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Rabbit Anti-phospho-MRCL3 (Thr18 + Ser19) antibody
Myosin is a highly conserved, ubiquitously expressed protein that interacts with Actin to generate the force for cellular movements. Conventional myosins are hexameric proteins consisting of two heavy chain subunits, a pair of non-phosphorylatable light chain subunits and a pair of phosphorylatable light chain subunits. Three general classes of myosin have been cloned: smooth muscle myosins, striated muscle myosins and non-muscle myosins. Myosin regulatory light chains, including MRCL3 (also known as MRLC3 or MLCB), MRLC2 (also known as MLSLCB) and MYL9 (also known as LC20, MLC2, MRLC1 or MYRL2), regulate contraction in smooth muscle and non-muscle cells via phosphorylation by myosin light chain kinase (MLCK). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the Actin-activated myosin ATPase activity, thereby regulating the contractile activity. Myosin light chain is also located in striated skeletal muscle, where its function remains undefined.
Function:
Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Implicated in cytokinesis, receptor capping, and cell locomotion.
Post-translational modifications:
Phosphorylation increases the actin-activated myosin ATPase activity and thereby regulates the contractile activity. It is required to generate the driving force in the migration of the cells but not necessary for localization of myosin-2 at the leading edge.
Similarity:
Contains 3 EF-hand domains.
SWISS:
P19105
Gene ID:
10627
Database links:
Entrez Gene: 10627 Human
Entrez Gene: 67268 Mouse
SwissProt: P19105 Human
Unigene: 190086 Human
Unigene: 261329 Mouse
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