High impact information on SEC15

• However, loss of sec15 does not cause cell lethality in contrast to loss of sec5 or sec6 [1].
• Loss of sec15 causes a targeting defect of photoreceptors that coincides with mislocalization of specific cell adhesion and signaling molecules [1].
• Concurrently, we biochemically purified the remaining unidentified polypeptides of the Sec6-Sec8-Sec15 complex for peptide microsequencing [2].
• SEC15 encodes a 116-kD protein that is essential for vesicular traffic from the Golgi apparatus to the cell surface in yeast [3].
• Sec15 protein, an essential component of the exocytotic apparatus, is associated with the plasma membrane and with a soluble 19.5S particle [3].

Biological context of SEC15

• Previously, we have shown that three of these genes, SEC6, SEC8 and SEC15, encode components of a multisubunit complex which localizes to the tip of the bud, the predominant site of exocytosis in S. cerevisiae [2].
• The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic in yeast [4].
• When this interaction is compromised, as in the case of cells lacking the N-terminal 138 residues of Bem1p, including the first Src-homology 3 (SH3) domain, the localization of green fluorescent protein (GFP)-tagged Sec15 is affected, especially in the early stage of bud growth [5].

Anatomical context of SEC15

• Two of these genes, SEC8 and SEC15, encode components of a 1-2-million D multi-subunit complex that is found in the cytoplasm and associated with the plasma membrane [6].
• Overproduction of Sec15 protein interferes with the secretory pathway, resulting in the formation of a cluster of secretory vesicles, and a patch of Sec15 protein revealed by immunofluorescence [4].

Physical interactions of SEC15

• Sec6 and Sec15 coimmunoprecipitate from lysates with c-myc-tagged Sec8 [6].

Other interactions of SEC15

• The Sec2 protein may function in conjunction with the Sec4 and Sec15 proteins to control vesicular traffic [7].
• We propose that Sec15 protein responds to the function of the Sec4 protein to control vesicular traffic [4].
• By co-immunoprecipitation we show that Sec10, which forms an exocyst subcomplex with Sec15, specifically associates with the Sec61beta component of the translocon and that Sec10 overexpression increases the association of other exocyst complex members with Sec61beta [8].

References