Phosphorylation of myosin light chains in mouse fast-twitch muscle associated with reduced actomyosin turnover rate.
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.
D000205:Actomyosin / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D004734:Energy Metabolism; D007700:Kinetics; D051379:Mice; D009119:Muscle Contraction; D009130:Muscle, Smooth / Q000378:metabolism; D009132:Muscles / Q000378:metabolism*; D043263:Myosin-Light-Chain Phosphatase; D009218:Myosins / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010766:Phosphorylation
D000205:Actomyosin; D010749:Phosphoprotein Phosphatases; D043263:Myosin-Light-Chain Phosphatase; D000251:Adenosine Triphosphatases; D009218:Myosins