Human Myosin Light Chain Kinase (MYLK) Protein

Background

Myosin light chain kinase (MYLK) is a crucial enzyme responsible for phosphorylating the regulatory light chain of myosin II, a process essential for modulating smooth muscle contraction and cellular motility. MYLK functions by activating the actomyosin complex, enhancing cross-bridge cycling, and facilitating tension generation in response to calcium-calmodulin signaling. It is highly expressed in smooth muscle cells, endothelial cells, and non-muscle tissues, reflecting its versatile roles in physiological processes like vascular tone regulation, cell migration, and maintaining epithelial barrier integrity. Dysregulation of MYLK activity has been implicated in pathological conditions such as hypertension, asthma, and acute lung injury, where excessive or insufficient contractile responses can disrupt normal tissue function. The gene encoding MYLK produces several isoforms, each tailored to specific tissue types and functional demands, further underscoring its adaptability in diverse cellular environments. MYLK's role in dynamic cytoskeletal organization and mechanical force generation makes it a focus of therapeutic research, especially in the context of cardiovascular and inflammatory diseases.