A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease - PubMed (original) (raw)

. 2004 Sep 24;15(6):853-65.

doi: 10.1016/j.molcel.2004.09.016.

Maciej Lalowski, Ulrich Stelzl, Stephanie Waelter, Martin Stroedicke, Uwe Worm, Anja Droege, Katrin S Lindenberg, Maria Knoblich, Christian Haenig, Martin Herbst, Jaana Suopanki, Eberhard Scherzinger, Claudia Abraham, Bianca Bauer, Renate Hasenbank, Anja Fritzsche, Andreas H Ludewig, Konrad Büssow, Sarah H Coleman, Claire-Anne Gutekunst, Bernhard G Landwehrmeyer, Hans Lehrach, Erich E Wanker

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• PMID: 15383276
• DOI: 10.1016/j.molcel.2004.09.016

Free article

A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease

Heike Goehler et al. Mol Cell. 2004.

Free article

Erratum in

• Mol Cell. 2005 Jul 22;19(2):287. Buessow, Konrad [corrected to Büssow, Konrad]

Abstract

Analysis of protein-protein interactions (PPIs) is a valuable approach for characterizing proteins of unknown function. Here, we have developed a strategy combining library and matrix yeast two-hybrid screens to generate a highly connected PPI network for Huntington's disease (HD). The network contains 186 PPIs among 35 bait and 51 prey proteins. It revealed 165 new potential interactions, 32 of which were confirmed by independent binding experiments. The network also permitted the functional annotation of 16 uncharacterized proteins and facilitated the discovery of GIT1, a G protein-coupled receptor kinase-interacting protein, which enhances huntingtin aggregation by recruitment of the protein into membranous vesicles. Coimmunoprecipitations and immunofluorescence studies revealed that GIT1 and huntingtin associate in mammalian cells under physiological conditions. Moreover, GIT1 localizes to neuronal inclusions, and is selectively cleaved in HD brains, indicating that its distribution and function is altered during disease pathogenesis.

Copyright 2004 Cell Press

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