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BIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin

Author

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  • Laura Picas

    (Institut Curie and CNRS UMR 144)

  • Julien Viaud

    (INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires)

  • Kristine Schauer

    (Institut Curie and CNRS UMR 144)

  • Stefano Vanni

    (Institut de Pharmacologie Moléculaire et Cellulaire, Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique)

  • Karim Hnia

    (IGBMC, U964, UMR7104, Strasbourg University, Collège de France)

  • Vincent Fraisier

    (Institut Curie and CNRS UMR 144, Cell and Tissue Imaging Platform)

  • Aurélien Roux

    (University of Geneva)

  • Patricia Bassereau

    (Institut Curie and CNRS UMR 168)

  • Frédérique Gaits-Iacovoni

    (INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires)

  • Bernard Payrastre

    (INSERM, UMR1048, Université Toulouse III, Institut des Maladies Métaboliques et Cardiovasculaires)

  • Jocelyn Laporte

    (IGBMC, U964, UMR7104, Strasbourg University, Collège de France)

  • Jean-Baptiste Manneville

    (Institut Curie and CNRS UMR 144)

  • Bruno Goud

    (Institut Curie and CNRS UMR 144)

Abstract

Phosphoinositides play a central role in many physiological processes by assisting the recruitment of proteins to membranes through specific phosphoinositide-binding motifs. How this recruitment is coordinated in space and time is not well understood. Here we show that BIN1/M-Amphiphysin2, a protein involved in T-tubule biogenesis in muscle cells and frequently mutated in centronuclear myopathies, clusters PtdIns(4,5)P2 to recruit its downstream partner dynamin. By using several mutants associated with centronuclear myopathies, we find that the N-BAR and the SH3 domains of BIN1 control the kinetics and the accumulation of dynamin on membranes, respectively. We show that phosphoinositide clustering is a mechanism shared by other proteins that interact with PtdIns(4,5)P2, but do not contain a BAR domain. Our numerical simulations point out that clustering is a diffusion-driven process in which phosphoinositide molecules are not sequestered. We propose that this mechanism plays a key role in the recruitment of downstream phosphoinositide-binding proteins.

Suggested Citation

  • Laura Picas & Julien Viaud & Kristine Schauer & Stefano Vanni & Karim Hnia & Vincent Fraisier & Aurélien Roux & Patricia Bassereau & Frédérique Gaits-Iacovoni & Bernard Payrastre & Jocelyn Laporte & J, 2014. "BIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin," Nature Communications, Nature, vol. 5(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6647
    DOI: 10.1038/ncomms6647
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    Cited by:

    1. Harrison M. York & Kunaal Joshi & Charles S. Wright & Laura Z. Kreplin & Samuel J. Rodgers & Ullhas K. Moorthi & Hetvi Gandhi & Abhishek Patil & Christina A. Mitchell & Srividya Iyer-Biswas & Senthil , 2023. "Deterministic early endosomal maturations emerge from a stochastic trigger-and-convert mechanism," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Maritzaida Varela Salgado & Ingrid E. Adriaans & Sandra A. Touati & Sandy Ibanes & Joséphine Lai-Kee-Him & Aurélie Ancelin & Luca Cipelletti & Laura Picas & Simonetta Piatti, 2024. "Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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