The exomer cargo adaptor structure reveals a novel GTPase-binding domain.

ABSTRACT: Cargo adaptors control intracellular trafficking of transmembrane proteins by sorting them into membrane transport carriers. The COPI, COPII, and clathrin cargo adaptors are structurally well characterized, but other cargo adaptors remain poorly understood. Exomer is a specialized cargo adaptor that sorts specific proteins into trans-Golgi network (TGN)-derived vesicles in response to cellular signals. Exomer is recruited to the TGN by the Arf1 GTPase, a universally conserved trafficking regulator. Here, we report the crystal structure of a tetrameric exomer complex composed of two copies each of the Chs5 and Chs6 subunits. The structure reveals the FN3 and BRCT domains of Chs5, which together we refer to as the FBE domain (FN3-BRCT of exomer), project from the exomer core complex. The ove

SUBMITTER: Paczkowski JE 

PROVIDER: S-EPMC3492730 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature