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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
The Journal of biological chemistry, 12/2009, Letnik: 284, Številka: 49Journal Article
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.
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