Background：

Stress-activated serine/threonine-protein kinase involved in cytokines production， endocytosis， cell migration， chromatin remodeling and transcriptional regulation. Following stress， it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14， leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence， Hyd-X-R-X2-S， where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3， share the same function and substrate specificity， but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1， KRT18， KRT20， RCSD1， RPS6KA3， TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress， leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-tran