| First Author | Applewhite DA | Year | 2007 |
| Journal | Mol Biol Cell | Volume | 18 |
| Issue | 7 | Pages | 2579-91 |
| PubMed ID | 17475772 | Mgi Jnum | J:127459 |
| Mgi Id | MGI:3763782 | Doi | 10.1091/mbc.E06-11-0990 |
| Citation | Applewhite DA, et al. (2007) Ena/VASP proteins have an anti-capping independent function in filopodia formation. Mol Biol Cell 18(7):2579-91 |
| abstractText | Filopodia have been implicated in a number of diverse cellular processes including growth-cone path finding, wound healing, and metastasis. The Ena/VASP family of proteins has emerged as key to filopodia formation but the exact mechanism for how they function has yet to be fully elucidated. Using cell spreading as a model system in combination with small interfering RNA depletion of Capping Protein, we determined that Ena/VASP proteins have a role beyond anticapping activity in filopodia formation. Analysis of mutant Ena/VASP proteins demonstrated that the entire EVH2 domain was the minimal domain required for filopodia formation. Fluorescent recovery after photobleaching data indicate that Ena/VASP proteins rapidly exchange at the leading edge of lamellipodia, whereas virtually no exchange occurred at filopodial tips. Mutation of the G-actin-binding motif (GAB) partially compromised stabilization of Ena/VASP at filopodia tips. These observations led us to propose a model where the EVH2 domain of Ena/VASP induces and maintains clustering of the barbed ends of actin filaments, which putatively corresponds to a transition from lamellipodial to filopodial localization. Furthermore, the EVH1 domain, together with the GAB motif in the EVH2 domain, helps to maintain Ena/VASP at the growing barbed ends. |
