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

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33 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)53-60
Number of pages8
JournalJournal of Muscle Research and Cell Motility
Volume33
Issue number1
DOIs
Publication statusPublished - May 2012

Keywords

  • Heart failure
  • TROPONIN-I PHOSPHORYLATION
  • RIBOSOMAL S6 KINASE
  • CARDIAC TROPONIN
  • Protein kinase D
  • Protein kinases
  • MEDIATED PHOSPHORYLATION
  • cMyBP-C
  • BINDING-PROTEIN-C
  • A PHOSPHORYLATION
  • Phosphorylation
  • NA+-H+ EXCHANGER
  • p90 ribosomal S6 kinase
  • Adrenergic receptors
  • FAILING HUMAN-HEART
  • CONTRACTILE FUNCTION
  • MYOFILAMENT CA2+ SENSITIVITY

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