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Literature summary for 2.7.11.18 extracted from
- Phosphorylation regulates interaction of 210-kDa myosin light chain kinase N-terminal domain with actin cytoskeleton (2015), Biochemistry (Moscow), 80, 1288-1297.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Calmodulin | dependent on | Gallus gallus |  |
| additional information | enzyme MLCK210 possesses actin binding regions both in the central part of the molecule and in its N-terminal tail domain | Gallus gallus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of FLAG-tagged N27-157 wild-type or phospho-mutant S140A/S149A constructs in HeLa cells | Gallus gallus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S140D/S149D | site-directed mutagenesis of MLCK, the mutation attenuates the phosphorylation at Ser140 and Ser149 by PKA and Aurora B kinases, overview | Gallus gallus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | phosphorylation at serine residues 140/149 by cAMP-dependent protein kinase (PKA) and Aurora B leads to a decrease in N27-157 binding to actin | Gallus gallus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytoskeleton | - |
Gallus gallus | 5856 | - |
| microtubule | - |
Gallus gallus | 5874 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | dependent on | Gallus gallus | |
| Mg2+ | required | Gallus gallus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 210000 | - |
high molecular weight myosin light chain kinase | Gallus gallus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [myosin light chain] | Gallus gallus | non-muscle myosin II | ADP + [myosin light chain] phosphate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Gallus gallus | P11799 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | in vitro, the N-terminal actinbinding domain of MLCK210 is located within residues 27-157 and is phosphorylated by cAMP-dependent protein kinase (PKA) and Aurora B at serine residues 140/149 leading to a decrease in N27-157 binding to actin, leading role of the S149D mutation in attenuation of N27-157 binding to the cytoskeletal structures. In vitro phosphorylation and determination of phosphorylation sites, overview | Gallus gallus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [myosin light chain] | non-muscle myosin II | Gallus gallus | ADP + [myosin light chain] phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| high molecular weight myosin light chain kinase | - |
Gallus gallus |
| MLCK | - |
Gallus gallus |
| MLCK210 | - |
Gallus gallus |
| myosin light chain kinase | - |
Gallus gallus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Gallus gallus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | mutation S140D/S149D attenuates the phosphorylation at Ser140 and Ser149 by PKA and Aurora B kinases | Gallus gallus |
| physiological function | high molecular weight myosin light chain kinase is a multifunctional protein involved in myosin II activation and integration of cytoskeletal components in cells, phosphorylation regulates interaction of 210-kDa myosin light chain kinase N-terminal domain with actin cytoskeleton. Phosphorylation at serine residues 140/149 by cAMP-dependent protein kinase (PKA) and Aurora B leads to a decrease in N27-157 binding to actin. Enzyme-cytoskeleton interactions: in non-muscle cells, MLCK210 functions as a cytoskeleton integrator and motility organizer. MLCK210 resides on microfilament bundles via its central high affinity actin binding site, whereas both the N- and C-terminal tails of the molecule are engaged in reversible interaction with other cytoskeletal and motile components of the cell. While MLCK210 resides on actin filaments, its KRPdomain binds to soluble monomeric non-muscle myosin II and facilitates the presentation of myosin II to the catalytic core of the kinase. Phosphorylation of myosin II allows selfassembly of myosin filaments, thereby supporting localized actomyosin motility, modelling | Gallus gallus |
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