Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads

Anthony L. Hessel (), Nichlas M. Engels, Michel N. Kuehn, Devin Nissen, Rachel L. Sadler, Weikang Ma, Thomas C. Irving, Wolfgang A. Linke and Samantha P. Harris ()
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Anthony L. Hessel: University of Muenster
Nichlas M. Engels: University of Arizona
Michel N. Kuehn: University of Muenster
Devin Nissen: Illinois Institute of Technology
Rachel L. Sadler: University of Arizona
Weikang Ma: Illinois Institute of Technology
Thomas C. Irving: Illinois Institute of Technology
Wolfgang A. Linke: University of Muenster
Samantha P. Harris: University of Arizona

Nature Communications, 2024, vol. 15, issue 1, 1-10

Abstract: 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-CC8C10), but may be loosely bound at its middle- and N-terminal end (MyBP-CC1C7) 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-CC1C7 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-CC1C7 to myofilament force production and regulation.

Date: 2024
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DOI: 10.1038/s41467-024-46957-7

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