, Volume 466, Issue 3, pp 439-444
Date: 10 Jan 2014

Molecular modulation of actomyosin function by cardiac myosin-binding protein C

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Abstract

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.

This article is published as part of the Special Issue on MYBPC3 mini-review series.