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Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependent fission, was also shown to have a regulatory role in actin dynamics. Here, we report that amphiphysin 1 interacts with N-WASP and stimulates N-WASP- and Arp2/3-dependent actin polymerization. Both the Src homology 3 and the N-BAR domains are required for this stimulation. Acidic liposome-triggered, N-WASP-dependent actin polymerization is strongly impaired in brain cytosol of amphiphysin 1 knock-out mice. FRET-FLIM analysis of Sertoli cells, where endogenously expressed amphiphysin 1 co-localizes with N-WASP in peripheral ruffles, confirmed the association between the two proteins in vivo. This association undergoes regulation and is enhanced by stimulating phosphatidylserine receptors on the cell surface with phosphatidylserine-containing liposomes that trigger ruffle formation. These results indicate that actin regulation is a key function of amphiphysin 1 and that such function cooperates with the endocytic adaptor role and membrane shaping/curvature sensing properties of the protein during the endocytic reaction.

Original publication

DOI

10.1074/jbc.M109.064204

Type

Journal article

Journal

J Biol Chem

Publication Date

04/12/2009

Volume

284

Pages

34244 - 34256

Keywords

Actins, Animals, Brain, Cell Membrane, Cytosol, Endocytosis, Fluorescence Resonance Energy Transfer, Gene Expression Regulation, Liposomes, Male, Mice, Mice, Knockout, Nerve Tissue Proteins, Rats, Receptors, Cell Surface, Sertoli Cells, Wiskott-Aldrich Syndrome Protein, Neuronal