The study suggests that actomyosin interactions in vertebrate skeletal muscle can be down-regulated by reversible covalent modification of myosin light chains, specifically in fast-twitch fibers.
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Should not change clinical practice in muscle disorders; hypothesis-generating for myosin light chain regulation in fast-twitch fibers.
Phosphorylation of the 18,000-dalton light chains of the fast-twitch myosin in mouse extensor digitorum longus muscles was correlated with reduction in the rate of the actomyosin adenosinetriphosphatase in vivo, but neither of these changes occurred in the soleus muscle. These results suggest that actomyosin interactions can be down-regulated by a reversible covalent modification of myosin light chains, that a mechanism for thick-filament regulation occurs in vertebrate skeletal muscle, and that the expression of this regulation may be limited to a specific fiber type.
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Crow et al. (1982) studied this question.
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