| First Author | Zhang M | Year | 2006 |
| Journal | EMBO J | Volume | 25 |
| Issue | 22 | Pages | 5284-93 |
| PubMed ID | 17082770 | Mgi Jnum | J:200425 |
| Mgi Id | MGI:5508619 | Doi | 10.1038/sj.emboj.7601406 |
| Citation | Zhang M, et al. (2006) CAP interacts with cytoskeletal proteins and regulates adhesion-mediated ERK activation and motility. EMBO J 25(22):5284-93 |
| abstractText | CAP/Ponsin belongs to the SoHo family of adaptor molecules that includes ArgBP2 and Vinexin. These proteins possess an N-terminal sorbin homology (SoHo) domain and three C-terminal SH3 domains that bind to diverse signaling molecules involved in a variety of cellular processes. Here, we show that CAP binds to the cytoskeletal proteins paxillin and vinculin. CAP localizes to cell-extracellular matrix (ECM) adhesion sites, and this process requires binding to vinculin. Overexpression of CAP induces the aggregation of paxillin, vinculin and actin at cell-ECM adhesion sites. Moreover, CAP inhibits adhesion-dependent processes such as cell spreading and focal adhesion turnover, whereas a CAP mutant that is unable to localize to cell-ECM adhesion sites is incapable of exerting these effects. Finally, depletion of CAP by siRNA-mediated knockdown leads to enhanced cell spreading, migration and the activation of the PAK/MEK/ERK pathway in REF52 cells. Taken together, these results indicate that CAP is a cytoskeletal adaptor protein involved in modulating adhesion-mediated signaling events that lead to cell migration. |
