Genomes and Genes
Gene Symbol: VAM3
Description: SNAP receptor VAM3
Alias: PTH1, SNAP receptor VAM3
Species: Saccharomyces cerevisiae S288c
- 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. ..
- Darsow T, Rieder S, Emr S. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. J Cell Biol. 1997;138:517-29 pubmed..b>VAM3 encodes a 283-amino acid protein that shares homology with the syntaxin family of t-SNARE molecules...
- Xu Z, Sato K, Wickner W. LMA1 binds to vacuoles at Sec18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion. Cell. 1998;93:1125-34 pubmed..LMA1 is released from vacuoles in a phosphatase-regulated reaction. This LMA1 cycle explains how priming by Sec18p is coupled to t-SNARE stabilization and to fusion. ..
- Wada Y, Nakamura N, Ohsumi Y, Hirata A. Vam3p, a new member of syntaxin related protein, is required for vacuolar assembly in the yeast Saccharomyces cerevisiae. J Cell Sci. 1997;110 ( Pt 11):1299-306 pubmed..b>VAM3 of Saccharomyces cerevisiae encodes a 33 kDa protein (Vam3p) with a hydrophobic transmembrane segment at its C ..
- Hickey C, Wickner W. HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assembly. Mol Biol Cell. 2010;21:2297-305 pubmed publisher..SNAREs further stabilize the associations of HOPS-tethered membranes. HOPS then protects newly formed trans-SNARE complexes from disassembly by Sec17p/Sec18p. ..
- 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..This functional characterization of Vam7p suggests a general role for SNAP-25 homologs, not only on the plasma membrane but along the secretory pathway. ..
- 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. ..
- Srivastava A, Jones E. Pth1/Vam3p is the syntaxin homolog at the vacuolar membrane of Saccharomyces cerevisiae required for the delivery of vacuolar hydrolases. Genetics. 1998;148:85-98 pubmed..This is in contrast to a pep12 mutant in which P2CpY is secreted from the cell. Furthermore, pep12 is epistatic to pth1/vam3 with respect to the CpY secretion phenotype...
- 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. ..
- Price A, Seals D, Wickner W, Ungermann C. 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;148:1231-8 pubmed..Thus, cis-SNARE complexes can contain Rab/Ypt effectors, and these effectors can be mobilized by NSF/Sec18p-driven priming, allowing their direct association with a Rab/Ypt protein to activate docking. ..
- 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. ..
- 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. ..
- Pieren M, Schmidt A, Mayer A. The SM protein Vps33 and the t-SNARE H(abc) domain promote fusion pore opening. Nat Struct Mol Biol. 2010;17:710-7 pubmed publisher..Deleting the H(abc) domain of the vacuolar t-SNARE Vam3, which interacts with Vps33, had the same effect...
- 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. ..
- 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. ..
- Rieder S, Emr S. A novel RING finger protein complex essential for a late step in protein transport to the yeast vacuole. Mol Biol Cell. 1997;8:2307-27 pubmed..Thus we propose that the class C Vps proteins are components of a hetero-oligomeric protein complex that mediates the delivery of multiple transport intermediates to the vacuole. ..
- 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..HOPS tethering 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...
- 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
- Sato T, Darsow T, Emr S. Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Mol Cell Biol. 1998;18:5308-19 pubmed..Furthermore, VAM7 displayed genetic interactions with the vacuolar syntaxin homolog, VAM3. Consistent with the genetic results, Vam7p physically associated in a complex containing Vam3p, and this ..
- Lobingier B, Merz A. Sec1/Munc18 protein Vps33 binds to SNARE domains and the quaternary SNARE complex. Mol Biol Cell. 2012;23:4611-22 pubmed publisher..HOPS binds the N-terminal H(abc) domain of the Qa-family SNARE Vam3, but Vps33 is not required for this interaction. Instead, Vps33 binds the SNARE domains of Vam3, Vam7, and Nyv1...
- 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. ..
- 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..VTI1 interacts genetically with the vacuolar t-SNARE VAM3, which is required for transport of both alkaline phosphatase and aminopeptidase I to the vacuole...
- Subramanian S, Woolford C, Jones E. The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Mol Biol Cell. 2004;15:2593-605 pubmed..This is the first report demonstrating the involvement of a single syntaxin with two SM proteins at the same organelle. ..
- 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. ..
- Sato T, Rehling P, Peterson M, Emr S. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Mol Cell. 2000;6:661-71 pubmed..In this study, we characterized and purified this complex and identified its interaction with the syntaxin homolog Vam3. Vam3 pairs with the SNAP-25 homolog Vam7 and VAMP homolog Vti1 to form SNARE complexes during vesicle docking/..
- Gotte M, Gallwitz D. High expression of the yeast syntaxin-related Vam3 protein suppresses the protein transport defects of a pep12 null mutant. FEBS Lett. 1997;411:48-52 pubmed..Exploiting the temperature-sensitive growth phenotype of pep12 deletion strains, we identified VAM3 as a multicopy suppressor...
- 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. ..
- Rehling P, Darsow T, Katzmann D, Emr S. Formation of AP-3 transport intermediates requires Vps41 function. Nat Cell Biol. 1999;1:346-53 pubmed..Vps41 binds to the AP-3 delta-adaptin subunit, suggesting that they function together in the formation of ALP pathway transport intermediates at the late Golgi. ..
- Brett C, Plemel R, Lobingier B, Lobinger B, Vignali M, Fields S, et al. Efficient termination of vacuolar Rab GTPase signaling requires coordinated action by a GAP and a protein kinase. J Cell Biol. 2008;182:1141-51 pubmed publisher..targets: a tether, the Vps-C/homotypic fusion and vacuole protein sorting (HOPS) subunit Vps41, and a SNARE, Vam3. Phosphorylation of both substrates is opposed by Ypt7-guanosine triphosphate (GTP)...
- 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..The truncated protein (Vam3 Delta N) is sorted normally to the vacuole and is functional, because the vacuolar morphology is unaltered in this ..
- 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. ..
- Kulkarni A, Alpadi K, Sirupangi T, Peters C. A dynamin homolog promotes the transition from hemifusion to content mixing in intracellular membrane fusion. Traffic. 2014;15:558-71 pubmed publisher..We propose a novel concept that Vps1, through its oligomerization and SNARE domain binding, promotes the hemifusion-content mixing transition in yeast vacuole fusion by increasing the number of trans-SNAREs. ..
- 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
- Schindler C, Spang A. Interaction of SNAREs with ArfGAPs precedes recruitment of Sec18p/NSF. Mol Biol Cell. 2007;18:2852-63 pubmed
- Miner G, Starr M, Hurst L, Sparks R, Padolina M, Fratti R. The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain. J Biol Chem. 2016;291:17651-63 pubmed publisher..PI3P binding was inhibited when the PX domain mutant Y42A was introduced into Vam7-6A to make Vam7-7A. Thus the Vam7 PBR affects PI3P binding by the PX domain and in turn affects binding to SNAREs and HOPS to support efficient fusion. ..
- Strasser B, Iwaszkiewicz J, Michielin O, Mayer A. The V-ATPase proteolipid cylinder promotes the lipid-mixing stage of SNARE-dependent fusion of yeast vacuoles. EMBO J. 2011;30:4126-41 pubmed publisher..We propose that a SNARE-dependent conformational change in V(0) proteolipids might stimulate fusion by creating a hydrophobic crevice that promotes lipid reorientation and formation of a lipidic fusion pore...
- Peterson M, Emr S. The class C Vps complex functions at multiple stages of the vacuolar transport pathway. Traffic. 2001;2:476-86 pubmed..Collectively, these results indicate that the Class C Vps complex plays essential roles in the processes of membrane docking and fusion at both the Golgi-to-endosome and endosome-to-vacuole stages of transport. ..
- Karunakaran S, Fratti R. The lipid composition and physical properties of the yeast vacuole affect the hemifusion-fusion transition. Traffic. 2013;14:650-62 pubmed publisher..Together, these data indicate that the physical properties and the lipid composition of the membrane affect the function of SNAREs in promoting the hemifusion-fusion transition. ..
- 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. ..
- 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..As different transport steps were affected our data demonstrate the importance of a folded Vti1p H(abc) domain for transport. ..
- 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. ..
- Kulkarni A, Alpadi K, Namjoshi S, Peters C. A tethering complex dimer catalyzes trans-SNARE complex formation in intracellular membrane fusion. Bioarchitecture. 2012;2:59-69 pubmed..Here we report a novel finding that a HOPS tethering complex dimer catalyzes Rab GTPase-dependent formation of a topologically preferred QbQcR-Qa trans-SNARE complex. ..
- Pieren M, DesfougÃ¨res 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 ..
- Sasser T, Lawrence G, Karunakaran S, Brown C, Fratti R. The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion. J Biol Chem. 2013;288:18300-10 pubmed publisher..The attenuated fusion of ycf1? vacuoles was rescued by the addition of recombinant Vam7p to in vitro experiments. Thus, Ycf1p contributes in the recruitment of Vam7p to the vacuole for efficient membrane fusion. ..
- Sasser T, Qiu Q, Karunakaran S, Padolina M, Reyes A, Flood B, et al. Yeast lipin 1 orthologue pah1p regulates vacuole homeostasis and membrane fusion. J Biol Chem. 2012;287:2221-36 pubmed publisher..These findings demonstrate that Pah1p and PA phosphatase activity are critical for vacuole homeostasis and fusion. ..
- 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. ..
- 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..Here, we analyzed the role of the transmembrane domain of the vacuolar SNARE Vam3 by replacing it by a lipid anchor...
- Qiu Q, Fratti R. The Na+/H+ exchanger Nhx1p regulates the initiation of Saccharomyces cerevisiae vacuole fusion. J Cell Sci. 2010;123:3266-75 pubmed publisher..In addition, the weak base chloroquine restored nhx1? fusion to wild-type levels. Together, these data indicate that Nhx1p regulates the initiation of fusion by controlling vacuole lumen pH. ..
- 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. ..
- Lai X, Beilharz T, Au W, Hammet A, Preiss T, Basrai M, et al. Yeast hEST1A/B (SMG5/6)-like proteins contribute to environment-sensing adaptive gene expression responses. G3 (Bethesda). 2013;3:1649-59 pubmed publisher..Overall, these results suggest that Esl1 and Esl2 contribute to the regulation of adaptive gene expression responses of environmental sensing pathways. ..
- 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. ..
- Lisman Q, Pomorski T, Vogelzangs C, Urli Stam D, de Cocq van Delwijnen W, Holthuis J. Protein sorting in the late Golgi of Saccharomyces cerevisiae does not require mannosylated sphingolipids. J Biol Chem. 2004;279:1020-9 pubmed..Our results indicate that protein sorting in the late Golgi of yeast does not require production of mannosylated sphingolipids. ..
- 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. ..
- Hofmann M, Peplowska K, Rohde J, Poschner B, Ungermann C, Langosch D. Self-interaction of a SNARE transmembrane domain promotes the hemifusion-to-fusion transition. J Mol Biol. 2006;364:1048-60 pubmed..Since covalent dimerisation of this mutant recovered wild-type behaviour, homodimerisation of a SNARE transmembrane domain appears to control the transition of a hemifusion intermediate to complete lipid mixing. ..
- LÃ¼rick A, Kuhlee A, BrÃ¶cker C, KÃ¼mmel D, Raunser S, Ungermann C. The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion. J Biol Chem. 2015;290:5405-13 pubmed publisher..Here, we present direct evidence for HOPS binding to SNAREs and the Habc domain of the Vam3 SNARE protein, which may explain its function during fusion...
- Hoffman Sommer M, Kucharczyk R, Piekarska I, Kozlowska E, Rytka J. Mutations in the Saccharomyces cerevisiae vacuolar fusion proteins Ccz1, Mon1 and Ypt7 cause defects in cell cycle progression in a num1Delta background. Eur J Cell Biol. 2009;88:639-52 pubmed publisher..Together, these results indicate that deregulation of the cell cycle in these mutants results from two separate mechanisms, one of which is related to calcium homeostasis. ..
- 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. ..
- Gurunathan S, David D, Gerst J. Dynamin and clathrin are required for the biogenesis of a distinct class of secretory vesicles in yeast. EMBO J. 2002;21:602-14 pubmed..e. VPS34 and VAM3, respectively) have no effect...