This gene encodes a conventional non-muscle myosin; this protein should not be confused with the unconventional myosin-9a or 9b (MYO9A or MYO9B). The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness.
Myosin, a structural component of muscle, consists of two heavy chains and four light chains. The protein encoded by this gene is a myosin light chain that 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. Two transcript variants encoding different isoforms have been found for this gene.
Myosin 1C (MYO1C) is a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus. The nuclear isoform associates with RNA polymerase I and II and functions in transcription initiation. The mouse ortholog of this protein also functions in intracellular vesicle transport to the plasma membrane. The related gene myosin 1E has been referred to as myosin 1C in the literature, but it is a distinct locus on chromosome 19.
This gene encodesThe regulatory light chain associated with cardiac myosin beta (or slow) heavy chain. Ca+ triggersThe phosphorylation of regulatory light chain that in turn triggers contraction. Mutations in this gene are associated with mid-left ventricular chamber type hypertrophic cardiomyopathy.
MYL3, also named as MLC1v, is an essential light chain of myosin that is associated with muscle contraction. It is expressed in ventricular and slow skeletal muscle. MYL3 may serve as a target for caspase-3 in dying cardiomyocytes. Mutations of MYL3 gene cause hypertrophic cardiomyopathy. MYL3 has been identified as potential serum biomarker for drug induced myotoxicity. Great increase in MYL3 serum concentration has been observed in rats with cardiac and skeletal muscle injury.
Myosin phosphatase target subunit 1, which is also called the myosin-binding subunit of myosin phosphatase, is one of the subunits of myosin phosphatase. Myosin phosphatase regulates the interaction of actin and myosin downstream of the guanosine triphosphatase Rho. The small guanosine triphosphatase Rho is implicated in myosin light chain (MLC) phosphorylation, which results in contraction of smooth muscle and interaction of actin and myosin in nonmuscle cells. The guanosine triphosphate (GTP)-bound, active form of RhoA (GTP.RhoA) specifically interacted with the myosin-binding subunit (MBS) of myosin phosphatase, which regulates the extent of phosphorylation of MLC. Rho-associated kinase (Rho-kinase), which is activated by GTP. RhoA, phosphorylated MBS and consequently inactivated myosin phosphatase.
Discovered in the 1970s, m6A is the most prevalent internal modification in polyadenylated mRNAs and long non-coding RNAs (lncRNAs) in higher eukaryotes. m6A is widely conserved among eukaryotic species that range from yeast, plants, flies to mammals, as well as among viral RNAs with a nuclear phase. The m6A-based modification is associated with a well-defined RNA motif, RRACH (R: A/G, H: A/C/U). As a representative of the epitranscriptome, m6A mRNA modifications participate in many vital activities in the cell, including stem cell self-renewal and differentiation, mRNA transcription, alternative splicing, nuclear export, translation, degradation, and microRNA processing. These processes determine the expression or inactivation of specific genes, which is vital for growth and development.(PMID: 30416848; PMID: 24662220; PMID: 30429466)
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