肌节
肌球蛋白
细胞生物学
生物物理学
化学
生物
心肌细胞
作者
Anthony L. Hessel,Nichlas M. Engels,Michel N. Kuehn,Devin Nissen,Rachel Sadler,Weikang Ma,Thomas C. Irving,Wolfgang A. Linke,S. Harris
标识
DOI:10.1038/s41467-024-46957-7
摘要
Abstract Muscle contraction is produced via the interaction of myofilaments and is regulated so that muscle performance matches demand. Myosin-binding protein C (MyBP-C) is a long and flexible protein that is tightly bound to the thick filament at its C-terminal end (MyBP-C C8C10 ), but may be loosely bound at its middle- and N-terminal end (MyBP-C C1C7 ) to myosin heads and/or the thin filament. MyBP-C is thought to control muscle contraction via the regulation of myosin motors, as mutations lead to debilitating disease. We use a combination of mechanics and small-angle X-ray diffraction to study the immediate and selective removal of the MyBP-C C1C7 domains of fast MyBP-C in permeabilized skeletal muscle. We show that cleavage leads to alterations in crossbridge kinetics and passive structural signatures of myofilaments that are indicative of a shift of myosin heads towards the ON state, highlighting the importance of MyBP-C C1C7 to myofilament force production and regulation.
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