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Phosphorylation and Prolyl Isomerization Independently Regulate the Signal Adapter Function of Crkll

机译:磷酸化和脯氨酰异构化独立调节Crkll的信号适配器功能

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The signaling protein Crkll switches between forms with high or low binding affinity. Both phosphorylation and native-state prolyl isomerization were suggested to regulate the transition between these forms. Here we analyzed how phosphorylation at Tyr222 and Tyr252 and the Pro238Ala substitution affect signal transfer of human and chicken Crkll to a downstream target. Human Crkll is regulated by phosphorylation only, but chicken Crkll is regulated by Pro238 trans -> cis isomerization and by Tyr222 phosphorylation. Surprisingly, they act in an independent fashion. Apparently, the allosteric transition to a low-activity form can be induced by phosphorylation or prolyl isomerization located at distant sites in Crkll. (C) 2014 Elsevier Ltd. All rights reserved.
机译:信号蛋白CrkII在具有高或低结合亲和力的形式之间切换。磷酸化和天然状态的脯氨酰异构化均被建议来调节这些形式之间的过渡。在这里,我们分析了Tyr222和Tyr252处的磷酸化以及Pro238Ala取代如何影响人和鸡CrkII向下游靶标的信号转移。人CrkII仅受磷酸化调节,但是鸡CrkII受Pro238反式->顺式异构化和Tyr222磷酸化调节。令人惊讶的是,它们以独立的方式运行。显然,可以通过位于CrkII远处的磷酸化或脯氨酰异构化来诱导向低活性形式的变构转变。 (C)2014 Elsevier Ltd.保留所有权利。

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