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