Abstract
Cardiac muscle contraction depends on precise interactions between thin (actin) and thick (myosin) filaments (TFs). TFs are regulated by intracellular Ca2+ levels as well as other sarcomeric proteins, such as cardiac myosin binding protein C (cMyBP-C) and myosin. Recent studies have shown the first four N-terminal domains (NTDs) of cMyBP-C (i.e. C0, C1, M and C2), are effective modulators of the TF activity. Their collective activation of the TF is regulated by the phosphorylation of the M domain but the mechanism is not fully understood.
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