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A Family of ADP-Ribosylation Factor Effectors That Can Alter Membrane Transport through the trans-Golgi

Boman, Annette L., Zhang, Chun-jiang, Zhu, Xinjun, Kahn, Richard A.·2000·Molecular Biology of the Cell
DOI 10.1091/mbc.11.4.1241
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Abstract

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 (≈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 γ-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, γ-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.

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Metadata

Authors
Boman, A. L., Zhang, C.-J., Zhu, X., & Kahn, R. A.
Venue
Molecular Biology of the Cell
Publisher
American Society for Cell Biology (ASCB)
Published
2000-04
Volume
11
Issue
4
Pages
1241-1255
ISSN
  • 1059-1524
  • 1939-4586
DOI
10.1091/mbc.11.4.1241
Cited by
237
References
2
Language
en

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