Muscle Contraction Mechanism Based on Actin Filament Rotation

  • Toshio Yanagida
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 592)


Muscle contraction is caused by relative sliding movement between interdigitating actin and myosin filaments. It has been thought that myosin heads protruding from the myosin filament rotate between two orientations, while they repeat detachment from and attachment to actin filament coupled to the ATP hydrolysis cycle and the rotation of the head may cause the sliding. Recently atomic structure obtained from X-ray crystallography supports the rotation of the myosin head relative to the actin filament. A small conformational change in the ATP binding domain is transmitted to a neck domain that connects a motor domain (head) and tail domain, depending on the chemical state of nucleotide bound. Thus the neck domain acts as a lever-arm that can cause a displacement of 5–10 nm for the muscle myosin. This lever-arm swinging model has been a paradigm not only for the muscle myosin but also for unconventional myosins. Large stepsize of unconventional processive myosin V motor can be explained by its large lever arm within the frame of the lever-arm swinging model.


Scanning Probe Myosin Head Actin Monomer Myosin Molecule Myosin Versus 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

30.5. References

  1. Galkin, V. E., VanLoock, M. S., Orlova, A., and Egelman, E. H., 2002. A new internal mode in F-actin helps explain the remarkable evolutionary conservation of actin’s sequence and structure. Curr. Biol. 12(7):570–575.PubMedCrossRefGoogle Scholar
  2. Harada, Y., Sakurada, Y., Aoki, T., Thomas, D. D., and Yanagida, T., 1990. Mechanochemmical coupling in actomyosin energy transduction studied by in vitro movement assay. J. Mol. Biol. 216:49–68.PubMedCrossRefGoogle Scholar
  3. Higuchi, H., and Goldman, Y. E., 1991, Sliding distance between actin and myosin filaments per ATP hydrolyzed in skinned muscle fibers. Nature 35:352–354.CrossRefGoogle Scholar
  4. Holmes, K. C., Angert, I., Kull, F. J., Jahn, W., and Schroder, R. R., 2003. Electron cryo-microscopy shoes how strong binding of myosin to actin releases nucleotide. Nature 425(6956):423–427.PubMedCrossRefGoogle Scholar
  5. Ishii, Y., Yoshida, T., Funatsu, T., Wazawa, T., and Yanagida, T., 1999. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys. 247:163–173.CrossRefGoogle Scholar
  6. Kitamura, K., Tokunaga, M., Esaki, S., Iwane, A. H., and Yanagida, T., 2005. Mechanism of mucle contraction based on stochastic properties of single actomyosin motors observed in vitro. Biophysics 1:1–19.CrossRefGoogle Scholar
  7. Kitamura, K., Tokunaga, M., Iwane, A. H., and Yanagida, T., 1999. Single myosin head moves alon an actin filament with regular steps of 5.3 nanometers. Nature 397:129.PubMedCrossRefGoogle Scholar
  8. Kozuka, J., Yokota, H., Arai, Y., Ishii, Y., and Yanagida, T., 2006. Dynamic polymorphism of single actin molecules in the actin filament. Nat. Chem. Biol. 2(2):83–86.PubMedCrossRefGoogle Scholar
  9. Otterbein, L. R., Graceffa, P., and Dominguez, R., 2001. The crystal structure of uncomplexed actin in the ADP state. Science 293(5530):708–711.PubMedCrossRefGoogle Scholar
  10. Prochniewicz, E., and Yanagida, T., 1990. Inhibition of sliding movement of F-actin by crosslinking emphasizes the role of actin structure in the mechanism of motility. J. Mol. Biol. 216(3):761–772.PubMedCrossRefGoogle Scholar
  11. Wakabayashi, K., Ueno, Y., Takezawa, Y., and Sugimoto, Y., 2001. Muscle contraction mechanism: Use of X-ray synchrotron radiation. Nature Encyclopedia of life science pp. 1–11.Google Scholar
  12. Yanagida, T., Arata, T., and Oosawa, F., 1985. Sliding distance induced by a myosin crossbridge during one ATP hydrolysis cycle. Nature 316:366–369.PubMedCrossRefGoogle Scholar
  13. Yanagida, T., Esaki, S., Iwane, A. H., Inoue, Y., Ishijima, A., Kitamura, K., Tanaka, H., and Tokunaga, M., 2000. Single-motor mechanics and models of myosin motor. Phil. Trans. R. Soc. Lond. B 255:441–447.CrossRefGoogle Scholar

Copyright information

© Springer 2007

Authors and Affiliations

  • Toshio Yanagida
    • 1
  1. 1.Formation of Soft Nanomachines, Core Research for Evolution Science and Technology, Japan Science and Technology Agency, Department of Biophysical Engineering, Osaka University, Soft Biosystem Group, Laboratories for Nanobiology, Graduate School of Frontier BiosciencesOsaka UniversitySuita, OsakaJapan

Personalised recommendations