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γ-COP Appendage Domain – Structure and Function
Article first published online: 23 DEC 2003
DOI: 10.1111/j.1600-0854.2004.00158.x
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How to Cite
Watson, P. J., Frigerio, G., Collins, B. M., Duden, R. and Owen, D. J. (2004), γ-COP Appendage Domain – Structure and Function. Traffic, 5: 79–88. doi: 10.1111/j.1600-0854.2004.00158.x
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Joint first authors.
Publication History
- Issue published online: 23 DEC 2003
- Article first published online: 23 DEC 2003
- Received 8 October 2003,revised andaccepted for publication 11 November 2003
- Abstract
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Keywords:
- coatomer;
- Golgi;
- structure;
- trafficking;
- vesicle
COPI-coated vesicles mediate retrograde transport from the Golgi back to the ER and intra-Golgi transport. The cytosolic precursor of the COPI coat, the heptameric coatomer complex, can be thought of as composed of two subcomplexes. The first consists of the β-, γ-, δ- and ζ-COP subunits which are distantly homologous to AP clathrin adaptor subunits. The second consists of the α-, β′- and ε-COP subunits. Here, we present the structure of the appendage domain of γ-COP and show that it has a similar overall fold as the α-appendage of AP2. Again, like the α-appendage the γ-COP appendage possesses a single protein/protein interaction site on its platform subdomain. We show that in yeast this site binds to the ARFGAP Glo3p, and in mammalian γ-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of γ-COP, Sec21p, a second binding site is proposed to exist on the γ-COP appendage that interacts with the α,β′,ε COPI subcomplex.