| First Author | Nada S | Year | 1994 |
| Journal | Oncogene | Volume | 9 |
| Issue | 12 | Pages | 3571-8 |
| PubMed ID | 7526315 | Mgi Jnum | J:22064 |
| Mgi Id | MGI:69955 | Citation | Nada S, et al. (1994) Identification of major tyrosine-phosphorylated proteins in Csk-deficient cells. Oncogene 9(12):3571-8 |
| abstractText | Csk is a non-receptor protein-tyrosine kinase that acts as a negative regulator of Src family tyrosine kinases. Csk-deficient mouse embryos exhibited developmental defects including inability to turn and impaired formation of neural tube. In these embryos, an accumulation of tyrosine phosphorylated proteins was observed as a consequence of constitutive activation of Src family kinases. In order to identify those tyrosine phosphorylated proteins, we established a Csk-deficient cell line from embryos lacking both Csk and the anti-oncogene product p53. On surveying several proteins known as Src substrates, we found that phosphorylation level of p80/85 (cortactin) was markedly elevated in the Csk-deficient cells. Enhancement of cortactin phosphorylation was also seen in Csk-deficient embryos. Furthermore, immunoprecipitated Src was able to directly phosphorylate cortactin in vitro. Thus, we suggest that cortactin is a good substrate of activated Src family kinases in vivo and may play important roles in signaling pathways mediated by Src family kinases. |
