MYLK: Difference between revisions

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Latest revision as of 18:18, 17 March 2025

MYLK or Myosin Light Chain Kinase is an enzyme that in humans is encoded by the MYLK gene. It plays a crucial role in muscle contraction and has been implicated in various human diseases.

Function[edit]

MYLK is a multi-functional kinase that phosphorylates the regulatory light chain (RLC) of myosin producing myosin activation. Myosin is a motor protein that, upon interaction with actin, utilizes ATP to generate force and motion. The activation of myosin is a key step in the process of muscle contraction, both in smooth muscle tissue and in skeletal and cardiac muscle tissue.

Structure[edit]

The MYLK gene is located on the long (q) arm of chromosome 3 at position 21.1. The encoded protein has a mass of approximately 211 kDa and is composed of 1,932 amino acids. The protein contains a kinase domain at its N-terminus, followed by a series of Ig-like C2-type domains, a fibronectin type-III domain, and a telokin domain at its C-terminus.

Clinical significance[edit]

Mutations in the MYLK gene have been associated with aortic aneurysms and dissections, as well as with asthma. In addition, MYLK has been implicated in the pathogenesis of inflammatory diseases such as sepsis and acute lung injury.

See also[edit]

References[edit]

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