| First Author | Liu J | Year | 1999 |
| Journal | Oncogene | Volume | 18 |
| Issue | 48 | Pages | 6700-6 |
| PubMed ID | 10597276 | Mgi Jnum | J:58868 |
| Mgi Id | MGI:1350523 | Doi | 10.1038/sj.onc.1203050 |
| Citation | Liu J, et al. (1999) Src is required for cell migration and shape changes induced by fibroblast growth factor 1. Oncogene 18(48):6700-6 |
| abstractText | Fibroblast growth factor 1 (FGF-1) is a potent chemotactic factor and induces tyrosine phosphorylation of a cortical actin-associated protein (cortactin). The tyrosine phosphorylation of cortactin induced by FGF-1 requires the tyrosine residues 421, 482 and 466, which are targeted by the protein tyrosine kinase Src in vitro. Furthermore, FGF-1 is unable to induce tyrosine phosphorylation of cortactin within the cells derived from Src knockout mice (Src-/-), indicating that Src is required for the tyrosine phosphorylation of cortactin induced by FGF-1. Although Src-/- cells are able to undergo rapid proliferation, they are impaired to respond to FGF-1 for the shape change and cell migration. Morphological analysis further reveals that FGF-1 fails to induce the formation of polarized lamellipodia and the translocation of cortactin into the leading edge of Src-/- cells. Consistent with the mitogenic response to FGF-1, the lack of Src does not affect the tyrosine phosphorylation of Snt (or Frs2), a FGF-1 early signaling protein that links to Ras. Therefore, our data support the notion that Src and cortactin participate in a FGF signal pathway for cell migration and shape change rather than mitogenesis. |
