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Related Experiment Video

Updated: Mar 25, 2026

Author Spotlight: Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
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Phosphorylation and calcium antagonistically tune myosin-binding protein C's structure and function.

Michael J Previs1, Ji Young Mun2, Arthur J Michalek1

  • 1Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT 05405;

Proceedings of the National Academy of Sciences of the United States of America
|February 25, 2016
PubMed
Summary

Phosphorylation of cardiac myosin-binding protein C

Keywords:
cMyBP-Cmuscle activationmuscle regulationstructure-function

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Area of Science:

  • Cardiovascular Biology
  • Muscle Physiology
  • Biochemistry

Background:

  • Cardiac contractility relies on calcium-regulated actin-myosin interactions.
  • Cardiac myosin-binding protein C (cMyBP-C) modulates these interactions.
  • Phosphorylation of cMyBP-C's M-domain influences its function.

Purpose of the Study:

  • To investigate the structural and functional impact of M-domain phosphorylation in cMyBP-C.
  • To elucidate the role of calcium levels in modulating these effects.

Main Methods:

  • Atomic force spectroscopy
  • Electron microscopy
  • Mutant protein expression
  • Motility assays

Main Results:

  • Phosphorylation reduces M-domain extensibility and compacts the N-terminal domain.
  • High calcium levels reverse these structural changes, increasing M-domain extensibility.
  • Phosphorylation's impact on sliding velocity is abolished by calcium.

Conclusions:

  • M-domain phosphorylation tunes cMyBP-C's calcium sensitization, particularly at low calcium levels.
  • At peak contraction, cMyBP-C remains a potent modulator irrespective of phosphorylation state.
  • This phosphorylation mechanism fine-tunes cardiac muscle contraction dynamics.