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The regulatory light chain mediates inactivation of myosin motors during active shortening of cardiac muscle

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  • Thomas Kampourakis

    (King’s College London
    King’s College London)

  • Malcolm Irving

    (King’s College London
    King’s College London)

Abstract

The normal function of heart muscle depends on its ability to contract more strongly at longer length. Increased venous filling stretches relaxed heart muscle cells, triggering a stronger contraction in the next beat- the Frank-Starling relation. Conversely, heart muscle cells are inactivated when they shorten during ejection, accelerating relaxation to facilitate refilling before the next beat. Although both effects are essential for the efficient function of the heart, the underlying mechanisms were unknown. Using bifunctional fluorescent probes on the regulatory light chain of the myosin motor we show that its N-terminal domain may be captured in the folded OFF state of the myosin dimer at the end of the working-stroke of the actin-attached motor, whilst its C-terminal domain joins the OFF state only after motor detachment from actin. We propose that sequential folding of myosin motors onto the filament backbone may be responsible for shortening-induced de-activation in the heart.

Suggested Citation

  • Thomas Kampourakis & Malcolm Irving, 2021. "The regulatory light chain mediates inactivation of myosin motors during active shortening of cardiac muscle," Nature Communications, Nature, vol. 12(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25601-8
    DOI: 10.1038/s41467-021-25601-8
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    Cited by:

    1. Priyanka Parijat & Seetharamaiah Attili & Zoe Hoare & Michael Shattock & Victor Kenyon & Thomas Kampourakis, 2023. "Discovery of a novel cardiac-specific myosin modulator using artificial intelligence-based virtual screening," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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