Key result
Unphosphorylated c-MyBPC decelerated ATP-induced dissociation of myosin from actin (K1k+2 0.12-0.22 M-1s-1 vs 0.42 M-1s-1 for myosin alone), an effect abolished by phosphorylation.
Population
In vitro model using cardiac myosin binding protein C (c-MyBPC), myosin, and actin
Comparison
Phosphorylation of c-MyBPC vs Unphosphorylated c-MyBPC
Design
Preclinical
Authors
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Supports direct c-MyBPC phosphorylation effects on cross-bridge kinetics in animals; leaves open human translation and therapeutic relevance.
Phosphorylation of c-MyBPC directly regulates cross-bridge kinetics independently of the thin filament, fine-tuning cardiac contractile behavior.
Coulton et al. (2012) studied Cardiac muscle contraction. c-MyBPC and its phosphorylation vs. Myosin alone / unphosphorylated c-MyBPC was evaluated on Binding of myosin to actin and ATP-induced dissociation of myosin from actin. Unphosphorylated c-MyBPC decelerated ATP-induced dissociation of myosin from actin (K1k+2 0.12-0.22 M-1s-1 vs 0.42 M-1s-1 for myosin alone), an effect abolished by phosphorylation.
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