BIROn - Birkbeck Institutional Research Online

    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.

    Text (Refereed)
    J. Biol. Chem.-2007-Ma-9805-12.pdf - Published Version of Record

    Download (532kB) | Preview


    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.


    Item Type: Article
    School: Birkbeck Faculties and Schools > Faculty of Science > School of Natural Sciences
    Depositing User: Sarah Hall
    Date Deposited: 30 Apr 2019 15:48
    Last Modified: 02 Aug 2023 17:51


    Activity Overview
    6 month trend
    6 month trend

    Additional statistics are available via IRStats2.

    Archive Staff Only (login required)

    Edit/View Item Edit/View Item