Binding partners for the COOH-Terminal appendage domains of the GGAs and gamma-adaptin

Lui, Winnie W. Y., Collins, Brett M., Hirst, Jennifer, Motley, Alison, Millar, Caroline, Schu, Peter, Owen, David J. and Robinson, Margaret S. (2003) Binding partners for the COOH-Terminal appendage domains of the GGAs and gamma-adaptin. Molecular Biology of The Cell, 14 6: 2385-2398. doi:10.1091/mbc.E02-11-0735

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Author Lui, Winnie W. Y.
Collins, Brett M.
Hirst, Jennifer
Motley, Alison
Millar, Caroline
Schu, Peter
Owen, David J.
Robinson, Margaret S.
Title Binding partners for the COOH-Terminal appendage domains of the GGAs and gamma-adaptin
Journal name Molecular Biology of The Cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2003-06
Sub-type Article (original research)
DOI 10.1091/mbc.E02-11-0735
Open Access Status File (Publisher version)
Volume 14
Issue 6
Start page 2385
End page 2398
Total pages 14
Place of publication Bethesda
Publisher American Society for Cell Biology
Language eng
Subject 0601 Biochemistry and Cell Biology
Abstract The adaptor appendage domains are believed to act as binding platforms for coated vesicle accessory proteins. Using glutathione S-transferase pulldowns from pig brain cytosol, we find three proteins that can bind to the appendage domains of both the AP-1 gamma subunit and the GGAs: gamma-synergin and two novel proteins, p56 and p200. p56 elicited better antibodies than p200 and was generally more tractable. Although p56 and gamma-synergin bind to both GGA and gamma appendages in vitro, immunofluorescence labeling of nocodazole-treated cells shows that p56 colocalizes with GGAs on TGN46-positive membranes, whereas gamma-synergin colocalizes with AP-1 primarily on a different membrane compartment. Furthermore, in AP-1-deficient cells, p56 remains membrane-associated whereas gamma-synergin becomes cytosolic. Thus, p56 and gamma-synergin show very strong preferences for GGAs and AP-1, respectively, in vivo. However, the GGA and gamma appendages share the same fold as determined by x-ray crystallography, and mutagenesis reveals that the same amino acids contribute to their binding sites. By overexpressing wild-type GGA and gamma appendage domains in cells, we can drive p56 and gamma-synergin, respectively, into the cytosol, suggesting a possible mechanism for selectively disrupting the two pathways.
Keyword Cell Biology
Trans-golgi Network
Structural Basis
Containing Protein
Vhs Domains
Clathrin
Ap-1
Recruitment
Crystallography
Recognition
Family
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 19 Sep 2007, 17:43:53 EST