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DUSP6 — EPHB2

Text-mined interactions from Literome

Zhou et al., J Biol Chem 1999 : The mitogen activated protein kinase phosphatase 3 ( MKP3 ) -catalyzed hydrolysis of aryl phosphates in the absence and presence of extracellular signal regulated kinase 2 ( ERK2 ) was investigated in order to provide insights into the molecular basis of the ERK2 induced MKP3 activation ... Increased catalytic activity and enhanced affinity for oxyanions are observed for MKP3 in the presence of ERK2 ... Remarkably, it is found that the extent of ERK2 induced MKP3 activation is substrate dependent, with smaller activation observed for bulkier substrates
Fjeld et al., J Biol Chem 2000 : In addition, ERK activated MKP3 catalyzes intermediate hydrolysis 5-6-fold more efficiently and binds ligands up to 19-fold more tightly
Reffas et al., Biochem J 2000 : Compartment-specific regulation of extracellular signal regulated kinase ( ERK ) and c-Jun N-terminal kinase (JNK) mitogen activated protein kinases ( MAPKs ) by ERK dependent and non-ERK dependent inductions of MAPK phosphatase (MKP)-3 and MKP-1 in differentiating P19 cells
Zhou et al., J Biol Chem 2001 : To determine the molecular basis of the specific ERK2 recognition by MKP3 and the ERK2 induced MKP3 activation, we have carried out a systematic mutational and deletion analysis of MKP3 ... Using activation based and competition based assays, we are able to quantitatively evaluate the contributions that residues/regions within MKP3 make to ERK2 binding and ERK2 induced MKP3 activation ... However, these two regions are not essential for ERK2 induced MKP3 activation ... Although deletion of this region or mutation of the putative ERK specific docking sequence ( 364 ) FTAP ( 367 ) in this region reduces MKP3 's affinity for ERK2 by less than 10-fold, this region is absolutely required for ERK2 induced MKP3 activation
Zhang et al., J Biol Chem 2003 (MAP Kinase Signaling System) : We show that binding and activation of MKP3 by ERK2 involve two distinct protein-protein interaction sites in ERK2 ... Thus, the common docking ( CD ) site composed of Glu-79, Tyr-126, Arg-133, Asp-160, Tyr-314, Asp-316, and Asp-319 are important for high affinity MKP3 binding but not essential for ERK2 induced MKP3 activation
Furukawa et al., Am J Pathol 2003 (Pancreatic Neoplasms) : Gain-of-function mutations of KRAS2 occur in the great majority of pancreatic cancer cells, and loss of expression of DUSP6/MKP-3 may synergistically promote constitutive activation of ERK and uncontrolled cell growth
Kim et al., Mol Cell Biol 2004 (MAP Kinase Signaling System) : However, the physiological roles of MKP-3 and the mechanism by which MKP-3 regulates Ras/Drosophila ERK ( DERK ) signaling in vivo have not been determined
Kar-Roy et al., J Biol Chem 2004 : This is the first example of a viral protein regulating ERK activation by inhibition of its cognate dual specificity phosphatase
Warmka et al., J Biol Chem 2004 (Breast Neoplasms) : These studies indicate that in initiated cells palytoxin unleashes ERK activity by down regulating MKP-3 , an ERK inhibitor , and further suggest that MKP-3 may be a vulnerable target in cells that express oncogenic Ras
Marchetti et al., Mol Cell Biol 2005 : Using a fibroblast model in which the expression of either MKP-3 or a more stable MKP-3-green fluorescent protein ( GFP ) chimera was induced by tetracycline, we found that serum induces the phosphorylation of MKP-3 and its subsequent degradation by the proteasome in a MEK1 and MEK2 (MEK1/2)-ERK1/2 dependent manner
Zou et al., Oncogene 2006 : Introduction of LIGHT into ES cells results in the dephosphorylation of MKP-3 and activation of extracellular signal regulated kinase ( ERK ) 5
Furukawa et al., Oncogene 2006 (MAP Kinase Signaling System...) : DUSP6/MKP-3 , a specific inhibitor of MAPK1/ERK2 , frequently loses its expression in primary pancreatic cancer tissues
Hu et al., Mol Cell Biol 2006 (Lung Neoplasms) : While activated ERK phosphorylates Hsf4b, DUSP26 controls the activity of ERK , leading to phosphorylation/dephosphorylation of Hsf4b, altering its ability to bind DNA
Smith et al., FEBS Lett 2006 (MAP Kinase Signaling System) : We conclude that MKP-3/Pyst1 expression is mediated by ERK activation and that negative feedback control predominates in limiting the extent of FGF induced ERK activity
Mitsushima et al., Exp Cell Res 2007 (MAP Kinase Signaling System) : Moreover, the coexpression of MKP3/rVH6 , an ERK2 specific phosphatase, suppressed the anchorage independent activation of ERK2 induced by vinexin beta
Mark et al., Protein Expr Purif 2007 (MAP Kinase Signaling System) : Furthermore, we demonstrate the use of a 96-well plate format refolding assay in which the ERK induced activity of MKP3 is simulated by 33 % DMSO
Arkell et al., Cell Signal 2008 : Recombinant ERK2 can induce catalytic activation of DUSP6 whereas ERK5 can not
Ekerot et al., Biochem J 2008 : DUSP6/MKP-3 is inducible by FGF ( fibroblast growth factor ) signalling and acts as a negative regulator of ERK activity in key and discrete signalling centres that direct outgrowth and patterning in early vertebrate embryos ... These findings identify a conserved Ets-factor dependent mechanism by which ERK signalling activates DUSP6/MKP-3 transcription to deliver ERK1/2-specific negative-feedback control of FGF signalling
Fan et al., Development 2008 : Reduced ERK1/2 phosphorylation was due , in part, to increased expression of MKP3 , an ERK1/2-specific phosphatase
Chan et al., Carcinogenesis 2008 (Disease Progression...) : Conversely, enforced expression of MKP3 in MKP3-deficient ovarian cancer cells significantly reduced ERK1/2 activity and inhibited cell proliferation, anchorage independent growth ability and tumor development in nude mice
Zeliadt et al., Toxicol Appl Pharmacol 2008 : Here we tested the roles of endogenous MKP-3 in modulating ERK1/2 under conditions of chronic stimulation of the Ras/Raf/MEK1/2/ERK1/2 pathway by expression of oncogenic Ras ... Third, we found that the regulation of ERK1/2 by MKP-3 is countered by the complex regulation of MKP-3 by ERK1/2 ... Potent ERK1/2 activators stimulated the loss of MKP-3 within 30 min due to an ERK1/2 dependent decrease in MKP-3 protein stability
Whetzel et al., Am J Physiol Cell Physiol 2009 (Diabetes Mellitus, Type 1...) : MKP-3 selectively regulates ERK1/2 activity through dephosphorylation
Tadaki et al., J Immunol 2009 (MAP Kinase Signaling System) : This synergistic effect on MUC5AC production may be due to enhanced activation of ERK through inhibition of MKP3 by poly ( I:C )
Romero-Sandoval et al., Molecular pain 2009 (Inflammation) : However, the inhibition of both MKP-1 and MKP-3 by triptolide induced an increase in p-ERK expression and in microglial migration using LPS+JWH015 treated microglia
Lønne et al., J Biol Chem 2009 (Breast Neoplasms...) : Depletion of MKP3 led to apoptosis and higher levels of ERK1/2 phosphorylation, suggesting that this may be a mechanism mediating the effect of PKCdelta down-regulation
Aragon et al., BMC developmental biology 2009 : While Ras-ERK1/2 activity is necessary for MKP3 , Krox20 and MafB induction, PI3K-Akt is not involved in that process
Zhang et al., Carcinogenesis 2010 (Carcinoma, Non-Small-Cell Lung...) : Our results indicate that DUSP6 expression is regulated by ERK signaling and that DUSP6 exerts antitumor effects via negative feedback regulation, pointing to an important feedback loop in NSCLC
Kar et al., J Leukoc Biol 2010 (Leishmaniasis, Visceral) : On the other hand, MKP3 and PP2A might play significant roles in the inhibition of iNOS expression through deactivation of ERK1/2
Nunes-Xavier et al., J Biol Chem 2010 (Breast Neoplasms) : MKP3/DUSP6 and DUSP5 MAP kinase phosphatases, two negative regulators of ERK1/2 , were specifically up-regulated in MCF-7 and SKBR3 cells in response to PMA
Wang et al., Molecular vision 2010 : DUSP5 and DUSP6 selectively control ERK pathway activity and proliferation
Zhang et al., J Biol Chem 2011 (MAP Kinase Signaling System) : Remarkably, MKP3, ERK2 , and phosphorylated p38a can form a stable ternary complex in solution, and the phosphatase activity of MKP3 toward p38a substrate is allosterically regulated by ERK2-MKP3 interaction ... This suggests that MKP3 not only controls the activities of ERK2 and p38a but also mediates cross-talk between these two MAPK pathways
Lee et al., Pathol Res Pract 2011 (Adenocarcinoma...) : These results indicate that DUSP6 acts as a negative feedback regulator of ERK in adenocarcinoma progression, but that DUSP6 does not play a role in the downregulation of ERK in squamous cell carcinoma
Lee et al., Eur J Endocrinol 2012 (Carcinoma, Papillary...) : To investigate the role of DUSP6 in the regulation of ERK1/2 ( MAPK3/1 ) -dependent transcription, 42 benign neoplasms and 167 PTCs were retrospectively analyzed by immunohistochemistry with dideoxy sequencing to detect BRAF ( V600E ) mutation
Landry et al., J Pain 2012 (Disease Models, Animal...) : We have previously shown that the cannabinoid type 2 receptor agonist JWH015 inhibits ERK activity by inducing MAPK phosphatase (MKP)-1 and MKP-3 ( the major regulators of MAPKs ) in vitro in microglial cells
Li et al., Nat Med 2012 (MAP Kinase Signaling System) : The defective ERK signaling was caused by the dual specific phosphatase 6 (DUSP6) , whose protein expression increased with age due to a decline in repression by miR-181a
Kim et al., Endocr Res 2013 (Adenocarcinoma, Papillary...) : The aims of this study were to evaluate the activation status of extracellular signal regulated kinase 1/2 ( ERK1/2 ) in human PTCs with BRAF ( V600E ) mutations compared to that of corresponding normal thyroid tissue and to determine the expressions of Raf kinase inhibitor protein (RKIP) and MAPK phosphatase 3 (MKP-3) , possible regulators of ERK1/2 activation
Muda et al., J Biol Chem 1996 : When expressed in COS-7 cells, MKP-3 blocks both the phosphorylation and enzymatic activation of ERK2 by mitogens
Camps et al., Science 1998 : MKP-3 was activated by direct binding to purified ERK2
Maloney et al., Am J Physiol 1999 : ANG II-induced activations of Fyn, Raf-1, and ERK were augmented in cells pretreated with BAPTA-AM, but ANG II-induced expression of the dual-specificity phosphatase mitogen activated protein kinase phosphatase-1 was blocked by BAPTA-AM pretreatment