| Summary: | 碩士 === 國立成功大學 === 藥理學研究所 === 91 === Eps8 was initially identified as a substrate of EGF receptor tyrosine kinase. Our previous studies have indicated that Eps8 could also be phosphorylated by both v-Src and active c-Src. Interestingly, both the expression and tyrosyl phosphorylation of Eps8 are enhanced in v-Src transformed cells. Thus, protein phosphorylation and expression of Eps8 may contribute to Src-mediated mitogenesis and oncogenesis. Previously, we have observed at least three potential Src-mediated Tyrosine residues on p97Eps8 and Tyr-45 was one of them, which was not present on p68Eps8. In this study, we utilized Site-directed mutagenesis and Mass spectrophotometer to identify the Src-mediated phosphorylation sites on p68Eps8. We found that both Tyr-524 and Tyr-674 on p68Eps8 were the two preferential phosphorylation residues mediated by Src both in vivo and in vitro.
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