Dev Cell. 2003 Mar;4(3):321-32.

The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.

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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.

PMID:: 12636914; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Crystal Structure Of The Human Gga1 Gat Domainÿ

PDB: 1NAF

Source: Homo sapiens

Method: X-Ray Diffraction

Resolution: 2.8 Å

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