作者: James S. Hardwick , Bartholomew M. Sefton
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摘要: Members of the Src family non-receptor tyrosine protein kinases are known to be inhibited by intramolecular association between a phosphorylated carboxyl-terminal residue and SH2 domain. We have previously shown that exposure cells H2O2 strongly activates Lck, lymphocyte-specific kinase, inducing phosphorylation on Tyr-394, an absolutely conserved within activation loop catalytic Here we show Lck has been activated is simultaneously at both (Tyr-505) Tyr-394. Thus, dephosphorylation Tyr-505 not prerequisite for either Tyr-394 or kinase. These results indicate dominant over any inhibition induced Tyr-505. propose these may extended all members.