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

Jon E. Paczkowski, Brian C. Richardson, Amanda M. Strassner, J. Christopher Fromme

Research output: Contribution to journalArticlepeer-review

23 Scopus citations

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 overall architecture of the FBE domain is reminiscent of the appendage domains of other cargo adaptors, although it exhibits a distinct topology. In contrast to appendage domains, which bind accessory factors, we show that the primary role of the FBE domain is to bind Arf1 for recruitment of exomer to membranes.

Original languageEnglish (US)
Pages (from-to)4191-4203
Number of pages13
JournalEMBO Journal
Volume31
Issue number21
DOIs
StatePublished - Oct 31 2012

Keywords

  • Arf1
  • GTPase
  • cargo adaptor
  • membrane trafficking
  • trans-Golgi network

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