Journal
EMBO JOURNAL
Volume 31, Issue 21, Pages 4191-4203Publisher
WILEY
DOI: 10.1038/emboj.2012.268
Keywords
Arf1; cargo adaptor; GTPase; membrane trafficking; trans-Golgi network
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Funding
- National Science Foundation
- National Institutes of Health/National Institute of General Medical Sciences under NSF [DMR-0225180]
- National Institutes of Health, through its National Center for Research Resources [RR-01646]
- Offices of Biological and Environmental Research
- Basic Energy Sciences of the US Department of Energy
- National Center for Research Resources of the National Institutes of Health [P41RR012408]
- JCF from Cornell University
- NIH [T32GM07273]
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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. The EMBO Journal (2012) 31, 4191-4203. doi: 10.1038/emboj.2012.268; Published online 21 September 2012
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