LC20 is the myosin light chain that may regulate muscle contraction by modulating the ATPase activity of myosin heads. LC20 protein binds calcium and is activated by myosin light chain kinase. Two transcript variants encoding different isoforms have been found for LC20 and the deduced 172-amino acid protein is highly conserved, with only 3 differences between the human and chicken proteins. Light chain phosphorylation causes the folded monomeric form of myosin to extend and assemble into filaments. This observation established the involvement of the LC20 in conformational transitions of smooth muscle myosin.
The Journal of biological chemistry, 261(17), 7778-7783 (1986-06-15)
Phosphorylation of the 20,000-Da light chains, LC20, of vertebrate smooth muscle myosins is thought to be the primary mechanism for regulating the actin-activated ATPase activities of these myosins and consequently smooth muscle contraction. While actin stimulates the MgATPase activities of
The Journal of biological chemistry, 263(31), 16485-16492 (1988-11-05)
Light chain phosphorylation causes the folded monomeric form of myosin to extend and assemble into filaments. This observation established the involvement of the 20-kDa regulatory light chain (LC20) in conformational transitions of smooth muscle myosin. To further assess the role
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