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Dynamic interaction of amphiphysin with N-WASP regulates actin assembly.

Abstract : 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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https://hal.archives-ouvertes.fr/hal-00503018
Contributor : Antonia Kropfinger <>
Submitted on : Friday, July 16, 2010 - 12:57:17 PM
Last modification on : Saturday, April 11, 2020 - 1:59:14 AM

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Hiroshi Yamada, Sergi Padilla-Parra, Sun-Joo Park, Toshiki Itoh, Mathilde Chaineau, et al.. Dynamic interaction of amphiphysin with N-WASP regulates actin assembly.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2009, 284 (49), pp.34244-56. ⟨10.1074/jbc.M109.064204⟩. ⟨hal-00503018⟩

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