September 12, 2025The Journal of Physiology

Myosin‐binding protein C slows cardiac myofibril relaxation kinetics

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Authors

ADAlexey V. DvornikovUniversity of Arizona SHSamantha P. HarrisNewYork–Presbyterian Hospital

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Observational analysis shows that cardiac myosin binding protein C influences relaxation kinetics in myofibrils, indicating mechanistic insights into hypertrophic cardiomyopathy.

Key Points

Acute loss of cardiac myosin binding protein C speeds up both relaxation phases in myofibrils, leading to enhanced kinetics after calcium activation.
Point mutation L348P in cMyBP-C slows relaxation phases, suggesting altered affinity for actin.
Phosphorylation of cMyBP-C enhances the fast relaxation phase while myosin inhibitor mavacamten accelerates relaxation independent of cMyBP-C.
Mutations in MYBPC3 are present in 20%–25% of hypertrophic cardiomyopathy cases, pointing to the importance of cMyBP-C's role in heart conditions.

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Dvornikov et al. (2025) studied this question.

synapsesocial.com/papers/68d413ee713b0b5dfea617f8 https://doi.org/10.1113/jp289201

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Implication

Observational analysis shows that cardiac myosin binding protein C influences relaxation kinetics in myofibrils, indicating mechanistic insights into hypertrophic cardiomyopathy.

Myosin‐binding protein C slows cardiac myofibril relaxation kinetics

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Cite This Study

Myosin‐binding protein C slows cardiac myofibril relaxation kinetics

Discussion

Member takes

Implication

Key Points

Cite This Study

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