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Literature summary for 2.7.12.2 extracted from
- Redox-dependent dimerization of p38alpha mitogen-activated protein kinase with mitogen-activated protein kinase kinase 3 (2017), J. Biol. Chem., 292, 16161-16173 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | B1H230 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cardiac muscle fiber | - |
Rattus norvegicus | - |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MAP2K3 | - |
Rattus norvegicus |
| MKK3 | - |
Rattus norvegicus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | kinase p38alpha MAPK is activated and forms a disulfide-bound heterodimer with MAP2K3 (MKK3) in rat cardiomyocytes and isolated hearts exposed to H2O2. The disulfide heterodimer is sensitive to reduction by mercaptoethanol and is enhanced by the thioredoxin-reductase inhibitor auranofin. The C119S mutation of p38alpha decreases whereas the C162S mutation increases the dimer formation. Disulfide heterodimer formation is abolished in H9C2 cells expressing both MKK3 and p38alpha C119S/C162S and subjected to simulated ischemia and reperfusion. The p38alphaC119S/C162S mutants do not exhibit appreciable alteration in activating dual phosphorylation | Rattus norvegicus |
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Release 2023.1 (January 2023)
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