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

Author

Listed:
  • Anthony L. Hessel

    (University of Muenster
    Accelerated Muscle Biotechnologies Consultants)

  • Nichlas M. Engels

    (University of Arizona)

  • Michel N. Kuehn

    (University of Muenster
    Accelerated Muscle Biotechnologies Consultants)

  • 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)

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.

Suggested Citation

  • Anthony L. Hessel & Nichlas M. Engels & Michel N. Kuehn & Devin Nissen & Rachel L. Sadler & Weikang Ma & Thomas C. Irving & Wolfgang A. Linke & Samantha P. Harris, 2024. "Myosin-binding protein C regulates the sarcomere lattice and stabilizes the OFF states of myosin heads," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-46957-7
    DOI: 10.1038/s41467-024-46957-7
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    References listed on IDEAS

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    1. Alessandro Grinzato & Daniel Auguin & Carlos Kikuti & Neha Nandwani & Dihia Moussaoui & Divya Pathak & Eaazhisai Kandiah & Kathleen M. Ruppel & James A. Spudich & Anne Houdusse & Julien Robert-Paganin, 2023. "Cryo-EM structure of the folded-back state of human β-cardiac myosin," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    2. Marco Linari & Elisabetta Brunello & Massimo Reconditi & Luca Fusi & Marco Caremani & Theyencheri Narayanan & Gabriella Piazzesi & Vincenzo Lombardi & Malcolm Irving, 2015. "Force generation by skeletal muscle is controlled by mechanosensing in myosin filaments," Nature, Nature, vol. 528(7581), pages 276-279, December.
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