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Lef1 (show LEF1 Proteins) has a role in regulating Dusp6 in formation of the zebrafish posterior lateral line primordium
During fin development, dusp6, a known MAPK/ERK (show MAPK1 Proteins) regulator, is induced in the mesoderm by FGF8 (show FGF8 Proteins) signaling, through the PI3 (show PI3 Proteins)/Akt (show AKT1 Proteins) pathway.
Mkp3 encodes a feedback attenuator of the FGF pathway, the expression of which is initiated at an early stage so as to ensure correct FGF signaling levels at the time of axial patterning.
Retinoic acid-dependent control of MAP kinase phosphatase-3 is necessary for early kidney development.
DUSP6 rs2279574 SNPs was not associated with chemoradiotherapy response, whereas tumor regression, weight loss, clinical stage, and cigarette smoking were independent prognostic predictors for these Chinese patients with non-small cell lung cancer.
DNA samples from each patient were genotyped for DUSP6 and TOP2A (show TOP2A Proteins) SNPs
Suppression of the FOXA1 (show FOXA1 Proteins)/DUSP6 signaling pathway may contribute to the development of Hirschsprung disease.
These observations led us to conclude that increased TSH signaling overcomes OIS and is essential for B-RafV600E-induced papillary thyroid carcinogenesis.
Dusp6 expression was higher in progestin-sensitive atypical endometrial hyperplasia groups compared with progestin-resistant groups. After treatment, Dusp6 expression was upregulated in progestin-sensitive groups, but not in progestin-resistant groups.
Our results suggest that DUSP6 gene expression in tumour samples may be a prognostic marker in NSCLC
DUSP6 downregulated the expression of matrix metallopeptidase 3 (show MMP3 Proteins).
These results therefore indicate that p53-mediated up-regulation of MKP-3 contributes to the establishment of the senescent cellular phenotype through dephosphorylating ERK1/2
Downregulation of Dusp6, Sprouty4, and Sef--negative modulators of FGF2/ERK1/2 signaling--was present in eutopic endometria of adenomyosis, which may play critical roles in the development of adenomyosis.
Higher expression of DUSP6 in tumor tissue, than in peritumor tissue, is associated with the recurrence after curative resection of HCC (show FAM126A Proteins), and the relative tumor DUSP6 expression has good power to predict the recurrence of HCC (show FAM126A Proteins).
this study shows that CCL2 (show CCL2 Proteins) supports the classical activation of macrophages, with miR (show MLXIP Proteins)-9 mediated down-regulation of Dusp6 and enhanced ERK (show EPHB2 Proteins)-mediated signal transduction possibly mediating this enhanced pro-inflammatory gene expression
Mitogen-activated protein kinase phosphatase 3 upregulation requires the activation of the Erk1/2 pathway, which correlates with the shutdown of this pathway.
MKP3 could be an important factor in the regulation of brown adipocyte differentiation.
DUSP6 regulates CD4 (show CD4 Proteins)+ T-cell activation and differentiation by inhibiting the TCR-dependent ERK1/2 activation and restraining spontaneous colitis in IL-10 (show IL10 Proteins)-deficient mice.
exercised obese mice had a lower expression of MKP-3 and FoxO1 (show FOXO1 Proteins)/MKP-3 association in the liver
c-Myb (show MYB Proteins) plays an important role in H-Ras (show HRAS Proteins)-induced MKP-3 transcription
Mice lacking MKP-3 protein develop an abnormal persistent state of mechanical allodynia following plantar incision, concurrent with long-lasting spinal phosphorylation of ERK-1 (show MAPK3 Proteins)/2 and p38 (show CRK Proteins).
Depletion of DUSP6 reduced the viability of cancer cell lines and increased the cytotoxicity of EGFR (show EGFR Proteins) and other targeted inhibitors, and cytotoxic agents.
LH/hCG (show CGA Proteins) tightly up-regulates MKP-3 which in turn, dephosphorylates ERK1/2 and drives p21 expression.
dual specificity phosphatases (Dusps) 6 and 14 are up-regulated by activation of beta-catenin (show CTNNB1 Proteins) in murine liver cells
The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product inactivates ERK2, is expressed in a variety of tissues with the highest levels in heart and pancreas, and unlike most other members of this family, is localized in the cytoplasm. Two transcript variants encoding different isoforms have been found for this gene.
dual specificity phosphatase 6
, dual specificity protein phosphatase 7
, dual specificity protein phosphatase 6
, MAP kinase phosphatase X17C
, Dual specificity protein phosphatase 6
, dual specificity protein phosphatase 6-like
, MAP kinase phosphatase 3
, dual specificity protein phosphatase PYST1
, mitogen-activated protein kinase phosphatase 3
, serine/threonine specific protein phosphatase