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Dual specificity phosphatase 10

MKP5, DUSP10, MAP kinase phosphatase 5
Dual specificity protein phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the MAPK superfamily (MAPK/ERK, SAPK/JNK, p38), which is associated with cellular proliferation and differentiation. Different members of this family of dual specificity phosphatases show distinct substrate specificities for MAPKs, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. This gene product binds to and inactivates p38 and SAPK/JNK, but not MAPK/ERK. Its subcellular localization is unique; it is evenly distributed in both the cytoplasm and the nucleus. This gene is widely expressed in various tissues and organs, and its expression is elevated by stress stimuli. Three transcript variants encoding two different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: p38, MAPK, JNK, ERK, AP-1
Papers on MKP5
DUSP10 regulates intestinal epithelial cell growth and colorectal tumorigenesis.
Zhang et al., Singapore, Singapore. In Oncogene, Feb 2016
Dual specificity phosphatase 10 (DUSP10), also known as MAP kinase phosphatase 5 (MKP5), negatively regulates the activation of MAP kinases.
AGR2 oncoprotein inhibits p38 MAPK and p53 activation through a DUSP10-mediated regulatory pathway.
Vojtesek et al., Brno, Czech Republic. In Mol Oncol, Jan 2016
We demonstrate that AGR2, which is overexpressed in a variety of human cancers and provides a poor prognosis, up-regulates DUSP10 which subsequently inhibits p38 MAPK and prevents p53 activation by phosphorylation.
Roux-en-Y Esophagojejunostomy Ameliorates Renal Function Through Reduction of Renal Inflammatory and Fibrotic Markers in Diabetic Nephropathy.
Han et al., Shenyang, China. In Obes Surg, Nov 2015
Kidney messenger RNA (mRNA) and/or protein content/distribution of phospho-c-Jun NH2-terminal kinase (JNK), monocyte chemoattractant protein (MCP)-1, transforming growth factor (TGF)-β1, and mitogen-activated protein kinase phosphatase 5 (MKP5) were evaluated by real-time PCR and/or Western blotting/immunohistochemistry.
Regulation of Adipose Tissue Inflammation and Insulin Resistance by MAPK Phosphatase 5.
Dong et al., Singapore, Singapore. In J Biol Chem, Jul 2015
In this study, we show that mice deficient in MAPK phosphatase 5 (MKP5) develop insulin resistance spontaneously at an early stage of life and glucose intolerance at a later age.
MAPK Phosphatase 5 Expression Induced by Influenza and Other RNA Virus Infection Negatively Regulates IRF3 Activation and Type I Interferon Response.
Zhang et al., Singapore, Singapore. In Cell Rep, Apr 2015
Here, we show that virus infection induces the expression of MAPK phosphatase 5 (MKP5), a dual-specificity phosphatase (DUSP), in host cells.
Polymorphisms in the DUSP10 gene are associated with sex-specific colorectal cancer risk in a Han population.
Chen et al., Xi'an, China. In Int J Clin Exp Pathol, 2014
In this study, we investigated the role of genetic polymorphisms in the dual specificity protein phosphatase 10 (DUSP10) gene especially in sex-specific.
Retinoic acid receptor beta and angiopoietin-like protein 1 are involved in the regulation of human androgen biosynthesis.
Flück et al., Bern, Switzerland. In Sci Rep, 2014
Microarray expression profiling of normal versus starved H295R cells revealed fourteen differentially expressed genes; HSD3B2, HSD3B1, CYP21A2, RARB, ASS1, CFI, ASCL1 and ENC1 play a role in steroid and energy metabolism and ANGPTL1, PLK2, DUSP6, DUSP10 and FREM2 are involved in signal transduction.
Relevance of vitamin D receptor target genes for monitoring the vitamin D responsiveness of primary human cells.
Carlberg et al., Kuopio, Finland. In Plos One, 2014
Network and self-organizing map analysis of these datasets together with that of the other 24 parameters was followed by relevance calculations and identified changes in parathyroid hormone serum levels and the expression of the newly selected genes STS, BCL6, ITGAM, LRRC25, LPGAT1 and TREM1 as well as of the previously reported genes DUSP10 and CD14 as the most relevant parameters for describing vitamin D responsiveness in vivo.
Transcriptional (ChIP-Chip) Analysis of ELF1, ETS2, RUNX1 and STAT5 in Human Abdominal Aortic Aneurysm.
Tromp et al., United States. In Int J Mol Sci, 2014
Quantitative PCR assays confirmed a sub-set of the transcription factor binding sites including those in MTMR11, DUSP10, ITGAM, MARCH1, HDAC8, MMP14, MAGI1, THBD and SPOCK1.
An essential function for MKP5 in the formation of oxidized low density lipid-induced foam cells.
Ge et al., Shanghai, China. In Cell Signal, 2012
MKP5 deficiency significantly reduces foam cell formation.
Novel function of MKP-5/DUSP10, a phosphatase of stress-activated kinases, on ERK-dependent gene expression, and upregulation of its gene expression in colon carcinomas.
Shima et al., Japan. In Oncol Rep, 2012
MKP-5 interacts with ERK, retains it in the cytoplasm, suppresses its activation and downregulates ERK-dependent transcription.
Map kinase phosphatase 5 protects against sepsis-induced acute lung injury.
Ye et al., Chicago, United States. In Am J Physiol Lung Cell Mol Physiol, 2012
MKP5 is crucial to homeostatic regulation of MAPK activation in inflammatory responses.
Dual specificity phosphatases 10 and 16 are positive regulators of EGF-stimulated ERK activity: indirect regulation of ERK signals by JNK/p38 selective MAPK phosphatases.
McArdle et al., Bristol, United Kingdom. In Cell Signal, 2012
DUSPs 10 and 16 are positive regulators of activation, apparently acting by modulating cross-talk between the p38 and ERK pathways.
A distinct interaction mode revealed by the crystal structure of the kinase p38α with the MAPK binding domain of the phosphatase MKP5.
Wang et al., Beijing, China. In Sci Signal, 2012
A distinct interaction mode revealed by the crystal structure of the kinase p38alpha with the MAPK binding domain of the phosphatase MKP5.
Three-dimensional docking in the MAPK p38α.
Goldsmith, Dallas, United States. In Sci Signal, 2012
The structure of a MAPK with a kinase-binding domain (KBD) from a MAPK phosphatase, MKP5, reveals that the contacts with the MAPK are made with the folded three-dimensional KBD, although the KBD occupies the same binding site on the kinase as canonical linear docking motifs found in substrates and MAPK kinases.
The dual-specificity MAP kinase phosphatases: critical roles in development and cancer.
Gimond et al., Nice, France. In Am J Physiol Cell Physiol, 2010
Whereas DUSP1, DUSP2, and DUSP10 appear as crucial players in the regulation of immune responses, other members of the family, like the ERK-specific DUSP6, were shown to play a major role in development.
Dual-specificity MAP kinase phosphatases (MKPs) and cancer.
Keyse, Dundee, United Kingdom. In Cancer Metastasis Rev, 2008
The final group consists of three MKPs DUSP8/hVH-5, DUSP10/MKP-5 and DUSP16/MKP-7 all of which preferentially inactivate the stress-activated p38 and JNK MAP kinases.
Calcitriol as a chemopreventive and therapeutic agent in prostate cancer: role of anti-inflammatory activity.
Feldman et al., Stanford, United States. In J Bone Miner Res, 2007
Acting on a separate anti-inflammatory pathway, calcitriol induces the expression of mitogen-activated protein kinase phosphatase 5 (MKP5), a member of a family of phosphatases that are negative regulators of MAP kinases, causing the selective dephosphorylation and inactivation of the stress-activated protein kinase p38.
DUSP meet immunology: dual specificity MAPK phosphatases in control of the inflammatory response.
Mages et al., München, Germany. In J Immunol, 2007
Recently, a series of investigations in mice deficient in DUSP1, DUSP2, or DUSP10 revealed specificity in the regulation of the different MAPK proteins, and defined essential roles in models of local and systemic inflammation.
Regulation of innate and adaptive immune responses by MAP kinase phosphatase 5.
Dong et al., Seattle, United States. In Nature, 2004
MKP5 has a principal function in both innate and adaptive immune responses, and represents a novel target for therapeutic intervention of immune diseases
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