PHOSPHORYLATION OF C-SRC ON TYROSINE-527 BY ANOTHER PROTEIN TYROSINE KINASE

被引:95
作者
THOMAS, JE
SORIANO, P
BRUGGE, JS
机构
[1] UNIV PENN, SCH MED, HOWARD HUGHES MED INST, DEPT MICROBIOL, PHILADELPHIA, PA 19104 USA
[2] BAYLOR COLL MED, HOWARD HUGHES MED INST, INST MOLEC GENET, HOUSTON, TX 77030 USA
关键词
D O I
10.1126/science.1719633
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The protein tyrosine kinase activity of the cellular Src protein is negatively regulated by phosphorylation at tyrosine residue 527 (Tyr527). It has not been established whether this regulatory modification of Src is mediated by autophosphorylation or by another cellular protein kinase. The phosphorylation of a modified form of c-Src that lacks kinase activity was examined in mouse cells that do not express endogenous Src (because of the targeted disruption of both src alleles). Phosphorylation of the inactive form of Src on Tyr527 occurred to a similar extent in cells lacking endogenous Src as it did in cells expressing Src. Therefore, Tyr527 phosphorylation, and thus negative control of Src kinase activity, is mediated by another cellular protein tyrosine kinase.
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页码:568 / 571
页数:4
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