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The loss of MKK6 protein diminishes p38 activation, leading to further degradation of the remaining TRIM9 in glioblastoma cells. The disruption of the TRIM9s-MKK6 mutual stabilization loop ultimately leads to the inactivation of p38 signaling and promotes tumor progression.
Data suggest that mitogen-activated protein kinase kinase 6 (MAP2K6) might be an important regulator of leukemia inhibitory factor receptor (LIFR)-induced radioresistance in nasopharyngeal carcinoma cells (NPC).
USP22 could interact directly with MKK6 promoter. Down-regulation of USP22 led to the decreased MKK6 mRNA expression
Advanced glycation end products significantly activated ASK1, MKK3, and MKK6, which led to activation of p38 MAPK, resulting in upregulated fibrotic response in human coronary smooth muscle cells.
Data show that miR-625-3p induces oxaliplatin resistance by abrogating MAP2K6-p38-regulated apoptosis and cell cycle control networks.
acts as a repressor of UCP1 expression, suggesting that its inhibition promotes adipose tissue browning and increases organismal energy expenditure
MEK2 was essential for the phosphorylation of MKK3/MKK6 and p38 MAPK that directly impacted on cyclin D1 expression.
Data indicate that mitogen-activated protein kinase kinase 6 (MKK6) levels were substantially higher in monocytes than in neutrophils.
Data show significant increase in the expression of MKK6 in Esophageal, Stomach, and Colon cancers as compared to controls.
uncover a new mechanism of deactivation of MKK6-p38 and substantiate a novel regulatory role of FBXO31 in stress response
Serine phosphorylation of p66shc is carried out by active MKK6. beta-Amyloid-induced ROS production and apoptosis increased in the presence of MKK6 and p66shc, which directly associate.
The models confirmed the reaction order, revealed processivity in the phosphorylation of MEK6 by ASK1, and suggested that the order of phosphorylation is dictated by both binding and catalysis rates.
crystal structure of human non-phosphorylated MAP2K6 (npMAP2K6) complexed with an ATP analogue was determined at 2.6 A resolution and represents an auto-inhibition state of MAP2K6
Data suggest aberrant MAP2K protein (MKK3, MKK4, MKK6, and MKK7) expression indicates that altered cellular signal transduction mediated via JNK and p38 may be common in bladder cancer.
the balance between MKK6 and MKK3 mediates p38 MAPK associated resistance to cisplatin in NSCLC
activation by mechanical stretch induces HMGB1 and cytokine expression in A549 cells
Results suggest that the p38alpha, MAPK, and MKK6 play prominent roles in IL-1beta and C/EBP-beta-mediated C3 gene expression in astrocytes.
Impaired cytokine production in natural killer (NK)T cells is demonstrated from MKK3-deficient6+/- mice.
we demonstrated that MKK6 has a role for regulation of dendricity in melanocytes.
MKK6 and other MAP2Ks are a distinct class of cellular redox sensors
MAP2K6 functions in mouse testis determination, via positive effects on Sry, and a minor role for MAP2K3.
MKK3 and MKK6 differentially regulate bone loss due to estrogen withdrawal. MKK3 directly mediates osteoclastogenesis while MKK6 likely contributes to pro-inflammatory cytokine production that promotes osteoclast formation.
Activation of distinct p38MAPK isoforms is regulated by the selective and synchronized action of two kinases, MKK3 and MKK6, in response to cell stress.
MKK6 is downreglated in peripheral CD4(+)T cells
p38alpha can negatively regulate the stability of the MKK6 mRNA and thus control the steady-state concentration of one of its upstream activators
Involvement of MKK6 in apoptotic cell death in thymocytes.
MKK6 is one of three different protein kinases which activate p38 MAPK in vitro.
MKK3 and MKK6 are rapidly activated during engagement of the Type I IFN receptor and play important roles in Type I IFN signaling and the generation of IFN responses
increased activity of Sox9 accounts at least in part for the phenotype caused by constitutive activation of MKK6 in chondrocytes
These results indicate that TAK1 and MKK6 constitute the p38 signalling pathway to participate to Oc differentiation by RANKL through p65 phosphorylation and NFATc1 induction.
All these results suggest that DGK may play a role in glucose transport in the skeletal muscle cells through modulating a MKK3/6-p38 signaling pathway.
MKK6 phosphorylation regulates production of superoxide by enhancing Rac GTPase activity.
MKK6-p38 and insulin growth factor 1 (IGF1)-induced PI3K/AKT pathways converge on the chromatin of muscle genes to target distinct components of the muscle transcriptosome.
These results suggest that p38 MAPK signaling plays a critical role in the survival of osteoclasts in inflammatory diseases.
MKK6 appears mainly to facilitate p38 and MK2 colocalization in the nucleus rather than to phosphorylate p38.
This gene encodes a member of the dual specificity protein kinase family, which functions as a mitogen-activated protein (MAP) kinase kinase. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act as an integration point for multiple biochemical signals. This protein phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. As an essential component of p38 MAP kinase mediated signal transduction pathway, this gene is involved in many cellular processes such as stress induced cell cycle arrest, transcription activation and apoptosis.
MAPK/ERK kinase 6
, MAPKK 6
, MEK 6
, SAPK kinase 3
, dual specificity mitogen-activated protein kinase kinase 6
, protein kinase, mitogen-activated, kinase 6 (MAP kinase kinase 6)
, stress-activated protein kinase kinase 3
, MAP kinase kinase 6
, mitogen activated protein kinase kinase 6
, protein kinase, mitogen activated, kinase 6
, mitogen-activated protein kinase kinase 3
, mitogen-activated protein kinase kinase 6 L homeolog