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J. Biol. Chem., Vol. 282, Issue 13, 9805-9812, March 30, 2007

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Targeting of AMSH to Endosomes Is Required for Epidermal Growth Factor Receptor Degradation^*

Yu May Ma, Emmanuel Boucrot¹, Judit Villén, El Bachir Affar^¶, Steven P. Gygi, Heinrich G. Göttlinger^||, and Tomas Kirchhausen²

From the CBR Institute for Biomedical Research, Department of Cell Biology, ^¶Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115 and the ^||Program in Gene Function and Expression, University of Massachusetts Medical School, Worcester, Massachusetts 01605

To reach the lysosomes, down-regulated receptors such as the epidermal growth factor receptor must first be sorted into internal vesicles of late endosomes (multivesicular bodies), a ubiquitin-dependent event that requires the coordinated function of the endosome sorting complex required for transport (ESCRT) proteins. Here we report that CHMP3, an ESCRT-III complex component, and associated molecule of SH3 domain of STAM (AMSH), a deubiquitinating enzyme, interact with each other in cells. A dominant-negative version of CHMP3, which specifically prevents targeting of AMSH to endosomes, inhibits degradation but not internalization of EGFR, suggesting that endosomal AMSH is a functional component of the multivesicular body pathway.

Received for publication, December 19, 2006

^* This work was funded by National Institutes of Health Grants GM036548 (to T. K.) and AI29873 (to H. G. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ A Human Frontier Science Program Long-Term Fellow.

² To whom correspondence should be addressed: CBR Institute for Biomedical Research and Dept. of Cell Biology, Harvard Medical School, 200 Longwood Ave., Boston, MA 02115. Tel.: 617-278-3140; Fax: 617-278-3131; E-mail: Kirchhausen{at}crystal.harvard.edu.

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