Phosphorylation of Myosin Light Chains in Mouse Fast-Twitch Muscle Associated with Reduced Actomyosin Turnover Rate
- 27 August 1982
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 217 (4562) , 835-837
- https://doi.org/10.1126/science.6285472
Abstract
Phosphorylation of the 18,000-dalton L chains of the fast-twitch myosin in mouse extensor digitorum longus muscles was correlated with reduction in the rate of the actomyosin ATPase in vivo, but neither of these changes occurred in the soleus muscle. Apparently actomyosin interactions can be down-regulated by a reversible covalent modification of myosin L chains; a mechanism for thick-filament regulation occurs in vertebrate skeletal muscle; and the expression of this regulation may be limited to a specific fiber type.This publication has 17 references indexed in Scilit:
- Chemical energetics of slow- and fast-twitch muscles of the mouse.The Journal of general physiology, 1982
- Myosin Phosphorylation and the Cross-Bridge Cycle in Arterial Smooth MuscleScience, 1981
- Myosin light chain phosphorylation and phosphorylase a activity in rat extensor digitorum longus muscleBiochemical and Biophysical Research Communications, 1979
- Phosphorylation of skeletal muscle contractile proteins in vivoBiochemical and Biophysical Research Communications, 1977
- Ca-Regulation of Mammalian Smooth Muscle Actomyosin via a Kinase-Phosphatase-Dependent Phosphorylation and Dephosphorylation of the 20000-Mr Light Chain of MyosinEuropean Journal of Biochemistry, 1977
- Regulatory light chains in myosinsJournal of Molecular Biology, 1976
- The light chains of scallop myosin as regulatory subunitsJournal of Molecular Biology, 1973
- Substructure of the myosin moleculeJournal of Molecular Biology, 1971
- Regulation in molluscan musclesJournal of Molecular Biology, 1970
- Control of muscle contractionQuarterly Reviews of Biophysics, 1969