Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 284, Issue 49, Pages 34244-34256Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M109.064204
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Funding
- National Institutes of Health
- Ministry of Education, Science, Sports, and Culture of Japan
- United States-Japan Brain Research Collaborative
- INSERM
- INSERM-Japan Society for the Promotion of Science
- Foundation pour la Recherche Medicale
- CNRS
- European Union-Marie-Curie [MRTN-CT-2005-019481]
- Ministero dell'Istruzione, dell'Universita e della Ricerca (Italy)
- Compagnia di San Paolo, Torino, Italy
- Ministry of Education, Science, and Technology [2009-0065739]
- Fondazione Telethon Funding Source: Custom
- National Research Foundation of Korea [2009-0065739] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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. Acidicliposome-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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