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Myosin light chain kinase 2, skeletal muscle (MYLK2) is a calcium/calmodulin-dependent serine/threonine protein kinase specifically and abundantly expressed in adult skeletal muscle, particularly in fast-twitch fibers[2][3][5]. It catalyzes the phosphorylation of the regulatory light chain of sarcomeric myosin at Ser15 in response to increases in intracellular calcium, a process that modulates the rate and sensitivity of muscle contraction and contributes to the potentiation of force generation during repetitive stimulation. MYLK2 is critical for normal muscle function and adaptation, and mutations in the MYLK2 gene are linked to certain forms of familial hypertrophic and dilated cardiomyopathy[5]. As an enzyme central to contraction regulation in skeletal muscle, MYLK2 represents a potential therapeutic target for disorders of muscle contractility, although at present, no clinically approved drugs specifically target MYLK2[2][3][5].
Drugs targeting MYLK2 would inhibit calcium/calmodulin-dependent phosphorylation of myosin regulatory light chain, thereby altering muscle contractility
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