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Journal of Muscle Research and Cell Motility

, Volume 28, Issue 7–8, pp 363–370 | Cite as

Folding and regulation in myosins II and V

  • James R. Sellers
  • Peter J. Knight
Review

Abstract

The enzymatic activity of many myosins is regulated by various means including calcium binding, phosphorylation or binding of receptor molecules. In this review we compare and contrast the regulation of smooth muscle myosin II and myosin Va with particular emphasis on the structural basis for the regulation. Both myosins adopt folded compact conformations in their off states, but the details of the conformations are markedly different. In the regulated smooth muscle myosin II, the key feature is an asymmetric interaction between the two heads of the molecule with contributions of specific tail–head interactions. In myosin V the key feature is an interaction between the heads and the globular tail domain.

Keywords

Myosin Regulation Calcium Phosphorylation 

Notes

Acknowledgements

This work was supported by the Wellcome Trust [076057](PJK) and by funds from intramural funds from the National Heart, Lung and Blood Institute.

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Copyright information

© Springer-Verlag 2008

Authors and Affiliations

  1. 1.Laboratory of Molecular Physiology, National Heart, Lung and Blood InstituteNational Institutes of HealthBethesdaUSA
  2. 2.Institute of Molecular and Cellular BiologyUniversity of LeedsLeedsUK
  3. 3.Astbury Centre for Structural Molecular BiologyUniversity of LeedsLeedsUK

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