MK2 is a serine/threonine kinase that functions downstream of p38 stress-activated mitogen-activated protein kinase with a role in experimental colitis
Phosphorylation of inhibitory PAS domain protein (IPAS) at Ser184 by MAPK-activated protein kinase 2 (MK2 or MAPKAPK2) enhances the proapoptotic function of IPAS.
p38MAPK/MK2 phosphorylation of RIPK1 is a crucial checkpoint for cell fate in inflammation and infection that determines the outcome of bacteria-host cell interaction.
Ube2j1 is phosphorylated in response to lipopolysaccharides in macrophages and contributes to MK2-dependent TNFalpha biosynthesis by an unknown mechanism.
MAPK-activated protein kinase-2 limits endothelial inflammation via the PIAS1 S522 phosphorylation-mediated increase in PIAS1 transrepression and SUMO ligase activity.
Data show that DNA damage stimulates the formation of a cytosolic complex of ATM NEMO RIP1 and TAK1 and that TAK1 mediates the NF-kappaB and p38 mitogen-activated protein kinase (MAPK)/MAPK-activated protein 2 responses to DNA damage.
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