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Myosin light chain kinases (MLCK) are Ca2+/calmodulin-regulated enzymes that catalyze the phosphorylation of the 20-kDa regulatory light chains of myosin. In smooth muscle, phosphorylation of the myosin regulatory light chain is an obligatory step involved in the initiation of contraction (17).
Abstract. Phosphorylation of the regulatory light chain of myosin by the Ca2+/calmodulin-dependent myosin light chain kinase plays an important role in smooth muscle contraction, nonmuscle cell shape changes, platelet contraction, secretion, and other cellular processes.
Abstract. Myosin light chain kinase (MLCK) plays a central role in regulating the actin-myosin interaction of smooth muscle. MLCK phosphorylates the light chain of myosin in the presence of Ca2+ and calmodulin (CaM) thereby activating myosin so that it can interact with actin.
Myosin regulatory light chains (RLCs) play a primary role in striated muscle contraction by regulating the movement of myosin head molecules for cross-bridge formation. The phosphorylation of RLC residues promotes the movement of myosin heads towards the actin filaments.
Abstract. Smooth muscle myosin light chain kinase (MLCK) plays a crucial role in artery contraction, which regulates blood pressure and blood flow distribution.
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Myosin light chains are required for the structural integrity of the myosin holoenzyme. In addition, they can have regulatory functions on the mechanoenzymatic activity of the protein complex.
(A) Active MLCP dephosphorylates the light chain of myosin (MLC20) at the Ser19 residue and induces smooth muscle relaxation. (B) Signaling pathway mediated by RhoA kinase (ROCK). Several agonists activate the RhoAROCK pathway. RhoA activation is dependent on GTP and can induce ROCK activity.
Myosin light chain phosphatase (MLCP) is responsible for the dephosphorylation of the regulatory light chain (RLC) of the motor protein myosin-II, and so negatively regulates actomyosin-based contractility.

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