The GAT Domains of Clathrin-associated GGA Proteins Have Two Ubiquitin Binding Motifs

Patricia S. Bilodeau; Stanley C. Winistorfer; Margaret M. Allaman; Kavitha Surendhran; William R. Kearney; Andrew D. Robertson; Robert C. Piper

doi:10.1074/jbc.M406654200

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The GAT Domains of Clathrin-associated GGA Proteins Have Two Ubiquitin Binding Motifs

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The GAT Domains of Clathrin-associated GGA Proteins Have Two Ubiquitin Binding Motifs

Patricia S. Bilodeau, Stanley C. Winistorfer, Margaret M. Allaman, Kavitha Surendhran, William R. Kearney, Andrew D. Robertson and Robert C. Piper

The Journal of biological chemistry, Vol.279(52), pp.54808-54816

12/24/2004

DOI: 10.1074/jbc.M406654200

PMCID: PMC2911622

PMID: 15494413

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Abstract

Ubiquitin (Ub) attachment to membrane proteins can serve as a sorting signal for lysosomal delivery. Recognition of Ub as a sorting signal can occur at the trans-Golgi network and is mediated in part by the clathrin-associated Golgi-localizing, γ-adaptin ear domain homology, ARF-binding proteins (GGA). GGA proteins bind Ub via a three-helix bundle subdomain in their GAT (GGA and target of Myb1 protein) domain, which is also present in the Ub binding domain of target of Myb1 protein. Ubiquitin binding by yeast Ggas is required to direct sorting of ubiquitinated proteins such as general amino acid permease (Gap1) from the trans-Golgi network to endosomes. Using affinity chromatography and nuclear magnetic resonance spectroscopy, we have found that the human GGA3 GAT domain contains two Ub binding motifs that bind to the same surface of ubiquitin. These motifs are found within different helices within the three-helix GAT subdomain. When functionally analyzed in yeast, each motif was sufficient to mediate trans-Golgi network to endosomal sorting of Gap1, and mutation of both motifs resulted in defective Gap1 sorting without defects in other GGA-dependent processes.

Details

Title: Subtitle: The GAT Domains of Clathrin-associated GGA Proteins Have Two Ubiquitin Binding Motifs
Creators: Patricia S. Bilodeau - University of Iowa
Stanley C. Winistorfer - University of Iowa
Margaret M. Allaman - University of Iowa
Kavitha Surendhran - University of Iowa
William R. Kearney - University of Iowa
Andrew D. Robertson - University of Iowa
Robert C. Piper - University of Iowa
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.279(52), pp.54808-54816
DOI: 10.1074/jbc.M406654200
PMID: 15494413
PMCID: PMC2911622
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: Elsevier Inc
Language: English
Date published: 12/24/2004
Academic Unit: Radiology; Molecular Physiology and Biophysics; Medicine Administration; Internal Medicine
Record Identifier: 9984297606602771

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