MYL9
MYL9 (myosin light chain 9, also known as MYRL2, MLC2, LC20 and MRLC1) is a myosin regulatory subunit that controls smooth muscle and nonmuscle cell contractile activity through its phosphorylation. It is a member of the class 2 myosin light chains. Browse Assay Genie's current range of MYL9 research reagents below, or read on for the biology behind the target.
MYL9 is a regulatory light chain of myosin. Myosin is a structural component of muscle and consists of two heavy chains and four light chains. The MYL9 protein plays an important role in regulating the contractile activity of both smooth muscle and nonmuscle cells, and it does so through its phosphorylation. It may regulate muscle contraction by modulating the ATPase activity of myosin heads. The encoded protein binds calcium and is activated by myosin light chain kinase.
Beyond contraction, MYL9 is implicated in cytokinesis, receptor capping and cell locomotion. In myoblasts it may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation. This fits its reported localisation to the cytoskeleton and the cell cortex within the cytoplasm. The human MYL9 gene has two reported transcript variants that encode different isoforms, and mouse and rat each have a Myl9 ortholog.
The gene was previously named myosin, light polypeptide 9, regulatory, and myosin, light chain 9, regulatory. It appears in the literature under several aliases, including MYRL2, MLC2, LC20 and MRLC1. HGNC places it in the myosin light chains, class 2 group, alongside related light chain genes such as MYL1, MYL2, MYL3 and MYL6B. Researchers studying the MYL9 gene or protein often work on smooth muscle biology, nonmuscle motility and phosphorylation-dependent control of actomyosin.
MYL9 regulates smooth muscle contractile activity through phosphorylation, making it a central readout in studies of myosin regulation.
The protein regulates contractile activity in nonmuscle cells and is implicated in cytokinesis and receptor capping.
MYL9 is implicated in cell locomotion, so it is relevant to work on actomyosin-driven movement.
In myoblasts, MYL9 may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation.
MYL9 is a myosin regulatory subunit that regulates smooth muscle and nonmuscle cell contractile activity via its phosphorylation. It is implicated in cytokinesis, receptor capping and cell locomotion, and it may modulate the ATPase activity of myosin heads. It binds calcium and is activated by myosin light chain kinase.
MYL9 is also known as MYRL2, MLC2, LC20 and MRLC1, and UniProt names it myosin regulatory light polypeptide 9. Earlier names were myosin, light polypeptide 9, regulatory, and myosin, light chain 9, regulatory. Two transcript variants encoding different isoforms have been reported.
Yes. The mouse and rat both have an ortholog named Myl9. HGNC classifies the human gene within the class 2 myosin light chains. Check the datasheet of any product for its validated reactivity.
Other myosin light chains and the myosin light chain kinase that activates MYL9, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P24844; product specifications from Assay Genie datasheets.