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Gene Review

SNC2  -  SNAP receptor SNC2

Saccharomyces cerevisiae S288c

Synonyms: Synaptobrevin homolog 2, YOR327C
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High impact information on SNC2

  • Here we describe the cloning of SNC2 and demonstrate that yeast lacking both SNC genes are deficient in normal bulk secretion, accumulate large numbers of post-Golgi vesicles, and display a variety of conditional lethal phenotypes [1].
  • When a 3Q/1R ratio is restored by a mirror R-->Q substitution in the R-SNARE Snc2p, wild-type functionality is observed [2].
  • In a screen for suppressors of a temperature-sensitive mutation in the yeast SNAP-25 homolog, Sec9, we have identified a gain-of-function mutation in the yeast synaptobrevin homolog, Snc2 [3].
  • The location of the mutations suggests that the C-terminal H2 helical domain of Sec9 is likely to be aligned in parallel with Snc2 in the SNARE complex [3].
  • In yeast, the assembly of the target (t)-SNAREs [Tlg2p/Tlg1p,Vti1p] and [Pep12p/Tlg1p,Vti1p] with the vesicular (v)-SNARE Snc2p promotes endocytic fusion [4].

Biological context of SNC2


Anatomical context of SNC2

  • In 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 [7].
  • In addition, we report that Tlg2p forms a SEC18-dependent SNARE complex with Snc2p, a vesicle SNARE known to function in Golgi to plasma membrane trafficking [8].

Regulatory relationships of SNC2

  • We found that the CTM of Snc2p targeted the enhanced cyan fluorescent protein (ECFP)-protein A fusion protein on the cytoplasmic face of the plasma membrane more strongly than that of Ras2p [9].

Other interactions of SNC2

  • However, Snc2p binds in vivo to many other syntaxin-like t-SNAREs, and binding of Sncp to the endosomal/Golgi t-SNARE Tlg2p is also reduced in sec4-8 cells [10].
  • The C-terminal transmembrane domain (CTM) of Ras2p and Snc2p was examined as the portions with anchoring ability to the cytoplasmic face of the plasma membrane [9].


  1. Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Protopopov, V., Govindan, B., Novick, P., Gerst, J.E. Cell (1993) [Pubmed]
  2. Exocytosis requires asymmetry in the central layer of the SNARE complex. Ossig, R., Schmitt, H.D., de Groot, B., Riedel, D., Keränen, S., Ronne, H., Grubmüller, H., Jahn, R. EMBO J. (2000) [Pubmed]
  3. 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. Katz, L., Hanson, P.I., Heuser, J.E., Brennwald, P. EMBO J. (1998) [Pubmed]
  4. Concerted auto-regulation in yeast endosomal t-SNAREs. Paumet, F., Rahimian, V., Di Liberto, M., Rothman, J.E. J. Biol. Chem. (2005) [Pubmed]
  5. Yeast synaptobrevin homologs are modified posttranslationally by the addition of palmitate. Couve, A., Protopopov, V., Gerst, J.E. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  6. Ca(2+)-synaptotagmin directly regulates t-SNARE function during reconstituted membrane fusion. Bhalla, A., Chicka, M.C., Tucker, W.C., Chapman, E.R. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  7. Yeast exocytic v-SNAREs confer endocytosis. Gurunathan, S., Chapman-Shimshoni, D., Trajkovic, S., Gerst, J.E. Mol. Biol. Cell (2000) [Pubmed]
  8. Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. Abeliovich, H., Grote, E., Novick, P., Ferro-Novick, S. J. Biol. Chem. (1998) [Pubmed]
  9. Detection of protein-protein interactions by a combination of a novel cytoplasmic membrane targeting system of recombinant proteins and fluorescence resonance energy transfer. Shibasaki, S., Kuroda, K., Duc Nguyen, H., Mori, T., Zou, W., Ueda, M. Appl. Microbiol. Biotechnol. (2006) [Pubmed]
  10. Promiscuity in Rab-SNARE interactions. Grote, E., Novick, P.J. Mol. Biol. Cell (1999) [Pubmed]
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