Cardiovascular Division, King's College London British Heart Foundation Centre of Research Excellence, The Rayne Institute, St Thomas' Hospital, London, UK.
J Muscle Res Cell Motil. 2012 May;33(1):53-60. doi: 10.1007/s10974-011-9276-3. Epub 2011 Nov 17.
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.
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。虽然迄今为止关于 cMyBP-C 磷酸化调节的大部分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/苏氨酸激酶，如 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 90kDa 核糖体 S6 激酶，也能够靶向这种关键的调节性肌小节蛋白。本文综述了这些证据，并提出了一些相关信号通路在心力衰竭时调节 cMyBP-C 磷酸化的假设作用。
