| First Author | Ishibe S | Year | 2003 |
| Journal | Mol Cell | Volume | 12 |
| Issue | 5 | Pages | 1275-85 |
| PubMed ID | 14636584 | Mgi Jnum | J:86622 |
| Mgi Id | MGI:2680875 | Doi | 10.1016/s1097-2765(03)00406-4 |
| Citation | Ishibe S, et al. (2003) Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol Cell 12(5):1275-85 |
| abstractText | Activation of the hepatocyte growth factor (HGF) receptor c-met results in the regulation of cell-matrix interactions, including the MAPK-dependent stimulation of epithelial cell morphogenesis. In the present study we demonstrate that HGF stimulates the localization of ERK to sites of cell-matrix interactions and that this is mediated by the tyrosine phosphorylation-dependent association of inactive ERK and the focal adhesion complex protein paxillin. In addition, paxillin was found to associate with the upstream MAP kinases Raf and MEK, resulting in a complex that can mediate localized ERK activation. Mutation of the ERK binding site in paxillin prevented HGF-stimulated ERK-paxillin association and eliminated HGF-induced cell spreading and branching process formation. These experiments reveal that paxillin-dependent ERK activation at sites of cell-matrix interaction is critical for HGF-stimulated epithelial morphogenesis. |
