Key result
Myosin light chain kinase (MLCK) modifies actin-myosin interaction through multifunctional properties, and its phosphorylation of MLC20 is not obligatory for inducing smooth muscle contraction.
This review provides evidence that myosin light chain kinase can regulate smooth muscle contraction through mechanisms independent of its traditional kinase activity.
Challenges canonical MLC20 phosphorylation requirement in smooth muscle contraction; leaves open MLCK non-kinase functions as potential cardiovascular therapeutic targets.
Myosin light chain kinase (MLCK) is a regulatory protein for smooth muscle contraction, which acts by phosphorylating 20-kDa myosin light chain (MLC20) to activate the myosin ATPase activity. Although this mode of action is well-established, there are numerous reports of smooth muscle contraction that is not associated with MLC20 phosphorylation. The kinase activity for the phosphorylation is localized at the central part of MLCK, which is also furnished with actin-binding activity at its N terminal and myosin-binding activity at its C terminal. This article overviews as to how such multifunctional properties of MLCK modify the actin-myosin interaction and presents our observations that the phosphorylation is not obligatory in induction of smooth muscle contraction.
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Gao et al. (2001) conducted a review in Smooth muscle contraction. Myosin light chain kinase (MLCK) was evaluated. Myosin light chain kinase (MLCK) modifies actin-myosin interaction through multifunctional properties, and its phosphorylation of MLC20 is not obligatory for inducing smooth muscle contraction.
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