Genomes and Genes
Gene Symbol: SNC2
Description: SNAP receptor SNC2
Alias: SNAP receptor SNC2
Species: Saccharomyces cerevisiae S288c
- 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. ..
- Lustgarten V, Gerst J. Yeast VSM1 encodes a v-SNARE binding protein that may act as a negative regulator of constitutive exocytosis. Mol Cell Biol. 1999;19:4480-94 pubmed..A novel protein, designated Vsm1, binds tightly to the Snc2 v-SNARE in the two-hybrid system and can be coimmunoprecipitated with Snc1 or Snc2 from solubilized yeast cell ..
- Songer J, Munson M. Sec6p anchors the assembled exocyst complex at sites of secretion. Mol Biol Cell. 2009;20:973-82 pubmed publisher..Our results indicate that assembly and polarization of the exocyst are functionally separable events, and that Sec6p is required to anchor exocyst complexes at sites of secretion. ..
- Jantti J, Aalto M, Oyen M, Sundqvist L, Keränen S, Ronne H. Characterization of temperature-sensitive mutations in the yeast syntaxin 1 homologues Sso1p and Sso2p, and evidence of a distinct function for Sso1p in sporulation. J Cell Sci. 2002;115:409-20 pubmed..copy number suppressors of sso2-1 yielded three genes that are involved in the terminal step of secretion: SNC1, SNC2 and SEC9...
- Gurunathan S, Chapman Shimshoni D, Trajkovic S, Gerst J. Yeast exocytic v-SNAREs confer endocytosis. Mol Biol Cell. 2000;11:3629-43 pubmedIn yeast, homologues of the synaptobrevin/VAMP family of v-SNAREs (Snc1 and Snc2) confer the docking and fusion of secretory vesicles at the cell surface...
- Katz L, Brennwald P. Testing the 3Q:1R "rule": mutational analysis of the ionic "zero" layer in the yeast exocytic SNARE complex reveals no requirement for arginine. Mol Biol Cell. 2000;11:3849-58 pubmed
- Carr C, Grote E, Munson M, Hughson F, Novick P. Sec1p binds to SNARE complexes and concentrates at sites of secretion. J Cell Biol. 1999;146:333-44 pubmed..The results presented here place yeast Sec1p at the core of the exocytic fusion machinery, bound to SNARE complexes and localized to sites of secretion. ..
- Weber Boyvat M, Aro N, Chernov K, Nyman T, Jantti J. Sec1p and Mso1p C-terminal tails cooperate with the SNAREs and Sec4p in polarized exocytosis. Mol Biol Cell. 2011;22:230-44 pubmed publisher..This association depends on the Sec4p guanine nucleotide exchange factor Sec2p. Our results reveal a novel binding mode between the Sec1p C-terminal tail and the SNARE complex, and suggest a role for Mso1p as an effector of Sec4p. ..
- 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. ..
- Togneri J, Cheng Y, Munson M, Hughson F, Carr C. Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. Proc Natl Acad Sci U S A. 2006;103:17730-5 pubmed..We propose that vesicle fusion requires a specific interaction between the SM protein and the ternary SNARE complex. ..
- Katz L, Hanson P, Heuser J, Brennwald P. Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. EMBO J. 1998;17:6200-9 pubmed..the yeast SNAP-25 homolog, Sec9, we have identified a gain-of-function mutation in the yeast synaptobrevin homolog, Snc2. The genetic properties of this suppression point to a specific interaction between the C-termini of Sec9 and Snc2 ..
- Abeliovich H, Grote E, Novick P, Ferro Novick S. Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. J Biol Chem. 1998;273:11719-27 pubmed..Based on these findings we propose that Tlg2p is a t-SNARE that functions in transport from the endosome to the late Golgi and on the endocytic pathway. ..
- Couve A, Gerst J. Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins. J Biol Chem. 1994;269:23391-4 pubmed..We have previously described the yeast homologs, Snc1 and Snc2, and demonstrated that they localize to secretory vesicles and are required for normal secretion...
- 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. ..
- Knop M, Miller K, Mazza M, Feng D, Weber M, Keränen S, et al. Molecular interactions position Mso1p, a novel PTB domain homologue, in the interface of the exocyst complex and the exocytic SNARE machinery in yeast. Mol Biol Cell. 2005;16:4543-56 pubmed..These results position Mso1p in the interface of the exocyst complex, Sec4p, and the SNARE machinery, and reveal a novel layer of molecular conservation in the exocytosis machinery. ..
- Brennwald P, Kearns B, Champion K, Keranen S, Bankaitis V, Novick P. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell. 1994;79:245-58 pubmed..Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases. ..
- 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. ..
- Neiman A, Katz L, Brennwald P. Identification of domains required for developmentally regulated SNARE function in Saccharomyces cerevisiae. Genetics. 2000;155:1643-55 pubmed..Deletion studies indicate that activation and inhibition are separable functions of the Spo20p N terminus. Our results reveal an additional layer of regulation of the SNARE complex, which is necessary only in sporulating cells. ..
- 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..The yeast homologs, Snc1 and Snc2, localize to secretory vesicles and are required for normal bulk secretion in Saccharomyces cerevisiae...
- Grote E, Baba M, Ohsumi Y, Novick P. Geranylgeranylated SNAREs are dominant inhibitors of membrane fusion. J Cell Biol. 2000;151:453-66 pubmed..In support of this model, the inverted cone-shaped lipid lysophosphatidylcholine rescues secretion from SNARE mutant cells. ..
- 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..By immunoprecipitation, it was found that Btn2 bound the yeast endocytic SNARE complex (e.g., Snc1 and Snc2 [Snc1/2], Tlg1, Tlg2, and Vti1), the Snx4 sorting nexin, and retromer (e.g., Vps26 and Vps35)...
- Su Z, Ishitsuka Y, Ha T, Shin Y. The SNARE complex from yeast is partially unstructured on the membrane. Structure. 2008;16:1138-46 pubmed publisher..Helix-breaking proline mutations in SN2 did not affect the rate of docking but reduced the rate of lipid mixing significantly, indicating that SN2 plays an essential role in activating the transition from docking to fusion. ..
- Boyd A, Ciufo L, Barclay J, Graham M, Haynes L, Doherty M, et al. A random mutagenesis approach to isolate dominant-negative yeast sec1 mutants reveals a functional role for domain 3a in yeast and mammalian Sec1/Munc18 proteins. Genetics. 2008;180:165-78 pubmed publisher..This effect of dominant-negative sec1 was suppressed by overexpression of the vesicle (v)-SNAREs, Snc1 and Snc2, but not the target (t)-SNAREs, Sec9 and Sso2...
- Shen D, Yuan H, Hutagalung A, Verma A, Kümmel D, Wu X, et al. The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p. J Cell Biol. 2013;202:509-26 pubmed publisher..An snc2 mutation that specifically disrupts this interaction led to exocyst mislocalization and a block in exocytosis in ..
- Williams D, Novick P. Analysis of SEC9 suppression reveals a relationship of SNARE function to cell physiology. PLoS ONE. 2009;4:e5449 pubmed publisher..Second, Sro7p acts to promote SNARE complex formation. Finally, Sec9p function and SNARE complex formation are tightly coupled to the physiological state of the cell. ..
- Marash M, Gerst J. Phosphorylation of the autoinhibitory domain of the Sso t-SNAREs promotes binding of the Vsm1 SNARE regulator in yeast. Mol Biol Cell. 2003;14:3114-25 pubmed..Thus, one way by which phosphorylation inhibits SNARE assembly could be by regulating the association of inhibitory factors that control the ability of t-SNAREs to form complexes in vivo. ..
- Tsui M, Banfield D. Yeast Golgi SNARE interactions are promiscuous. J Cell Sci. 2000;113 ( Pt 1):145-52 pubmed
- 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. Thus, one branch of the secretory pathway in yeast involves an intermediate sorting compartment and has a specific requirement for clathrin and a dynamin-related protein in SV biogenesis. ..
- David D, Sundarababu S, Gerst J. Involvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeast. J Cell Biol. 1998;143:1167-82 pubmed
- 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. ..
- Chen S, Shah A, Segev N. Ypt31/32 GTPases and their F-Box effector Rcy1 regulate ubiquitination of recycling proteins. Cell Logist. 2011;1:21-31 pubmed..Together, these results suggest a new role for ubiquitination in cargo recycling. Moreover, we propose that Ypt/Rabs integrate intra-cellular trafficking with ubiquitination. ..
- Yang H, Nakanishi H, Liu S, McNew J, Neiman A. Binding interactions control SNARE specificity in vivo. J Cell Biol. 2008;183:1089-100 pubmed publisher..mutant form of Spo20 displayed enhanced activity in in vitro fusion assays, as well as tighter binding to Sso1 and Snc2. These results demonstrate that differences within the SNARE helices can discriminate between closely related ..
- Lu X, Zhang Y, Shin Y. Supramolecular SNARE assembly precedes hemifusion in SNARE-mediated membrane fusion. Nat Struct Mol Biol. 2008;15:700-6 pubmed publisher..This higher-order protein intermediate evolves, by involving lipid molecules, to the hemifusion state. Hemifusion is subsequently followed by distal leaflet mixing and formation of the cis-SNARE complex. ..