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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Dual specificity phosphatase 14

MKP6, DUSP14, MAP kinase phosphatase 6, MKP-L
Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP14 contains the consensus DUSP C-terminal catalytic domain but lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009] (from NCBI)
Top mentioned proteins: MAPK, JNK, ERK, fibrillin-1, HAD
Papers on MKP6
TRAF2-mediated Lys63-linked ubiquitination of DUSP14/MKP6 is essential for its phosphatase activity.
Tan et al., Taiwan. In Cell Signal, Jan 2016
Dual-specificity phosphatase 14 (DUSP14, also known as MKP6) is a MAP kinase phosphatase that dephosphorylates JNK, ERK, and p38 in vitro.
Folate receptor-targeted multimodality imaging of ovarian cancer in a novel syngeneic mouse model.
Gach et al., Pittsburgh, United States. In Mol Pharm, Mar 2015
Adult female C57BL/6 mice were injected i.p. with 6 × 10(6) MKP-L FR+ cells.
Phosphotyrosine Substrate Sequence Motifs for Dual Specificity Phosphatases.
Ulrich et al., Frederick, United States. In Plos One, 2014
We investigated the interactions of peptide substrates with select DUSPs of four types: MAP kinases (DUSP1 and DUSP7), atypical (DUSP3, DUSP14, DUSP22 and DUSP27), viral (variola VH1), and Cdc25 (A-C).
The Epigenetic Modifications of Genes Associated with Tuberculosis Susceptibility and Implications for Epi-Drugs.
Xie et al., Beibei, China. In Crit Rev Eukaryot Gene Expr, 2014
Many genes involved in tuberculosis susceptibility (e.g., NRAMP1 (SLC11A1), IFNG, NOS2A, VDR, ISG15, TACO, TLR1, TLR, IL18R1, chemokines, PADI, DUSP14, MBL, and MASP-2) have been subjected to epigenetic modification.
Dual-specificity phosphatase 14 (DUSP14/MKP6) negatively regulates TCR signaling by inhibiting TAB1 activation.
Tan et al., Taiwan. In J Immunol, 2014
Dual-specificity phosphatase 14 (DUSP14; also known as MKP6) is classified as a MAPK phosphatase.
Arsenite suppression of BMP signaling in human keratinocytes.
Rice et al., Davis, United States. In Toxicol Appl Pharmacol, 2013
Knockdown of DUSP2 or DUSP14 using shRNAs greatly reduced FOXN1 and keratins 1 and 10 mRNA levels and their induction by BMP.
Association between functional polymorphisms in genes involved in the MAPK signaling pathways and cutaneous melanoma risk.
Wei et al., Houston, United States. In Carcinogenesis, 2013
The risk associations with 16 SNPs around DUSP14 (rs1051849) and a previous reported melanoma locus MAFF/PLA2G6 (proxy SNP rs4608623) were replicated in the GenoMEL dataset (P < 0.01) but failed in the Australian dataset.
The dual-specificity phosphatase DUSP14 negatively regulates tumor necrosis factor- and interleukin-1-induced nuclear factor-κB activation by dephosphorylating the protein kinase TAK1.
Shu et al., Wuhan, China. In J Biol Chem, 2013
In this study, we identified a member of the dual-specificity phosphatase family, DUSP14, as a negative regulator of TNF- and IL-1-triggered NF-κB activation by expression screens.
Deciphering the genetic architecture of variation in the immune response to Mycobacterium tuberculosis infection.
Gilad et al., Chicago, United States. In Proc Natl Acad Sci U S A, 2012
DUSP14 may be a susceptibility gene for pulmonary tuberculosis.
Prenatally diagnosed 17q12 microdeletion syndrome with a novel association with congenital diaphragmatic hernia.
Rajkovic et al., Pittsburgh, United States. In Fetal Diagn Ther, 2011
The deletion caused haploinsufficiency for 17 genes, including AATF, ACACA, DDX52, DUSP14, GGNBP2, HNF-1B, LHX1, PIGW, SYNRG, TADA2A, and ZNHIT3.
Chronic stress and impaired glutamate function elicit a depressive-like phenotype and common changes in gene expression in the mouse frontal cortex.
Del Rio et al., Pamplona, Spain. In Eur Neuropsychopharmacol, 2011
Moreover, genes that inhibit the MAPK pathways (Dusp14), stimulate oxidative metabolism (Eif4a2) and enhance glutamate transmission (Rab8b) were upregulated.
PTP inhibitor IV protects JNK kinase activity by inhibiting dual-specificity phosphatase 14 (DUSP14).
Cho et al., Taejŏn, South Korea. In Biochem Biophys Res Commun, 2009
PTP inhibitor IV inhibited DUSP14 phosphatase activity.
Overproduction, purification and structure determination of human dual-specificity phosphatase 14.
Waugh et al., Frederick, United States. In Acta Crystallogr D Biol Crystallogr, 2009
The overproduction, purification and crystal structure at 1.88 A resolution of human dual-specificity phosphatase 14, DUSP14 (MKP6), are reported.
Characteristics of dual specificity phosphatases mRNA regulation by 3,4-methylenedioxymethamphetamine acute treatment in mice striatum.
Noble et al., Paris, France. In Brain Res, 2008
We found that the increase in Dusp14 mRNA depends on the activation of ERK and lasts longer than those of Dusp1 and Dusp5.
Increasing GLP-1-induced beta-cell proliferation by silencing the negative regulators of signaling cAMP response element modulator-alpha and DUSP14.
Thorens et al., Lausanne, Switzerland. In Diabetes, 2008
knockdown of CREMalpha or DUSP14 or expression of a dominant-negative form of DUSP14 increased beta-cell line proliferation and enhanced the GLP-1-induced proliferation of primary beta-cells
Mycobacterial lipomannan induces MAP kinase phosphatase-1 expression in macrophages.
Guérardel et al., Villeneuve-d'Ascq, France. In Febs Lett, 2008
The binding of Lipomannan to TLR2 triggers MAPK activation, followed by an up-regulation of MKP-1 expression, which in turn may act as a negative regulator of MAPK activation.
JNK1 Is required for the induction of Mkp1 expression in macrophages during proliferation and lipopolysaccharide-dependent activation.
Celada et al., Barcelona, Spain. In J Biol Chem, 2007
critical role for JNK1 in the regulation of Mkp1 induction and in LPS-dependent macrophage activation.
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