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PMID:6238848
| Citation |
Perry, SV, Cole, HA, Hudlicka, O, Patchell, VB and Westwood, SA (1984) Role of myosin light chain kinase in muscle contraction. Fed. Proc. 43:3015-20 |
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| Abstract |
In resting striated muscles of the rabbit muscle in vivo, the phosphorylatable light chain is partially phosphorylated. Tetanic stimulation increased the level of phosphorylation more rapidly in fast twitch than in slow twitch muscle. In both types of muscle the rate of dephosphorylation was relatively slow. In rabbit fast twitch muscles, phosphorylation levels persisted significantly above the resting value for some time after posttetanic potentiation had disappeared. The role of myosin light chain kinase in modulating contractile response in striated muscle is uncertain. In vertebrate smooth muscle the role of myosin phosphorylation appears to be different from that in striated muscle despite the general similarity of the actomyosin system in both tissues. Although phosphorylation in vitro increases the Mg2+ -ATPase of actomyosin, a number of features imply that a somewhat complex relationship exists between the level of phosphorylation and the actin activation of the Mg2+ -ATPase in vertebrate smooth muscle. Contrary to many earlier reports, preparations of smooth muscle actomyosin can be obtained with Mg2+ -ATPase activities comparable to those of actomyosin from skeletal muscle. Preliminary evidence is presented that suggests that phosphorylation changes the Ca2+ sensitivity of the Mg2+ -ATPase of smooth muscle actomyosin. |
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| Keywords |
Actomyosin/metabolism; Adenosine Triphosphatases/metabolism; Animals; Muscle Contraction; Muscle, Smooth/enzymology; Muscles/enzymology; Myosin-Light-Chain Kinase; Myosins/metabolism; Phosphorylation; Protein Kinases/physiology |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0006936: muscle contraction |
ECO:0000314: |
P |
Figure 2 A shows the sub fragments of myosin chains that helps in movement. The recent crystal structure of myosin subfragment-1 suggests the presence of two distinct domains: a catalytic or motor domain, from which extends a long, 8.5-nm alpha-helix that is stabilized by the regulatory and essential light chains. |
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See also
References
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