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首页> 外文期刊>Journal of Muscle Research and Cell Motility >CMyBP-C as a promiscuous substrate: Phosphorylation by non-PKA kinases and its potential significance
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CMyBP-C as a promiscuous substrate: Phosphorylation by non-PKA kinases and its potential significance

机译:CMyBP-C作为混杂底物:非PKA激酶的磷酸化及其潜在意义

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摘要

It is now generally accepted that phosphorylation of cMyBP-C is critically important in maintaining normal cardiac function. Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca 2+/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein. This article reviews such evidence and proposes a hypothetical role for some of the pertinent signalling pathways in phospho-regulation of cMyBP-C in the setting of heart failure.
机译:现在,人们普遍认为cMyBP-C的磷酸化对于维持正常的心脏功能至关重要。尽管迄今为止有关cMyBP-C磷酸调节的许多工作都集中在蛋白激酶A(PKA,也称为cAMP依赖性蛋白激酶)的作用上,但最近的证据表明,许多非PKA丝氨酸/苏氨酸Ca 2 + /钙调蛋白依赖性蛋白激酶II,蛋白激酶C,蛋白激酶D和90-kDa核糖体S6激酶等激酶也能够靶向这种关键的调节性肌节蛋白。本文回顾了这些证据,并提出了在心力衰竭中cMyBP-C磷酸调节中某些相关信号通路的假设作用。

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