Pflügers Archiv - European Journal of Physiology

, Volume 466, Issue 3, pp 439–444

Molecular modulation of actomyosin function by cardiac myosin-binding protein C

  • Michael J. Previs
  • Arthur J. Michalek
  • David M. Warshaw
Invited Review

DOI: 10.1007/s00424-013-1433-7

Cite this article as:
Previs, M.J., Michalek, A.J. & Warshaw, D.M. Pflugers Arch - Eur J Physiol (2014) 466: 439. doi:10.1007/s00424-013-1433-7

Abstract

Cardiac myosin-binding protein C is a key regulator of cardiac contractility and is capable of both activating the thin filament to initiate actomyosin motion generation and governing maximal sliding velocities. While MyBP-C’s C terminus localizes the molecule within the sarcomere, the N terminus appears to confer regulatory function by binding to the myosin motor domain and/or actin. Literature pertaining to how MyBP-C binding to the myosin motor domain and or actin leads to MyBP-C’s dual modulatory roles that can impact actomyosin interactions are discussed.

Keywords

Cardiac contractility Thick filament Thin filament Myosin Actin Regulation 

Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  • Michael J. Previs
    • 1
  • Arthur J. Michalek
    • 1
  • David M. Warshaw
    • 1
  1. 1.Department of Molecular Physiology & BiophysicsUniversity of VermontBurlingtonUSA