Regulation and Kinetics of the Actin-Myosin-ATP Interaction

Regulation and Kinetics of the Actin-Myosin-ATP Interaction ••.....•...•.••••..•.•••..•.••.•....••.•...•••..•.••....•••••.•.••..•...••.•..••..•..••.•..•.•••••..•••••.•.•••.• r;o�:�'Jj:;':f'R�;���i��··:::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::: PERSPECTIVES AND SUMMARY The two major proteins involved in muscle contraction are actin and myosin. In skeletal, cardiac, and smooth muscle these two proteins are formed into two types of filaments. Muscle contraction consists of the cyclic attachment and detachment of the globular portion of the myosin molecule to the actin filament, which results in the sliding of the filaments past each other. The energy for the actin-myosin interaction is supplied by ATP. The actin-activated ATPase activity of myosin is the in vitro correlate of muscle contraction. Therefore the regulation and kinetics of the actin­ myosin-ATP interaction has been studied by analyzing the actin-activated ATPase activity of myosin. Resting muscle has a free CaH concentration of about 10"-7 M. A rise in Ca2+ to 10-5 M initiates contraction. The manner in which Ca2+ acts to regulate the actin-myosin interaction varies for different types of muscle. Three major types of regulation have been described to date. First, in vertebrate skeletal and cardiac muscle the interaction of actin with myosin is inhibited at low CaH concentrations (10"-7 M) by a complex of proteins, troponin-tropomyosin. This inhibition of the actin-activated ATPase activ­ ity is relieved by the binding of http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biochemistry Annual Reviews

Regulation and Kinetics of the Actin-Myosin-ATP Interaction

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Publisher
Annual Reviews
Copyright
Copyright 1980 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0066-4154
eISSN
1545-4509
DOI
10.1146/annurev.bi.49.070180.004421
pmid
6447472
Publisher site
See Article on Publisher Site

Abstract

••.....•...•.••••..•.•••..•.••.•....••.•...•••..•.••....•••••.•.••..•...••.•..••..•..••.•..•.•••••..•••••.•.•••.• r;o�:�'Jj:;':f'R�;���i��··:::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::::: PERSPECTIVES AND SUMMARY The two major proteins involved in muscle contraction are actin and myosin. In skeletal, cardiac, and smooth muscle these two proteins are formed into two types of filaments. Muscle contraction consists of the cyclic attachment and detachment of the globular portion of the myosin molecule to the actin filament, which results in the sliding of the filaments past each other. The energy for the actin-myosin interaction is supplied by ATP. The actin-activated ATPase activity of myosin is the in vitro correlate of muscle contraction. Therefore the regulation and kinetics of the actin­ myosin-ATP interaction has been studied by analyzing the actin-activated ATPase activity of myosin. Resting muscle has a free CaH concentration of about 10"-7 M. A rise in Ca2+ to 10-5 M initiates contraction. The manner in which Ca2+ acts to regulate the actin-myosin interaction varies for different types of muscle. Three major types of regulation have been described to date. First, in vertebrate skeletal and cardiac muscle the interaction of actin with myosin is inhibited at low CaH concentrations (10"-7 M) by a complex of proteins, troponin-tropomyosin. This inhibition of the actin-activated ATPase activ­ ity is relieved by the binding of

Journal

Annual Review of BiochemistryAnnual Reviews

Published: Jul 1, 1980

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