Summary
Myosin light chain kinase (MLCK), a key regulator of smooth muscle contraction, has a property to bind to actin filaments that is obviously unrelated to the kinase activity innate in MLCK. We have found that this property exerts an inhibitory effect on the ATP-dependent interaction between actin and myosin. The N-terminal, actin-binding fragment was responsible for the inhibition. Calmodulin in the presence of Ca2+ (Ca2+/CaM) efficiently relieved the inhibition imposed by MLCK. The inhibitory effect was potent enough to explain physiological involvement in terms of the amount of MLCK that was present as a cytoskeletal protein in smooth muscle.
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© 1995 Springer-Verlag Tokyo
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Ye, LH., Hayakawa, K., Okagaki, T., Kohama, K. (1995). Actin-Binding Property of Myosin Light Chain Kinase and Its Role in Regulating Actin-Myosin Interaction of Smooth Muscle. In: Nakano, T., Hartshorne, D.J. (eds) Regulation of the Contractile Cycle in Smooth Muscle. Springer, Tokyo. https://doi.org/10.1007/978-4-431-65880-1_10
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DOI: https://doi.org/10.1007/978-4-431-65880-1_10
Publisher Name: Springer, Tokyo
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