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Literature summary for 2.7.11.18 extracted from

  • Taniguchi, M.; Okamoto, R.; Ito, M.; Goto, I.; Fujita, S.; Konishi, K.; Mizutani, H.; Dohi, K.; Hartshorne, D.J.; Itoh, T.
    New isoform of cardiac myosin light chain kinase and the role of cardiac myosin phosphorylation in alpha1-adrenoceptor mediated inotropic response (2015), PLoS ONE, 10, e0141130.
    View publication on PubMedView publication on EuropePMC

Activating Compound

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(Commentary)

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

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

Metals/Ions Comment Organism Structure
Ca2+ dependent on Mus musculus
Mg2+ required Mus musculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
61000
-
-
Mus musculus

Natural Substrates/ Products (Substrates)

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

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

Source Tissue Comment Organism Textmining
cardiomyocyte
-
Mus musculus
-
heart
-
Mus musculus
-

Substrates and Products (Substrate)

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

Subunits Comment Organism
? x * 61000, isozyme cMLCK-2, SDS-PAGE Mus musculus

Synonyms

Synonyms Comment Organism
cardiac myosin light chain kinase
-
Mus musculus
cMLCK
-
Mus musculus
Mylk3
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus

General Information

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