Gene Symbol: NYV1
Description: Nyv1p
Alias: MAM2, Nyv1p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. 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. ..
  2. 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
  3. McNew J, Parlati F, Fukuda R, Johnston R, Paz K, Paumet F, et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature. 2000;407:153-9 pubmed
    ..Here we find that, to a marked degree, the pattern of membrane flow in the cell is encoded and recapitulated by its isolated SNARE proteins, as predicted by the SNARE hypothesis. ..
  4. 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
    ..Analysis of vacuole protein complexes indicated that Ykt6 is part of a complex distinct from the second R-SNARE, Nyv1. We speculate that during vacuole fusion, Nyv1 is the classical R-SNARE, whereas the Ykt6-containing complex has a ..
  5. 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. ..
  6. 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. ..
  7. 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
    ..Instead, Vps33 binds the SNARE domains of Vam3, Vam7, and Nyv1. Vps33 directly binds vacuolar quaternary SNARE complexes, and the affinity of Vps33 for SNARE complexes is greater ..
  8. 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. ..
  9. 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
    ..HOPS thus directs the Sec17p/Sec18p chaperone system to maximize functional trans-SNARE complex for membrane fusion, a new role of tethering factors during membrane traffic. ..

More Information


  1. 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. ..
  2. 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. ..
  3. Zick M, Wickner W. The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexes. Mol Biol Cell. 2013;24:3746-53 pubmed publisher
    ..Our findings establish yet another function among the multiple tasks that HOPS performs to catalyze the fusion of yeast vacuoles. ..
  4. 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. ..
  5. 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
    ..Even in the absence of the vacuolar v-SNARE Nyv1p, a subcomplex which includes Vam7p and the t-SNARE Vam3p is preserved...
  6. Fratti R, Collins K, Hickey C, Wickner W. Stringent 3Q.1R composition of the SNARE 0-layer can be bypassed for fusion by compensatory SNARE mutation or by lipid bilayer modification. J Biol Chem. 2007;282:14861-7 pubmed
    ..the Rab Ypt7p, the Rab-effector complex HOPS, and 4 SNAREs: the Q-SNAREs Vti1p, Vam3p, and Vam7p and the R-SNARE Nyv1p. We now report that alterations in the 0-layer Gln or Arg residues of Vam7p or Nyv1p, respectively, strongly ..
  7. 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. ..
  8. 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. ..
  9. 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
    Vacuole SNAREs, including the t-SNAREs Vam3p and Vam7p and the v-SNARE Nyv1p, are found in a multisubunit "cis" complex on isolated organelles...
  10. 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
    ..We found that not only vacuolar R-SNARE Nyv1p but also the non-cognate R-SNAREs, endosomal Snc2p, and endoplasmic reticulum-Golgi Sec22p caused efficient fusion ..
  11. 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. ..
  12. Angers C, Merz A. HOPS interacts with Apl5 at the vacuole membrane and is required for consumption of AP-3 transport vesicles. Mol Biol Cell. 2009;20:4563-74 pubmed publisher
    ..We propose that AP-3 remains associated with budded vesicles, interacts with Vps41 and HOPS upon vesicle docking at the vacuole, and finally dissociates during docking or fusion. ..
  13. 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. ..
  14. 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
    Vacuole fusion requires Sec18p (NSF), Sec17p (alpha-SNAP), Ypt7p (GTP binding protein), Vam3p (t-SNARE), Nyv1p (v-SNARE), and LMA1 (low Mr activity 1, a heterodimer of thioredoxin and I(B)2)...
  15. Sato K, Wickner W. Functional reconstitution of ypt7p GTPase and a purified vacuole SNARE complex. Science. 1998;281:700-2 pubmed
    ..membrane proteins, including the Ypt7p guanosine triphosphatase and a "SNARE complex" with Vam3p and Nyv1p. Proteoliposomes from extracts immunodepleted of either Vam3p or Ypt7p could not fuse, but vesicles reconstituted ..
  16. 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
    ..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...
  17. Kweon Y, Rothe A, Conibear E, Stevens T. Ykt6p is a multifunctional yeast R-SNARE that is required for multiple membrane transport pathways to the vacuole. Mol Biol Cell. 2003;14:1868-81 pubmed
    ..phosphatase transport, and aminopeptidase I delivery, and in one mutant, overexpression of the SNARE protein Nyv1p suppresses the alkaline phosphatase transport defect...
  18. 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. ..
  19. Fratti R, Wickner W. Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7p. J Biol Chem. 2007;282:13133-8 pubmed
    ..The PX domain, through its affinities for phosphoinositides and HOPS, is thus exclusively required for enhancing the targeting of Vam7p rather than for execution of the Vam7p functions in HOPS.SNARE complex assembly and fusion. ..
  20. 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. ..
  21. 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. ..
  22. 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. ..
  23. 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. ..
  24. 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. ..
  25. Brown C, Liu J, Hung G, Carter D, Cui D, Chiang H. The Vid vesicle to vacuole trafficking event requires components of the SNARE membrane fusion machinery. J Biol Chem. 2003;278:25688-99 pubmed
    ..Likewise, a number of v-SNAREs (Ykt6p, Nyv1p, Vti1p) and homotypic fusion vacuole protein sorting complex family members (Vps39p and Vps41p) were required for ..
  26. 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
    ..Deletion of the vacuolar v-SNARE Nyv1 has the same effect, suggesting that both types of mutations similarly alter the conformation of V(0)...
  27. Zhao Y, Xiong B, Xu H, Jiang L. Expression of NYV1 encoding the negative regulator of Pmc1 is repressed by two transcriptional repressors, Nrg1 and Mig1. FEBS Lett. 2014;588:3195-201 pubmed publisher
    ..Here, we show that overexpression of PMC1 and its negative regulator gene NYV1 suppresses and increases calcium hypersensitivity of ESCRT mutants, respectively...
  28. Takita Y, Engstrom L, Ungermann C, Cunningham K. Inhibition of the Ca(2+)-ATPase Pmc1p by the v-SNARE protein Nyv1p. J Biol Chem. 2001;276:6200-6 pubmed
    ..In a genetic screen for potential negative regulators of Pmc1p, a vacuolar v-SNARE protein, Nyv1p, was recovered...
  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. 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. ..
  31. 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
    ..the following two v-SNAREs: Bet1p, which is involved in endoplasmic reticulum to Golgi vesicular transport, and Nyv1p, implicated in vacuolar inheritance...
  32. 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 ..
  33. 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
    ..the SNARE motif mutations and the insertions did not alter the association of Vam3p with Vam7p, Vti1p, Nyv1p, and Ykt6p, other vacuolar SNARE proteins implicated in fusion...
  34. Gebre S, Connor R, Xia Y, Jawed S, Bush J, Bard M, et al. Osh6 overexpression extends the lifespan of yeast by increasing vacuole fusion. Cell Cycle. 2012;11:2176-88 pubmed publisher
    ..lifespan, we screened for genes that can complement the fusion defect of selected mutants (erg6?, a sterol mutant; nyv1?,  a mutant involved in the vacuolar SNARE complex and vac8?, a vacuolar membrane protein mutant)...
  35. 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
    ..over SNARE activation in the cytosol requires the cytosolic cyclin-dependent kinase Pho80-Pho85 and the R-SNARE Nyv1. These results suggest that cells can adapt the volume of vacuoles to their content through feedback from the ..
  36. 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
    ..In contrast, formation of the quaternary SNARE complex from recombinant Vam3p, Nyv1p, Vti1p, and Vam7p subunits did not depend on the transmembrane segment of Vam3p nor on the transmembrane segments ..
  37. 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. ..
  38. Wen W, Chen L, Wu H, Sun X, Zhang M, Banfield D. Identification of the yeast R-SNARE Nyv1p as a novel longin domain-containing protein. Mol Biol Cell. 2006;17:4282-99 pubmed
    ..Using nuclear magnetic resonance spectroscopy, we establish that the N-terminal domain of the yeast vacuolar R-SNARE Nyv1p adopts a longin-like fold similar to those of Sec22b and Ykt6p...
  39. Xu H, Zick M, Wickner W, Jun Y. A lipid-anchored SNARE supports membrane fusion. Proc Natl Acad Sci U S A. 2011;108:17325-30 pubmed publisher
    ..However, an R-SNARE, Nyv1p, with a genetically engineered lipid anchor that spans half of the bilayer suffices for the fusion of isolated ..
  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
    ..As different transport steps were affected our data demonstrate the importance of a folded Vti1p H(abc) domain for transport. ..
  41. 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. ..
  42. Isgandarova S, Jones L, Forsberg D, Loncar A, Dawson J, Tedrick K, et al. Stimulation of actin polymerization by vacuoles via Cdc42p-dependent signaling. J Biol Chem. 2007;282:30466-75 pubmed
    ..Our results suggest that actin polymerization is a subreaction of vacuole membrane fusion governed by Cdc42p signal transduction. ..
  43. 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. ..
  44. 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. ..
  45. 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. ..