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Gene Review

SEC3  -  Sec3p

Saccharomyces cerevisiae S288c

Synonyms: Exocyst complex component SEC3, PSL1, Protein PSL1, YER008C
 
 
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High impact information on SEC3

  • One component of the complex, Sec3, is thought to be a spatial landmark for polarized exocytosis [1].
  • The SEC3 gene in high copy suppresses pfy1-111 and sec5-24 and causes synthetic growth defects with ypt1, sec8-9, sec10-2, and sec15-1 [2].
  • Two new temperature-sensitive alleles of SEC3, 1 of 10 late-acting SEC genes required for targeting or fusion of post-Golgi secretory vesicles to the plasma membrane in Saccharomyces cerevisiae, were isolated in a screen for temperature-sensitive secretory mutants that are synthetically lethal with sec4-8 [2].
  • All of the sec3 alleles genetically interact with a profilin mutation, pfy1-111 [2].
  • All alleles of sec3 cause bud site selection defects in homozygous diploids, as do sec4-8 and sec9-4 [2].
 

Anatomical context of SEC3

  • A soluble form of this Vbeta mutant was a potent inhibitor of SEC3-mediated T cell activity, suggesting that these engineered proteins may be useful as antagonists [3].
  • Functional assays revealed that Sec3 increased the transporter capacity of GLYT1, suggesting that the exocyst favors insertion of GLYT1 into the plasma membrane [4].
 

Associations of SEC3 with chemical compounds

  • The glycine transporter GLYT1 interacts with Sec3, a component of the exocyst complex [4].
 

Physical interactions of SEC3

  • Residues Phe77, Ile115 and Leu131 of Sec3 bind to an extended hydrophobic surface formed around switch regions I and II of Rho1 [5].
 

Other interactions of SEC3

  • SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection [6].

References

  1. Spatial regulation of the exocyst complex by Rho1 GTPase. Guo, W., Tamanoi, F., Novick, P. Nat. Cell Biol. (2001) [Pubmed]
  2. Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae. Finger, F.P., Novick, P. Mol. Biol. Cell (1997) [Pubmed]
  3. High affinity T cell receptors from yeast display libraries block T cell activation by superantigens. Kieke, M.C., Sundberg, E., Shusta, E.V., Mariuzza, R.A., Wittrup, K.D., Kranz, D.M. J. Mol. Biol. (2001) [Pubmed]
  4. The glycine transporter GLYT1 interacts with Sec3, a component of the exocyst complex. Cubelos, B., Giménez, C., Zafra, F. Neuropharmacology (2005) [Pubmed]
  5. Structural basis for the Rho- and phosphoinositide-dependent localization of the exocyst subunit Sec3. Yamashita, M., Kurokawa, K., Sato, Y., Yamagata, A., Mimura, H., Yoshikawa, A., Sato, K., Nakano, A., Fukai, S. Nat. Struct. Mol. Biol. (2010) [Pubmed]
  6. SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection. Haarer, B.K., Corbett, A., Kweon, Y., Petzold, A.S., Silver, P., Brown, S.S. Genetics (1996) [Pubmed]
 
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