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    Endophilin marks and controls a clathrin-independent endocytic pathway

    Boucrot, Emmanuel and Ferreira, Antonio P.A. and Almeida-Souza, L. and Debard, Sylvain and Vallis, Y. and Howard, G. and Bertot, L. and Sauvonnet, N. and McMahon, H.T. (2015) Endophilin marks and controls a clathrin-independent endocytic pathway. Nature 517 , pp. 460-465. ISSN 0028-0836.

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    Abstract

    Endocytosis is required for internalization of micronutrients and turnover of membrane components. Endophilin has been assigned as a component of clathrin-mediated endocytosis. Here we show in mammalian cells that endophilin marks and controls a fast-acting tubulovesicular endocytic pathway that is independent of AP2 and clathrin, activated upon ligand binding to cargo receptors, inhibited by inhibitors of dynamin, Rac, phosphatidylinositol-3-OH kinase, PAK1 and actin polymerization, and activated upon Cdc42 inhibition. This pathway is prominent at the leading edges of cells where phosphatidylinositol-3,4-bisphosphate—produced by the dephosphorylation of phosphatidylinositol-3,4,5-triphosphate by SHIP1 and SHIP2—recruits lamellipodin, which in turn engages endophilin. This pathway mediates the ligand-triggered uptake of several G-protein-coupled receptors such as α2a- and β1-adrenergic, dopaminergic D3 and D4 receptors and muscarinic acetylcholine receptor 4, the receptor tyrosine kinases EGFR, HGFR, VEGFR, PDGFR, NGFR and IGF1R, as well as interleukin-2 receptor. We call this new endocytic route fast endophilin-mediated endocytosis (FEME).

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Research Centre: Structural Molecular Biology, Institute of (ISMB)
    Depositing User: Administrator
    Date Deposited: 18 Dec 2014 12:07
    Last Modified: 06 Dec 2016 11:15
    URI: http://eprints.bbk.ac.uk/id/eprint/11322

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