Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Calmodulin | dependent on | Mus musculus | |
calyculin A | calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N | Mus musculus |
Cloned (Comment) | Organism |
---|---|
gene Mylk3, two isoforms X1 and isoform X2, DNA and amino acid sequence determination and analysis, sequence comparions | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
T146A | a naturally occuring point mutation in strain C57BL/6N, the mutation locates in exon1 of gene Mylk3 | Mus musculus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | dependent on | Mus musculus | |
Mg2+ | required | Mus musculus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
61000 | - |
- |
Mus musculus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [myosin light chain] | Mus musculus | phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice | ADP + [myosin light chain] phosphate | - |
? | |
ATP + [myosin light chain] | Mus musculus C57BL/6N/C57BL/6J | phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice | ADP + [myosin light chain] phosphate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q3UIZ8 | two isoforms X1 and isoform X2 | - |
Mus musculus C57BL/6N/C57BL/6J | Q3UIZ8 | two isoforms X1 and isoform X2 | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cardiomyocyte | - |
Mus musculus | - |
heart | - |
Mus musculus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [myosin light chain] | phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice | Mus musculus | ADP + [myosin light chain] phosphate | - |
? | |
ATP + [myosin light chain] | MLC2 | Mus musculus | ADP + [myosin light chain] phosphate | - |
? | |
ATP + [myosin light chain] | phosphorylation levels of MLC2v in the apex of the hearts. The MLC2v phosphorylation in strain C57BL/6N is significantly lower than that in C57BL/6J mice | Mus musculus C57BL/6N/C57BL/6J | ADP + [myosin light chain] phosphate | - |
? | |
ATP + [myosin light chain] | MLC2 | Mus musculus C57BL/6N/C57BL/6J | ADP + [myosin light chain] phosphate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 61000, isozyme cMLCK-2, SDS-PAGE | Mus musculus |
Synonyms | Comment | Organism |
---|---|---|
cardiac myosin light chain kinase | - |
Mus musculus |
cMLCK | - |
Mus musculus |
Mylk3 | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
malfunction | in cultured cardiomyocytes, the knockdown of cMLCK impaired epinephrine-induced activation of sarcomere reassemble and overexpression of cMLCK promoted sarcomere organization. The lack of MLC2 phosphorylation in heart induces reduction in cardiac performance in genetically modified cMLCK knockout mice. Reduced levels of MLC2 phosphorylation induces cardiac dysfunction | Mus musculus |
physiological function | in cardiac muscle the dominant regulatory mechanism is centered on the thin-filament protein, troponin, where binding of Ca2+ to troponin C induces contraction. MLC2 phosphorylation plays modulatory roles. The spatial gradient of MLC2 phosphorylation from base to apex and from endocardium to epicardium plays a physiological role in producing cardiac torsion and maintaining normal cardiac contraction. MLC2 phosphorylation may influence actin-myosin interactions independent to the actin-bound regulatory proteins. Cardiac myosin light chain kinase (cMLCK) plays an obligatory role in maintaining the phosphorylation levels of regulatory myosin light chain (MLC2), which is thought to be crucial for regulation of cardiac function. The papillary muscle twitch tension induced by electrical field stimulation is smaller in C57BL/6N than C57BL/6J. Phenylephrine has no effect on MLC2v phosphorylation in either strains but increased the twitch tension more potently in C57BL/6J than in C57BL/6N. Calyculin A increased papillary muscle MLC2v phosphorylation to a similar extent in both strains but increased the phenylephrine-induced inotropic response only in C57BL/6N. cMLCK is an indispensable kinase for MLC2 phosphorylation in myocardium | Mus musculus |