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 language | English |
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Pages (from-to) | 53-60 |
Number of pages | 8 |
Journal | Journal of Muscle Research and Cell Motility |
Volume | 33 |
Issue number | 1 |
DOIs | |
Publication status | Published - 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