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

被引：0
作者：
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
Bruno Goud
机构：
[1] Institut Curie and CNRS UMR 144,Department of Translational Medicine
[2] INSERM,Biochemistry Department
[3] UMR1048,undefined
[4] Université Toulouse III,undefined
[5] Institut des Maladies Métaboliques et Cardiovasculaires,undefined
[6] Institut de Pharmacologie Moléculaire et Cellulaire,undefined
[7] Université de Nice Sophia-Antipolis and Centre National de la Recherche Scientifique,undefined
[8] IGBMC,undefined
[9] U964,undefined
[10] UMR7104,undefined
[11] Strasbourg University,undefined
[12] Collège de France,undefined
[13] Institut Curie and CNRS UMR 144,undefined
[14] Cell and Tissue Imaging Platform,undefined
[15] University of Geneva,undefined
[16] Institut Curie and CNRS UMR 168,undefined
来源：
Nature Communications | / 5卷
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摘要：
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.
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