High impact information on SEC5

• A truncation mutant of Sec5 (sec5(E13)) allows the formation of normally sized oocytes but with greatly reduced yolk uptake [1].
• The exocyst component Sec5 is present on endocytic vesicles in the oocyte of Drosophila melanogaster [1].
• Human Sec3 (hSec3) shares 17% sequence identity with yeast Sec3p, interacts in the two-hybrid system with other subunits of the complex (Sec5 and Sec8), and is expressed in almost all tissues tested [2].
• We provide evidence that mammalian exocyst components are present as distinct subcomplexes on vesicles and the plasma membrane and that Ral GTPases regulate the assembly interface of a full octameric exocyst complex through interaction with Sec5 and Exo84 [3].
• A conditional sterol esterification defect in yeast having either a sec1 or sec5 mutation in the secretory pathway [4].

Anatomical context of SEC5

• When grown at 37 degrees C on defined medium, the strains with sec5 or sec1 accumulated the usual secretory vesicles, but when grown under similar conditions with elevated levels of inositol, accumulated an additional vesicular-like body [4].

Associations of SEC5 with chemical compounds

• Two temperature-conditional secretory mutations, sec1 and sec5, cause the accumulation of post-Golgi vesicles when strains containing these mutations are grown at 37 degrees C. In addition to accumulating vesicles, the mutants do not esterify free sterol on rich media at the restrictive temperature [4].

References