MYL9 Regulates Muscle Contractions and Relaxation (G10398)

Target Name: MYL9

NCBI ID: G10398

MYL9

MYL9 Regulates Muscle Contractions and Relaxation

Myosin regulatory light chain 9 (MYL9) is a protein that plays a critical role in muscle contraction and relaxation. It is a member of the myosin regulatory protein family that consists of six genes, including MYL8, MYL6, MYL7, MYL5, MYL4, and MYL3. These genes encode for light chain proteins that interact with the myosin heads, which are the structural units of muscle myosin.

MYL9 is a 21-kDa protein that is expressed in a variety of tissues, including muscle, heart, and brain. It is primarily localized to the sarcolemma, which is the outermost layer of muscle cells. MYL9 is involved in the regulation of muscle contractions and in the regulation of muscle relaxation.

Drugs that target MYL9 have the potential to be useful in treating a variety of muscle-related conditions, including myopathies, myopathic neuromuscular disorders, and muscle-related pain.MYL9 has also been identified as a potential biomarker for certain muscle-related conditions.

MYL9 functions as a negative regulator of myosin phosphorylase (MPC), which is an enzyme that regulates the activity of myosin. MPC is activated by the addition of ATP to the alpha-tubulin filaments, which results in the recruitment of myosin and the subsequent generation of the myosin heads. The addition of ATP to the alpha-tubulin filaments also triggers a cascade of events that results in the release of calcium ions from the sarcolemma, which can cause muscle contraction.

MYL9 functions as a negative regulator of myosin phosphorylase by binding to the alpha-tubulin protein and preventing its phosphorylation. This interaction between MYL9 and alpha-tubulin has important implications for the regulation of muscle contractions. If MYL9 is inhibited, muscle contractions will be less forceful and more frequent.

MYL9 is also involved in the regulation of muscle relaxation. This is accomplished through its interaction with the protein called myosin light chain protein 2 (MLC2). MLC2 is a protein that is expressed in the sarcolemma and is involved in the regulation of muscle relaxation.

MYL9 functions as a positive regulator of MLC2 by binding to its alpha-tubulin substrate and promoting its phosphorylation. This interaction between MYL9 and MLC2 has important implications for the regulation of muscle relaxation. If MYL9 is activated, muscle relaxation will be more rapid and more complete.

MYL9 is also involved in the regulation of muscle cell survival. This is accomplished through its interaction with the protein called p160GTP. p160GTP is a protein that is expressed in various tissues and is involved in the regulation of cell survival.

MYL9 functions as a negative regulator of p160GTP by binding to its alpha-tubulin substrate and preventing its phosphorylation. This interaction between MYL9 and p160GTP has important implications for the regulation of muscle cell survival. If MYL9 is inhibited, muscle cells will have a reduced chance of surviving and will be more likely to undergo apoptosis.

MYL9 is also involved in the regulation of muscle protein synthesis. This is accomplished through its interaction with the protein called myosin regulatory protein 2 (MRP2). MRP2 is a protein that is expressed in various tissues and is involved in the regulation of muscle protein synthesis.

MYL9 functions as a positive regulator of MRP2 by binding to its alpha-tubulin substrate and promoting its phosphorylation. This interaction between MYL9 and MRP2 has important implications for the regulation of muscle protein synthesis. If MYL9 is activated, muscle protein synthesis will be increased, which can lead to the growth of muscle cells.

MYL9 is also involved in the regulation of muscle function. This is accomplished through its interaction with the

Protein Name: Myosin Light Chain 9

Functions: 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)

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•   general information;
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•   the target screening and validation;
•   expression level;
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•   advantages and risks of development, etc.
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