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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.