| First Author | Lock P | Year | 1998 |
| Journal | EMBO J | Volume | 17 |
| Issue | 15 | Pages | 4346-57 |
| PubMed ID | 9687503 | Mgi Jnum | J:49136 |
| Mgi Id | MGI:1276760 | Doi | 10.1093/emboj/17.15.4346 |
| Citation | Lock P, et al. (1998) A new method for isolating tyrosine kinase substrates used to identify fish, an SH3 and PX domain-containing protein, and Src substrate. EMBO J 17(15):4346-57 |
| abstractText | We describe a method for identifying tyrosine kinase substrates using anti-phosphotyrosine antibodies to screen tyrosine-phosphorylated cDNA expression libraries. Several potential Src substrates were identified including Fish, which has five SH3 domains and a recently discovered phox homology (PX) domain. Fish is tyrosine-phosphorylated in Src-transformed fibroblasts (suggesting that it is a target of Src in vivo) and in normal cells following treatment with several growth factors. Treatment of cells with cytochalasin D also resulted in rapid tyrosine phosphorylation of Fish, concomitant with activation of Src. These data suggest that Fish is involved in signalling by tyrosine kinases, and imply a specialized role in the actin cytoskeleton. |
