| First Author | Yamada H | Year | 2009 |
| Journal | J Biol Chem | Volume | 284 |
| Issue | 49 | Pages | 34244-56 |
| PubMed ID | 19759398 | Mgi Jnum | J:157410 |
| Mgi Id | MGI:4430785 | Doi | 10.1074/jbc.M109.064204 |
| Citation | Yamada H, et al. (2009) Dynamic interaction of amphiphysin with N-WASP regulates actin assembly. J Biol Chem 284(49):34244-56 |
| abstractText | 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. |
