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Lipid-mediated PX-BAR domain recruitment couples local membrane constriction to endocytic vesicle fission

Author

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  • Johannes Schöneberg

    (Freie Universität Berlin
    Present address: Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California 94720, USA)

  • Martin Lehmann

    (Leibniz-Institut für Molekulare Pharmakologie
    Faculty of Biology, Chemistry, Pharmacy, Freie Universität Berlin)

  • Alexander Ullrich

    (Freie Universität Berlin)

  • York Posor

    (Leibniz-Institut für Molekulare Pharmakologie
    Faculty of Biology, Chemistry, Pharmacy, Freie Universität Berlin)

  • Wen-Ting Lo

    (Leibniz-Institut für Molekulare Pharmakologie)

  • Gregor Lichtner

    (Freie Universität Berlin
    Leibniz-Institut für Molekulare Pharmakologie)

  • Jan Schmoranzer

    (Leibniz-Institut für Molekulare Pharmakologie
    Faculty of Biology, Chemistry, Pharmacy, Freie Universität Berlin
    Present address: Charité Universitätsmedizin Berlin, Virchowweg 6, 10117 Berlin, Germany)

  • Volker Haucke

    (Leibniz-Institut für Molekulare Pharmakologie
    Faculty of Biology, Chemistry, Pharmacy, Freie Universität Berlin
    NeuroCure Cluster of Excellence, Charité Universitätsmedizin Berlin)

  • Frank Noé

    (Freie Universität Berlin)

Abstract

Clathrin-mediated endocytosis (CME) involves membrane-associated scaffolds of the bin-amphiphysin-rvs (BAR) domain protein family as well as the GTPase dynamin, and is accompanied and perhaps triggered by changes in local lipid composition. How protein recruitment, scaffold assembly and membrane deformation is spatiotemporally controlled and coupled to fission is poorly understood. We show by computational modelling and super-resolution imaging that phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] synthesis within the clathrin-coated area of endocytic intermediates triggers selective recruitment of the PX-BAR domain protein SNX9, as a result of complex interactions of endocytic proteins competing for phospholipids. The specific architecture induces positioning of SNX9 at the invagination neck where its self-assembly regulates membrane constriction, thereby providing a template for dynamin fission. These data explain how lipid conversion at endocytic pits couples local membrane constriction to fission. Our work demonstrates how computational modelling and super-resolution imaging can be combined to unravel function and mechanisms of complex cellular processes.

Suggested Citation

  • Johannes Schöneberg & Martin Lehmann & Alexander Ullrich & York Posor & Wen-Ting Lo & Gregor Lichtner & Jan Schmoranzer & Volker Haucke & Frank Noé, 2017. "Lipid-mediated PX-BAR domain recruitment couples local membrane constriction to endocytic vesicle fission," Nature Communications, Nature, vol. 8(1), pages 1-17, August.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms15873
    DOI: 10.1038/ncomms15873
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