| First Author | Ramesh N | Year | 2014 |
| Journal | Mol Cell Biol | Volume | 34 |
| Issue | 14 | Pages | 2600-10 |
| PubMed ID | 24797074 | Mgi Jnum | J:223687 |
| Mgi Id | MGI:5660074 | Doi | 10.1128/MCB.00017-14 |
| Citation | Ramesh N, et al. (2014) Binding of the WASP/N-WASP-interacting protein WIP to actin regulates focal adhesion assembly and adhesion. Mol Cell Biol 34(14):2600-10 |
| abstractText | The actin cytoskeleton is essential for cell adhesion and migration, functions important for tumor invasion. In addition to binding N-WASP/WASP, WIP binds and stabilizes F-actin. WIP(-/-) fibroblasts were used to test the role of WIP in F-actin function. WIP(-/-) cells had defective focal adhesion (FA), stress fiber assembly, and adherence to substrates, functions that were restored by transduction of wild-type WIP. Protein and mRNA levels of several FA constituents regulated by the myocardin-related transcription factor (MRTF)-serum response factor (SRF) transcription factor complex were reduced in WIP(-/-) fibroblasts. The level of G-actin, which sequesters MRTF in the cytoplasm, was increased, and nuclear localization of MRTF-A and SRF was reduced, in WIP(-/-) fibroblasts. Transfection of an MRTF-A mutant that constitutively translocates to the nucleus or transfection of constitutively active SRF restored FA and stress fiber assembly. Fibroblasts from knock-in mice expressing a WIP mutant that fails to bind actin phenocopied WIP(-/-) fibroblasts. Thus, WIP is a novel regulator of FA assembly and cell adhesion. |
