407:198-202 pubmed
    ..SNAP-25 may thus be the exception rather than the rule, having been derived from genes that encoded separate light chains that fused during evolution to produce a single gene encoding one protein with two helices. ..
  2. 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
    ..Furthermore, vti1 temperature-sensitive alleles cause a synthetic fusion-defective phenotype in our reaction...
  3. Stein I, Gottfried A, Zimmermann J, Fischer von Mollard G. TVP23 interacts genetically with the yeast SNARE VTI1 and functions in retrograde transport from the early endosome to the late Golgi. Biochem J. 2009;419:229-36 pubmed publisher
    ..Here, we identified the late Golgi membrane protein TVP23 as a multicopy suppressor of the growth defect in vti1-2 cells. By contrast, the growth defect in vti1-11 cells was not suppressed by TVP23 overexpression...
  4. 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. ..
  5. von Mollard G, Nothwehr S, Stevens T. The yeast v-SNARE Vti1p mediates two vesicle transport pathways through interactions with the t-SNAREs Sed5p and Pep12p. J Cell Biol. 1997;137:1511-24 pubmed
    ..We identified a novel Saccharomyces cerevisiae v-SNARE (Vti1p) encoded by the essential gene, VTI1. Vti1p interacts with the prevacuolar t-SNARE Pep12p to direct Golgi to prevacuolar traffic...
  6. Izawa R, Onoue T, Furukawa N, Mima J. Distinct contributions of vacuolar Qabc- and R-SNARE proteins to membrane fusion specificity. J Biol Chem. 2012;287:3445-53 pubmed publisher
    ..Thus, our current study establishes that an appropriate assembly of Qabc-SNAREs is crucial for regulating fusion specificity, whereas R-SNARE itself has little contribution to specificity. ..
  7. Peters C, Baars T, Buhler S, Mayer A. Mutual control of membrane fission and fusion proteins. Cell. 2004;119:667-78 pubmed
    ..We propose that reciprocal control between fusion and fission components exists, which may prevent futile cycles of fission and fusion. ..
  8. Wang J, Gossing M, Fang P, Zimmermann J, Li X, von Mollard G, et al. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. Proc Natl Acad Sci U S A. 2011;108:12277-82 pubmed publisher
    ..This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport. ..
  9. Kama R, Robinson M, Gerst J. Btn2, a Hook1 ortholog and potential Batten disease-related protein, mediates late endosome-Golgi protein sorting in yeast. Mol Cell Biol. 2007;27:605-21 pubmed
    ..g., Snc1 and Snc2 [Snc1/2], Tlg1, Tlg2, and Vti1), the Snx4 sorting nexin, and retromer (e.g., Vps26 and Vps35)...
  10. Kanneganti V, Kama R, Gerst J. Btn3 is a negative regulator of Btn2-mediated endosomal protein trafficking and prion curing in yeast. Mol Biol Cell. 2011;22:1648-63 pubmed publisher
    ..Therefore Btn3 is a novel negative regulator of intracellular protein sorting, which may be of importance in the onset of complex I deficiency and Batten disease in humans. ..
  11. Krämer L, Ungermann C. HOPS drives vacuole fusion by binding the vacuolar SNARE complex and the Vam7 PX domain via two distinct sites. Mol Biol Cell. 2011;22:2601-11 pubmed publisher
    ..complex controls fusion through specific interactions with the vacuolar SNARE complex (consisting of Vam3, Vam7, Vti1, and Nyv1) and the N-terminal domains of Vam7 and Vam3...
  12. Bryant N, James D. Vps45p stabilizes the syntaxin homologue Tlg2p and positively regulates SNARE complex formation. EMBO J. 2001;20:3380-8 pubmed
    ..First, SM proteins act as chaperone-like molecules for their cognate t-SNAREs. Secondly, SM proteins play an essential role in the activation process allowing their cognate t-SNARE to participate in ternary complex formation. ..
  13. Chidambaram S, Müllers N, Wiederhold K, Haucke V, von Mollard G. Specific interaction between SNAREs and epsin N-terminal homology (ENTH) domains of epsin-related proteins in trans-Golgi network to endosome transport. J Biol Chem. 2004;279:4175-9 pubmed
    ..Vti1p is required for multiple transport steps in the endosomal system. Genetic interactions between VTI1 and ENT3 were investigated...
  14. Paumet F, Brugger B, Parlati F, McNew J, Sollner T, Rothman J. A t-SNARE of the endocytic pathway must be activated for fusion. J Cell Biol. 2001;155:961-8 pubmed
    ..Locking t-SNAREs creates the potential for spatial and temporal regulation of fusion by signaling processes that unleash their fusion capacity. ..
  15. Paumet F, Rahimian V, Rothman J. The specificity of SNARE-dependent fusion is encoded in the SNARE motif. Proc Natl Acad Sci U S A. 2004;101:3376-80 pubmed
    ..Studying this complex and the previously identified early endosomal SNARE complex, we find that the specificity of fusion resides in the SNARE motifs. ..
  16. Dilcher M, Kohler B, von Mollard G. Genetic interactions with the yeast Q-SNARE VTI1 reveal novel functions for the R-SNARE YKT6. J Biol Chem. 2001;276:34537-44 pubmed
    ..and the R-SNARE YKT6 both as multicopy and as low copy suppressors of the growth and vacuolar transport defect in vti1-2 cells. Ykt6p was known to function in retrograde traffic to the cis-Golgi and homotypic vacuolar fusion...
  17. Alpadi K, Kulkarni A, Comte V, Reinhardt M, Schmidt A, Namjoshi S, et al. Sequential analysis of trans-SNARE formation in intracellular membrane fusion. PLoS Biol. 2012;10:e1001243 pubmed publisher
    ..This suggests that the vacuolar Rab-GTPase, Ypt7, and HOPS restrict cis-SNARE disassembly and thereby bias trans-SNARE assembly into a preferred topology. ..
  18. Lewis M, Pelham H. A new yeast endosomal SNARE related to mammalian syntaxin 8. Traffic. 2002;3:922-9 pubmed
    ..Syn8p thus appears to be a functional homolog of mammalian syntaxin 8, but Tlg1p can, amongst other roles, provide an equivalent function. ..
  19. 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. ..
  20. Roy R, Peplowska K, Rohde J, Ungermann C, Langosch D. Role of the Vam3p transmembrane segment in homodimerization and SNARE complex formation. Biochemistry. 2006;45:7654-60 pubmed
  21. Bryant N, James D. The Sec1p/Munc18 (SM) protein, Vps45p, cycles on and off membranes during vesicle transport. J Cell Biol. 2003;161:691-6 pubmed
    ..These data reveal that SM proteins cycle on and off membranes in a stage-specific manner during the vesicle transport reaction, and suggest that protein phosphorylation plays a key role in the regulation of this cycle. ..
  22. Zimmermann J, Chidambaram S, Fischer von Mollard G. Dissecting Ent3p: the ENTH domain binds different SNAREs via distinct amino acid residues while the C-terminus is sufficient for retrograde transport from endosomes. Biochem J. 2010;431:123-34 pubmed publisher
    ..This provides the necessary flexibility to bind three SNAREs with little sequence homology but maintains the specificity of the interaction. ..
  23. Wang Y, Dulubova I, Rizo J, Sudhof T. Functional analysis of conserved structural elements in yeast syntaxin Vam3p. J Biol Chem. 2001;276:28598-605 pubmed
    ..Our data suggest that in contrast to previously characterized syntaxins, Vam3p contains only two domains essential for fusion, the SNARE motif and the TMR, and these domains have to be closely coupled to function in fusion. ..
  24. Balderhaar H, Lachmann J, Yavavli E, Bröcker C, Lürick A, Ungermann C. The CORVET complex promotes tethering and fusion of Rab5/Vps21-positive membranes. Proc Natl Acad Sci U S A. 2013;110:3823-8 pubmed publisher
    ..We therefore conclude that CORVET is a tethering complex that promotes fusion of Rab5-positive membranes and thus facilitates receptor down-regulation and recycling at the late endosome. ..
  25. 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. ..
  26. 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. ..
  27. Kama R, Kanneganti V, Ungermann C, Gerst J. The yeast Batten disease orthologue Btn1 controls endosome-Golgi retrograde transport via SNARE assembly. J Cell Biol. 2011;195:203-15 pubmed publisher
    ..Thus, Btn1 controls retrograde sorting by regulating SNARE phosphorylation and assembly, a process that may be adversely affected in Batten Disease patients. ..
  28. Paumet F, Rahimian V, Di Liberto M, Rothman J. Concerted auto-regulation in yeast endosomal t-SNAREs. J Biol Chem. 2005;280:21137-43 pubmed
    ..These internal controls provide a potential mechanism to enable SNARE-dependent fusion to be regulated. ..
  29. 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. ..
  30. Tsui M, Banfield D. Yeast Golgi SNARE interactions are promiscuous. J Cell Sci. 2000;113 ( Pt 1):145-52 pubmed
  31. Meiringer C, Auffarth K, Hou H, Ungermann C. Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway. Traffic. 2008;9:1510-21 pubmed publisher
    ..Thus, depalmitoylation and release of Ykt6 are needed for its recycling and to circumvent its entry into the endosomal multivesicular body pathway. ..
  32. Jun Y, Thorngren N, Starai V, Fratti R, Collins K, Wickner W. Reversible, cooperative reactions of yeast vacuole docking. EMBO J. 2006;25:5260-9 pubmed
    ..Docked vacuoles finally assemble SNARE complexes, yet still require physiological temperature and lipid rearrangements to complete fusion. ..
  33. Rohde J, Dietrich L, Langosch D, Ungermann C. The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion. J Biol Chem. 2003;278:1656-62 pubmed
    ..Since palmitoylated Vac8 is required beyond trans-SNARE complex formation, this may partially explain the fusion deficiency. ..
  34. Furukawa N, Mima J. Multiple and distinct strategies of yeast SNAREs to confer the specificity of membrane fusion. Sci Rep. 2014;4:4277 pubmed publisher
    ..Thus, our findings uncover multiple and distinct strategies of SNAREs to directly mediate fusion specificity. ..
  35. Pieren M, Desfougères Y, Michaillat L, Schmidt A, Mayer A. Vacuolar SNARE protein transmembrane domains serve as nonspecific membrane anchors with unequal roles in lipid mixing. J Biol Chem. 2015;290:12821-32 pubmed publisher
    ..We replaced the TMDs of all vacuolar SNAREs (Nyv1, Vam3, and Vti1) by a lipid anchor, by a TMD from a protein unrelated to the membrane fusion machinery, or by artificial leucine-..
  36. Lemus L, Ribas J, Sikorska N, Goder V. An ER-Localized SNARE Protein Is Exported in Specific COPII Vesicles for Autophagosome Biogenesis. Cell Rep. 2016;14:1710-1722 pubmed publisher
    ..Under the same conditions, sec23-1 cells are hypersensitive to starvation and deficient in autophagy. Our data suggest that ER membranes containing Ufe1 are delivered to sites of autophagosome formation in specific COPII vesicles. ..
  37. 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
    ..Once SNAREs are partially zipped, Sec17 promotes fusion in either the presence or absence of HOPS, but with faster kinetics when HOPS is absent, suggesting that ejection of the SM is a rate-limiting step. ..
  38. Xu H, Wickner W. N-terminal domain of vacuolar SNARE Vam7p promotes trans-SNARE complex assembly. Proc Natl Acad Sci U S A. 2012;109:17936-41 pubmed publisher
    ..This function of the Vam7p N-domain depends on the presence of PI3P and its affinity for PI3P. Added N-domain can even promote SNARE complex assembly when Vam7 still bears its own N-domain. ..
  39. 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. ..
  40. Gossing M, Chidambaram S, Fischer von Mollard G. Importance of the N-terminal domain of the Qb-SNARE Vti1p for different membrane transport steps in the yeast endosomal system. PLoS ONE. 2013;8:e66304 pubmed publisher
    ..So far, all vti1 mutants investigated had mutations within the SNARE motif...