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Cooperativity in the Ca2+ Regulation of Muscle Contraction

  • Chapter
Molecular Interactions of Actin

Part of the book series: Results and Problems in Cell Differentiation ((RESULTS,volume 36))

Abstract

We have recently reviewed the evidence that the muscle thin filament operates as a classical Monod-Wyman-Changeux (MWC, 1965) cooperative/allosteric system while interacting with myosin heads (Lehrer and Geeves 1998). We showed that much of the available biochemical in vitro data can be explained if actin is considered to be the catalyst (enzyme) which accelerates the loss of Pi from the myosin-ADP-Pi substrate. In this scheme, tropomyosin (Tm) is the regulatory component, myosin complexed with ADP is the activating ligand and troponin (Tn) in the absence or presence of Ca2+ is the allosteric inhibitor or activator, respectively. The myosin product complex “turns-on” the activity by shifting the equilibrium from the T (closed) to the R-state (open), facilitated by Tn in the presence of Ca2+. Thus, the ATPase activity of the system is mostly off in the absence of myosin heads, even in the presence of Ca2+.

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Author information

Authors and Affiliations

  1. Department of Biosciences, University of Kent, Canterbury, Kent, CT2 7NJ, UK

    Michael A. Geeves

  2. Muscle Research Group, Boston Biomedical Research Institute, Watertown, Massachusetts, 02472, USA

    Sherwin S. Lehrer

Authors
  1. Michael A. Geeves
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  2. Sherwin S. Lehrer
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Minnesota Medical School, 55455, Minneapolis, MN, USA

    David D. Thomas

  2. Department of Anatomy and Histology, Institute for Biomedical Research, University of Sydney, 2006, Sydney, Australia

    Cristobal G. Dos Remedios

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© 2002 Springer-Verlag Berlin Heidelberg

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Geeves, M.A., Lehrer, S.S. (2002). Cooperativity in the Ca2+ Regulation of Muscle Contraction. In: Thomas, D.D., Dos Remedios, C.G. (eds) Molecular Interactions of Actin. Results and Problems in Cell Differentiation, vol 36. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-540-46558-4_10

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  • DOI: https://doi.org/10.1007/978-3-540-46558-4_10

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-08641-0

  • Online ISBN: 978-3-540-46558-4

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