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These results suggest that in the early response to stressful stimuli, MLK4beta-MLK3 binding is important for regulating MLK3 activity and MAPK (show MAPK1 Proteins) signalling, and after prolonged periods of stress exposure, MLK4beta and MLK3 proteins decline via CHIP-dependent degradation.
In summary, this investigation identifies an EGFR (show EGFR Proteins)-DOCK180 (show DOCK1 Proteins)-RAC1-MLK3-JNK (show MAPK8 Proteins) signaling axis that drives glioblastoma cell migration and dissemination.IMPLICATIONS: On the basis of these findings, MLK3 emerges as a potential therapeutic target for the treatment of glioblastoma
chronic hypoxia can reduce MLK3 expression in a posttranscriptional regulatory manner.
In lipotoxic hepatocytes, MLK3 activates a MAPK (show MAPK1 Proteins) signaling cascade, resulting in the activating phosphorylation of STAT1 (show STAT1 Proteins), and CXCL10 (show CXCL10 Proteins) transcriptional upregulation.
Data indicate that BTG2 (show BTG2 Proteins), MAP3K11, RPS6KA1 (show RPS6KA1 Proteins) and PRDM1 (show PRDM1 Proteins) as putative targets of microRNA miR (show MLXIP Proteins)-125b.
Increased expression of MAP3K11 is associated with esophageal cancer.
During hepatocyte lipotoxicity, activated MLK3 induces the release of CXCL10 (show CXCL10 Proteins)-bearing vesicles from hepatocytes, which are chemotactic for macrophages.
MLK3 serves as a common upstream kinase of AMPK (show PRKAA1 Proteins) and JNK (show MAPK8 Proteins) and functions as a direct upstream kinase for AMPK (show PRKAA1 Proteins) independent of LKB1 (show STK11 Proteins)
MLK3 represents a newly recognized integral component of HER2 (show ERBB2 Proteins) biology in HER2 (show ERBB2 Proteins)+ breast tumors.
MLK3 is a critical factor controlling the activity of kinase networks that control the cellular responses to different concentrations of reactive oxygen species.
MAP3K11 might function as an important tumor suppressor neutralized by oncomiR-125b in B-cell leukemia.
TRB3 (show TRIB3 Proteins)(-/-) islets show a decrease in both the amplitude and duration of cytokine-stimulated MLK3 induction and JNK (show MAPK8 Proteins) activation.
MLK3 limits RhoA (show RHOA Proteins) activation and injury-induced neointima formation by binding to and inhibiting the activation of p63Rho guanine nucleotide exchange factor (show ARHGEF12 Proteins), a RhoA (show RHOA Proteins) activator.
Genetic or pharmacologic inhibition of MLK3 blocks fMLP (show FPR1 Proteins)-mediated motility of neutrophils both in vitro and in vivo, suggesting that MLK3 may be a therapeutic target in human diseases characterized by exuberant neutrophil migration.
Data indicate URMC-099 as an orally bioavailable, potent mixed lineage kinase 3 MLK3 inhibitor.
Data from knockout mice suggest that MLK3 plays role in saturated fatty acid-induced activation of MAP kinase (show MAPK1 Proteins) signaling; MLK3 appears to be involved in pathogenesis of obesity, adipose tissue in fl ammation, insulin (show INS Proteins) resistance, and fatty liver disease.
Lysine 63-linked ubiquitination modulates mixed lineage kinase-3 interaction with JIP1 (show MAPK8IP1 Proteins) scaffold protein (show HOMER1 Proteins) in cytokine-induced pancreatic beta cell death
These results reveal a novel role for MLK3 signaling in the regulation of intestinal epithelial migration in vivo and suggest that MLK3 may be an important target for the regulation of intestinal mucosal healing.
The protein encoded by this gene is a member of the serine/threonine kinase family. This kinase contains a SH3 domain and a leucine zipper-basic motif. This kinase preferentially activates MAPK8/JNK kinase, and functions as a positive regulator of JNK signaling pathway. This kinase can directly phosphorylate, and activates IkappaB kinase alpha and beta, and is found to be involved in the transcription activity of NF-kappaB mediated by Rho family GTPases and CDC42.
SH3 domain-containing proline-rich kinase
, mixed lineage kinase 3
, protein-tyrosine kinase PTK1
, src-homology 3 domain-containing proline-rich kinase
, mitogen activated protein kinase kinase kinase 11