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    Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation

    Ma, Y.M. and Boucrot, Emmanuel and Villén, J. and Affar, E.B. and Gygi, S.P. and Göttlinger, H.G. and Kirchhausen, T. (2007) Targeting of AMSH to endosomes is required for epidermal growth factor receptor degradation. Journal of Biological Chemistry 282 (13), pp. 9805-9812. ISSN 0021-9258.

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    Abstract

    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 30 Apr 2019 15:48
    Last Modified: 27 Jul 2019 13:52
    URI: http://eprints.bbk.ac.uk/id/eprint/27374

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