The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs.
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.
Mesh Terms:
ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Carrier Proteins, Cell Compartmentation, Cells, Cultured, Clathrin-Coated Vesicles, Eukaryotic Cells, Humans, Intracellular Membranes, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Protein Transport, Rats, Swine, trans-Golgi Network
ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Carrier Proteins, Cell Compartmentation, Cells, Cultured, Clathrin-Coated Vesicles, Eukaryotic Cells, Humans, Intracellular Membranes, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Protein Transport, Rats, Swine, trans-Golgi Network
Dev. Cell
Date: Mar. 01, 2003
PubMed ID: 12636914
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