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Gene Review

VAM3  -  Vam3p

Saccharomyces cerevisiae S288c

Synonyms: PTH1, Syntaxin VAM3, Vacuolar morphogenesis protein 3, YOR106W, YOR3220W
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High impact information on VAM3

  • Furthermore, temperature-conditional mutations in the Class C VPS genes destabilized Vam3-Vti1-Vam7 pairing [1].
  • In contrast, deletions in genes that selectively confer vacuolar hydrolase sorting to the PVC or protein transport to the vacuole (i.e. VPS34 and VAM3, respectively) have no effect [2].
  • Here we show that mutations in VAM3 (vacuolar t-SNARE) and YPT7 (rab GTPase), which are required to direct protein and membrane delivery from prevacuolar endosomal compartments to the vacuole, dramatically increase/stabilize PtdIns(3)P levels in vivo by disrupting its turnover [3].
  • Surprisingly, despite their organelle-specific functions in sorting of vacuolar proteins, overexpression of VAM3 can suppress the protein sorting defects of pep12Delta cells [4].
  • Genetic interactions between VAM3 and a SEC1 family member, VPS33, suggest the two proteins may act together to direct the docking and/or fusion of multiple transport intermediates with the vacuole [5].

Biological context of VAM3


Anatomical context of VAM3

  • The PEP12 homolog Pth1p (Pep twelve homolog 1) is predicted to be similar in size to Pep12p, the endosomal syntaxin homolog that mediates docking of Golgi-derived transport vesicles and, like other members of the syntaxin family, is predicted to be a cytoplasmically oriented, integral membrane protein with a C-terminal transmembrane domain [8].
  • Subcellular fractionation localizes Pth1/Vam3p to vacuolar membranes [8].

Physical interactions of VAM3

  • VTI1 interacts genetically with the vacuolar t-SNARE VAM3, which is required for transport of both alkaline phosphatase and aminopeptidase I to the vacuole [9].

Regulatory relationships of VAM3


Other interactions of VAM3

  • Furthermore, VAM7 displayed genetic interactions with the vacuolar syntaxin homolog, VAM3 [10].
  • Here we report characterization of Vps33p, an SM family member previously thought to act exclusively at the vacuolar membrane with the vacuolar syntaxin Vam3p [11].
  • Using a combination of immunofluorescence localization and pulse/chase immunoprecipitation analysis, we demonstrate that, in addition to ALP, the vacuolar syntaxin Vam3p also follows this VPS45/27-independent pathway to the vacuole [12].
  • As a consequence efficient cis-SNARE complex disassembly that occurs at priming as a prerequisite of fusion requires addition of exogenous Sec18. trans-SNARE complexes in this mutant accumulate up to 4-fold over wild type, suggesting that the transmembrane domain of Vam3 is required to transit through this step [13].


  1. Class C Vps protein complex regulates vacuolar SNARE pairing and is required for vesicle docking/fusion. Sato, T.K., Rehling, P., Peterson, M.R., Emr, S.D. Mol. Cell (2000) [Pubmed]
  2. Dynamin and clathrin are required for the biogenesis of a distinct class of secretory vesicles in yeast. Gurunathan, S., David, D., Gerst, J.E. EMBO J. (2002) [Pubmed]
  3. Phosphoinositide signaling and turnover: PtdIns(3)P, a regulator of membrane traffic, is transported to the vacuole and degraded by a process that requires lumenal vacuolar hydrolase activities. Wurmser, A.E., Emr, S.D. EMBO J. (1998) [Pubmed]
  4. Acidic di-leucine motif essential for AP-3-dependent sorting and restriction of the functional specificity of the Vam3p vacuolar t-SNARE. Darsow, T., Burd, C.G., Emr, S.D. J. Cell Biol. (1998) [Pubmed]
  5. A multispecificity syntaxin homologue, Vam3p, essential for autophagic and biosynthetic protein transport to the vacuole. Darsow, T., Rieder, S.E., Emr, S.D. J. Cell Biol. (1997) [Pubmed]
  6. High expression of the yeast syntaxin-related Vam3 protein suppresses the protein transport defects of a pep12 null mutant. Götte, M., Gallwitz, D. FEBS Lett. (1997) [Pubmed]
  7. A syntaxin homolog encoded by VAM3 mediates down-regulation of a yeast G protein-coupled receptor. Stefan, C.J., Blumer, K.J. J. Biol. Chem. (1999) [Pubmed]
  8. Pth1/Vam3p is the syntaxin homolog at the vacuolar membrane of Saccharomyces cerevisiae required for the delivery of vacuolar hydrolases. Srivastava, A., Jones, E.W. Genetics (1998) [Pubmed]
  9. The Saccharomyces cerevisiae v-SNARE Vti1p is required for multiple membrane transport pathways to the vacuole. Fischer von Mollard, G., Stevens, T.H. Mol. Biol. Cell (1999) [Pubmed]
  10. Vam7p, a SNAP-25-like molecule, and Vam3p, a syntaxin homolog, function together in yeast vacuolar protein trafficking. Sato, T.K., Darsow, T., Emr, S.D. Mol. Cell. Biol. (1998) [Pubmed]
  11. The Sec1/Munc18 protein, Vps33p, functions at the endosome and the vacuole of Saccharomyces cerevisiae. Subramanian, S., Woolford, C.A., Jones, E.W. Mol. Biol. Cell (2004) [Pubmed]
  12. The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. Piper, R.C., Bryant, N.J., Stevens, T.H. J. Cell Biol. (1997) [Pubmed]
  13. The transmembrane domain of Vam3 affects the composition of cis- and trans-SNARE complexes to promote homotypic vacuole fusion. Rohde, J., Dietrich, L., Langosch, D., Ungermann, C. J. Biol. Chem. (2003) [Pubmed]
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