Molecular modulation of actomyosin function by cardiac myosin-binding protein C
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- Previs, M.J., Michalek, A.J. & Warshaw, D.M. Pflugers Arch - Eur J Physiol (2014) 466: 439. doi:10.1007/s00424-013-1433-7
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Cardiac myosin-binding protein C is a key regulator of cardiac contractility and is capable of both activating the thin filament to initiate actomyosin motion generation and governing maximal sliding velocities. While MyBP-C’s C terminus localizes the molecule within the sarcomere, the N terminus appears to confer regulatory function by binding to the myosin motor domain and/or actin. Literature pertaining to how MyBP-C binding to the myosin motor domain and or actin leads to MyBP-C’s dual modulatory roles that can impact actomyosin interactions are discussed.