The BioGRID | PUBLICATION VIEW

	Dev. Cell Mar (2003); 4(3):321-32
The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.
Collins BM, Watson PJ, Owen DJ
Department of Clinical Biochemistry, University of Cambridge, Hills Road, CB2 2XY, Cambridge, United Kingdom. bmc25@cam.ac.uk
Abstract: The GGAs are a family of clathrin adaptor proteins involved in vesicular transport between the trans-Golgi network and endosomal system. Here we confirm reports that GGAs are targeted to the Golgi via interaction between the GGA-GAT domain and ARF-GTP, and we present the structure of the GAT domain of human GGA1, completing the structural description of the folded domains of GGA proteins. The GGA-GAT domain possesses an all alpha-helical fold with a "paper clip" topology comprising two independent subdomains. Structure-based mutagenesis demonstrates that ARF1-GTP binding by GGAs is exclusively governed by the N-terminal "hook" subdomain, and, using an in vitro recruitment assay, we show that ARF-GTP binding by this small structure is required and sufficient for Golgi targeting of GGAs.
[PUBMED: 12636914]