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cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance

Research output: Contribution to journalLiterature reviewpeer-review

Original languageEnglish
Pages (from-to)53-60
Number of pages8
JournalJournal of Muscle Research and Cell Motility
Issue number1
PublishedMay 2012

King's Authors


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 Ca2+/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.

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