Phosphorylation of myosin light chains in mouse fast-twitch muscle associated with reduced actomyosin turnover rate

M. T. Crow, M. J. Kushmerick

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)835-837
Number of pages3
JournalScience
Volume217
Issue number4562
StatePublished - 1982
Externally publishedYes

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Actomyosin
Myosin Light Chains
Myosins
Skeletal Muscle
Phosphorylation
Muscles
Vertebrates
Light

ASJC Scopus subject areas

  • General

Cite this

Phosphorylation of myosin light chains in mouse fast-twitch muscle associated with reduced actomyosin turnover rate. / Crow, M. T.; Kushmerick, M. J.

In: Science, Vol. 217, No. 4562, 1982, p. 835-837.

Research output: Contribution to journalArticle

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