A family of ADP-ribosylation factor effectors that can alter membrane transport through the trans-Golgi.

A family of three structurally related proteins were cloned from human cDNA libraries by their ability to interact preferentially with the activated form of human ADP-ribosylation factor 3 (ARF3) in two-hybrid assays. The specific and GTP-dependent binding was later confirmed through direct protein binding of recombinant proteins. The three proteins ...
share large ( approximately 300 residues) domains at their N termini that are 60-70% identical to each other and a shorter (73 residues) domain at their C termini with 70% homology to the C-terminal "ear" domain of gamma-adaptin. Although GGA1 is found predominantly as a soluble protein by cell fractionation, all three proteins were found to localize to the trans-Golgi network (TGN) by indirect immunofluorescence. The binding of GGAs to TGN was sensitive to brefeldin A, consistent with this being an ARF-dependent event. Thus, these proteins have been named Golgi-localizing, gamma-adaptin ear homology domain, ARF-binding proteins, or GGAs. The finding that overexpression of GGAs was sufficient to alter the distribution of markers of the TGN (TGN38 and mannose 6-phosphate receptors) led us to propose that GGAs are effectors for ARFs that function in the regulation of membrane traffic through the TGN.
Mesh Terms:
ADP-Ribosylation Factors, Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Biological Transport, Blotting, Northern, Carrier Proteins, Cells, Cultured, Fibroblasts, Fluorescent Antibody Technique, Indirect, Golgi Apparatus, Humans, Immunoblotting, Intracellular Membranes, Kidney, Molecular Sequence Data, Organ Specificity, Protein Structure, Tertiary, Proteins, Rats, Sequence Alignment, Two-Hybrid System Techniques, Yeasts
Mol. Biol. Cell
Date: Apr. 01, 2000
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