MYLK Antibodies

Target Information

MYLK (MLCK) is a serine/threonine kinase that phosphorylates myosin regulatory light chains to assist in the production of contractile activity (myosin-actin interaction). MLCK is responsible for smooth muscle contraction via phosphorylation of a specific serine in the N-terminus of myosin light chains (MLC), an event that facilitates myosin interaction with actin filaments. It is a central determinant in the development of vascular permeability and tissue edema formation. In the nervous system it has been shown to control the growth initiation of astrocytic processes in culture and to participate in transmitter release at synapses formed between cultured sympathetic ganglion cells. MLCK acts as a critical participant in signaling sequences that result in fibroblast apoptosis. Smooth muscle and non-muscle isozymes are expressed in a wide variety of adult and fetal tissues and in cultured endothelium with qualitative expression appearing to be neither tissue- nor development-specific. Non-muscle isoform 2 is the dominant splice variant expressed in various tissues. The Telokin isoform, which binds calmodulin, has been found in a wide variety of adult and fetal tissues. MLCK is probably down-regulated by phosphorylation. The protein contains 1 fibronectin type III domain and 9 immunoglobulin-like C2-type domains.

Synonyms

155 kda myosin light chain kinase homolog; 9530072E15Rik; A930019C19Rik; AAT7; AW489456; Kinase-related protein; KRP; MLCK; MLCK1; MLCK108; MLCK210; MSTP083; MYLK; MYLK1; myosin light chain kinase; myosin light chain kinase, smooth muscle; Myosin light chain kinase, smooth muscle, deglutamylated form; myosin, light chain kinase; myosin, light polypeptide kinase; nmMlck; smMLCK; smooth muscle myosin light chain kinase; smooth muscle myosin light chain kinase (61-kDa active fragment); telokin