Reports

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

+ See all authors and affiliations

Science  27 Aug 1982:
Vol. 217, Issue 4562, pp. 835-837
DOI: 10.1126/science.6285472

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.

Related Content