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

Laura Picas, Julien Viaud, Kristine Schauer, Stefano Vanni, Karim Hnia, Vincent Fraisier, Aurélien Roux, Patricia Bassereau, Frédérique Gaits-Iacovoni, Bernard Payrastre, Jocelyn Laporte, Jean-Baptiste Manneville () and Bruno Goud ()
Additional contact information
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

Nature Communications, 2014, vol. 5, issue 1, 1-12

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms6647

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