MYL9
GeneName
MYL9
Summary
MYL9, also known as myosin light chain, MLC2, or LC20, is a 20 kDa protein that plays a vital role in muscle contraction and cellular motility. It is primarily expressed in muscle tissues, where it is a component of the myosin II complex and is localised in structures such as the cytoplasm, cell cortex, and myofibrils. MYL9 is involved in myofibril assembly and stress fiber assembly, and it interacts with myosin heavy chains, contributing to the structural integrity of the cytoskeleton. Additionally, it has the ability to bind calcium ions, which is essential for its function in muscle contraction and platelet aggregation.
Importance
MYL9 is relevant to: - Muscle physiology and pathology, as it is essential for muscle contraction and myofibril integrity - Platelet function and thrombus formation, due to its role in platelet aggregation - Cellular processes involving motility and shape changes, given its involvement in stress fiber assembly - Understanding diseases related to muscle dysfunction and cardiovascular conditions, where alterations in myosin light chain dynamics may play a role
Top Products
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Abcam Product Citation Summary
The MYL9 gene has been studied in the context of oesophageal squamous cell carcinoma (ESCC) using various techniques, including immunohistochemistry (IHC) and western blotting. The consistent use of the same antibody in both cell lines and tissue specimens highlights its relevance in cancer research.
Abcam Product Citation Table
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 (PubMed:11942626, PubMed:2526655). In myoblasts, may regulate PIEZO1-dependent cortical actomyosin assembly involved in myotube formation (By similarity).
Involvement in disease
Megacystis-microcolon-intestinal hypoperistalsis syndrome 4
MMIHS4
A form of megacystis-microcolon-intestinal hypoperistalsis syndrome, a congenital visceral myopathy primarily affecting females, and characterized by loss of smooth muscle contraction in the bladder and intestine. Affected individuals present at birth with functional obstruction of intestine, microcolon, dilation of bladder, and secondary hydronephrosis. The majority of cases have a fatal outcome due to malnutrition and sepsis, followed by multiorgan failure. MMIHS4 inheritance is autosomal recessive.
None
The disease may be caused by variants affecting the gene represented in this entry.
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. Phosphorylation is required for myotube formation. Phosphorylated by DAPK3; DAPK3-mediated phosphorylation is inhibited by LUZP1 (PubMed:38009294).
Tissue Specificity
Smooth muscle tissues and in some, but not all, nonmuscle cells.
Cellular localization
- Cytoplasm
- Cytoskeleton
- Cytoplasm
- Cell cortex
- Colocalizes with F-actin, MYH9 and PIEZO1 at the actomyosin cortex in myoblasts.
Alternative names
MLC2, MRLC1, MYRL2, MYL9, Myosin regulatory light polypeptide 9, 20 kDa myosin light chain, MLC-2C, Myosin RLC, Myosin regulatory light chain 9, Myosin regulatory light chain MRLC1, LC20