Endophilin marks and controls a clathrin-independent endocytic pathway

Emmanuel Boucrot (), Antonio P. A. Ferreira, Leonardo Almeida-Souza, Sylvain Debard, Yvonne Vallis, Gillian Howard, Laetitia Bertot, Nathalie Sauvonnet and Harvey T. McMahon ()
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Emmanuel Boucrot: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK
Antonio P. A. Ferreira: Institute of Structural and Molecular Biology, University College London & Birkbeck College, London WC1E 6BT, UK
Leonardo Almeida-Souza: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK
Sylvain Debard: Institute of Structural and Molecular Biology, University College London & Birkbeck College, London WC1E 6BT, UK
Yvonne Vallis: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK
Gillian Howard: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK
Laetitia Bertot: Institut Pasteur, Unité de Pathogenie Moleculaire Microbienne, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France
Nathalie Sauvonnet: Institut Pasteur, Unité de Pathogenie Moleculaire Microbienne, 28 rue du Docteur Roux, 75724 Paris Cedex 15, France
Harvey T. McMahon: MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge CB2 0QH, UK

Nature, 2015, vol. 517, issue 7535, 460-465

Abstract: 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).

Date: 2015
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DOI: 10.1038/nature14067

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