Dynamic interaction of amphiphysin with N-WASP regulates actin assembly

Hiroshi Yamada, Sergi Padilla-Parra, Sun Joo Park, Toshiki Itoh, Mathilde Chaineau, Ilaria Monaldi, Ottavio Cremona, Fabio Benfenati, Pietro De Camilli, Maïté Coppey-Moisan, Marc Tramier, Thierry Galli, Kohji Takei

Research output: Contribution to journalArticlepeer-review

55 Citations (Scopus)


Amphiphysin 1, an endocytic adaptor concentrated at synapses that couples clathrin-mediated endocytosis to dynamin-dependentfission, wasalsoshowntohavearegulatoryroleinactindynamics. 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 colocalizes 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 languageEnglish
Pages (from-to)34244-34256
Number of pages13
JournalJournal of Biological Chemistry
Issue number49
Publication statusPublished - Dec 4 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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