Dynamic Interaction of Amphiphysin with N-WASP Regulates Actin Assembly

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...

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Bibliographic Details
Published in:The Journal of biological chemistry 2009-12, Vol.284 (49), p.34244-34256
Main Authors: Yamada, Hiroshi, Padilla-Parra, Sergi, Park, Sun-Joo, Itoh, Toshiki, Chaineau, Mathilde, Monaldi, Ilaria, Cremona, Ottavio, Benfenati, Fabio, De Camilli, Pietro, Coppey-Moisan, Maïté, Tramier, Marc, Galli, Thierry, Takei, Kohji
Format: Article
Language:English
Subjects:
Actins
Actins - chemistry
Actins - metabolism
Animals
Biochemistry, Molecular Biology
Brain
Brain - metabolism
Cell Membrane
Cell Membrane - metabolism
Cytosol
Cytosol - metabolism
Endocytosis
Fluorescence Resonance Energy Transfer
Gene Expression Regulation
Life Sciences
Liposomes
Liposomes - chemistry
Male
Membrane Transport, Structure, Function, and Biogenesis
Mice
Mice, Knockout
Nerve Tissue Proteins
Nerve Tissue Proteins - metabolism
Rats
Receptors, Cell Surface
Receptors, Cell Surface - metabolism
Sertoli Cells
Sertoli Cells - metabolism
Wiskott-Aldrich Syndrome Protein, Neuronal
Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M109.064204