Sec24 is a coincidence detector that simultaneously binds two signals to drive ER export.

ABSTRACT:

Background

Incorporation of secretory proteins into ER-derived vesicles involves recognition of cytosolic signals by the COPII coat protein, Sec24. Additional cargo diversity is achieved through cargo receptors, which include the Erv14/Cornichon family that mediates export of transmembrane proteins despite the potential for such clients to directly interact with Sec24. The molecular function of Erv14 thus remains unclear, with possible roles in COPII binding, membrane domain chaperoning, and lipid organization.

Results

Using a targeted mutagenesis approach to define the mechanism of Erv14 function, we identify conserved residues in the second transmembrane domain of Erv14 that mediate interaction with a subset of Erv14 clients. We further show that interaction of Erv14 with

SUBMITTER: Pagant S 

PROVIDER: S-EPMC4334704 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature