Cardiac myosin binding protein C phosphorylation is markedly reduced in both end-stage heart failure and familial hypertrophic cardiomyopathy, contributing to sarcomeric dysfunction.
Perturbations in sarcomeric function may in part underlie systolic and diastolic dysfunction of the failing heart. Sarcomeric dysfunction has been ascribed to changes in phosphorylation status of sarcomeric proteins caused by an altered balance between intracellular kinases and phosphatases during the development of cardiac disease. In the present review we discuss changes in phosphorylation of the thick filament protein myosin binding protein C (cMyBP-C) reported in failing myocardium, with emphasis on phosphorylation changes observed in familial hypertrophic cardiomyopathy caused by mutations in MYBPC3. Moreover, we will discuss assays which allow to distinguish between functional consequences of mutant sarcomeric proteins and (mal)adaptive changes in sarcomeric protein phosphorylation.
Kuster et al. (Wed,) conducted a review in Heart failure and familial hypertrophic cardiomyopathy. Cardiac myosin binding protein C (cMyBP-C) phosphorylation was evaluated. Cardiac myosin binding protein C phosphorylation is markedly reduced in both end-stage heart failure and familial hypertrophic cardiomyopathy, contributing to sarcomeric dysfunction.
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