Abstract
The major motor protein in all hollow organs, except the heart, is smooth-muscle myosin II (SmM) and the emphasis of this chapter is on the function of SmM in differentiated smooth muscle. A sliding-filament mechanism is assumed for smooth muscle, as in striated muscle, but there are differences in smooth-muscle thick filaments with respect to assembly and stability. Various isoforms of SmM are expressed and are discussed. SmM differs from its striated muscle counterparts in the requirement for phosphorylation of the regulatory light chains to regulate motor activity. The components of myosin structure required for phosphorylation dependence are outlined. The level of SmM phosphorylation is controlled by opposing actions of the Ca2+-calmodulin-dependent myosin-light-chain kinase and myosin phosphatase. Both are subject to regulation and putative mechanisms are presented. The focus of recent research has been on regulation of myosin phosphatase and inhibition and activation are proposed. Several signaling pathways converge at the myosin phosphatase target subunit to regulate activity. Two pathways that work in opposition are inhibition via the RhoA/Rho-kinase couple and activation by cyclic nucleotides, particularly cGMP. Each is vital in smooth-muscle function and both pathways have important clinical application and are argeted bypharmacological intervention in treatment of smooth-muscle disorders.
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Cremo, C.R., Hartshorne, D.J. (2008). Smooth-Muscle Myosin II. In: Myosins. Proteins and Cell Regulation, vol 7. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6519-4_6
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DOI: https://doi.org/10.1007/978-1-4020-6519-4_6
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