心肌肌球蛋白结合蛋白 C 对肌动球蛋白功能的分子调节。
Molecular modulation of actomyosin function by cardiac myosin-binding protein C.
机构信息
Department of Molecular Physiology & Biophysics, University of Vermont, 149 Beaumont Ave., HSRF Building Rm.-116, Burlington, VT, 05405, USA.
出版信息
Pflugers Arch. 2014 Mar;466(3):439-44. doi: 10.1007/s00424-013-1433-7. Epub 2014 Jan 10.
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.
摘要
心肌球蛋白结合蛋白 C 是心肌收缩力的关键调节因子，能够激活细肌丝启动肌球蛋白运动的产生，并控制最大滑行速度。虽然 MyBP-C 的 C 端将分子定位于肌节内，但 N 端似乎通过与肌球蛋白马达结构域和/或肌动蛋白结合赋予调节功能。本文讨论了 MyBP-C 与肌球蛋白马达结构域和/或肌动蛋白的结合如何导致 MyBP-C 的双重调节作用，从而影响肌球蛋白与肌动蛋白的相互作用。
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