Gene interactions and pathways from curated databases and text-mining

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DUSP1 — EPHB2

Text-mined interactions from Literome

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
Araujo et al., J Thorac Cardiovasc Surg 2001 : We found a consistent inactivation of MEK/ERK pathway in both ventricular and atrial myocardium with an increase in MKP-1 , a negative regulator of ERK1/2
Byon et al., Mol Cell Biochem 2001 : In conclusion, induction of MKP-1 mRNA expression in Hirc B cells by insulin requires activation of both the ERK and JNK pathways, but not p38MAPK
Plows et al., Biochem J 2002 (Cell Transformation, Neoplastic...) : This is the first report on the ability of Ras, in the absence of growth factors, to transiently activate the MAPK pathway in the nucleus and show an involvement of MKP-1 in nuclear ERK2 regulation
Tong et al., Cancer Res 2002 (Li-Fraumeni Syndrome...) : These observations suggest that sustained ERK1/2 activation protects cells from Photofrin mediated phototoxicity and that the duration of ERK1/2 activation is regulated by MKP-1
Zhou et al., Chin J Cancer 2002 (Carcinoma, Hepatocellular...) : Manumycin may significantly inhibit the growth of human hepatoma cell line HepG2, which was related to its inhibition on the combination of Ras and cell membrane and increasing the expression of MKP-1 , accordingly inhibiting activation of ERK1/2 and AKT
Stawowy et al., Biochem Biophys Res Commun 2003 : Induction of MKP-1 by LPS was inhibited by the protein kinase C ( PKC ) -inhibitor calphostin C, but not by the ERK1/2-pathway inhibitor PD98059, suggesting that PKC but not ERK1/2 is required for LPS mediated MKP-1 induction in CFBs
Lin et al., J Biol Chem 2003 : Taken together, these results demonstrate that activated ERK1/2 can trigger MKP-1 degradation via the ubiquitin-proteasome pathway, thus facilitating long-term activation of ERK1/2 against cytotoxicity
Zhao et al., Biochem Pharmacol 2003 : Increased MKP-1 expression was dependent on the mitogen activated protein kinase, Erk
Castillo et al., J Nutr 2003 : The MKP-1 mutant did not affect ERK activity, indicating that MKP-1 preferentially down-regulates SAPK/JNK in C3H10T 1/2 cells
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
Wu et al., J Biol Chem 2005 (MAP Kinase Signaling System) : Blocking Dex induced MKP-1 induction using small interfering RNA increased ERK1/2 and JNK phosphorylation and decreased cell survival
Gorostizaga et al., Biochem Biophys Res Commun 2005 : The temporal profiles of MKP-1 protein levels and MAPKs phospho-dephosphorylation suggest that MKP-1 induction could contribute to ERK1/2 and JNK inactivation after HS
Gorostizaga et al., Endocr Res 2004 (Heat Stress Disorders...) : Comparison of the temporal profiles of MKP-1 protein induction and MAPKs phospho-dephosphorylation suggests that MKP-1 induction could contribute to ERK1/2 and JNK inactivation after HS
Lin et al., J Biol Chem 2006 (Cell Transformation, Neoplastic) : ERK activation by serum increased the endogenous level of ubiquitinated phospho-Ser ( 296 ) MKP-1 and the degradation of MKP-1
Kim et al., Biochem Biophys Res Commun 2005 (Neuroblastoma) : These data therefore suggest that MKP-1 , a negative regulator of ERK1/2 , plays a proapoptotic role in oxidative stress induced cell death in a neuronal cell line
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
Morisco et al., Cardiovasc Res 2007 (Insulin Resistance) : Isoproterenol stimulation failed to induce expression of MKP-1 ; moreover, insulin resistance induced by long-term beta-adrenergic stimulation inhibited insulin evoked expression of MKP-1 by impairing insulin induced phosphorylation of both ERK1/2 and JNK without affecting Akt kinase activity
Horsch et al., Mol Endocrinol 2007 : Regulation of ERK by MKP-1 provides a novel mechanism for control of osteoblast proliferation by GCs
Kinney et al., Am J Physiol Cell Physiol 2008 : Moreover, VEGF induced MKP-1 expression required JNK, whereas ERK was critical for thrombin induced MKP-1 expression
Wang et al., Cancer Res 2007 (Ovarian Neoplasms) : Here, we show that ERK2 mediated MKP-1 expression is critical for cisplatin resistance
Caunt et al., J Biol Chem 2008 (MAP Kinase Signaling System) : Overexpression of DUSP1 , -2, or -4 prevented ERK2 activation, but only DUSP2 and -4 caused ERK2-GFP nuclear accumulation or could be immunoprecipitated with ERK2
Calvisi et al., Int J Cancer 2008 (Genetic Predisposition to Disease...) : Levels of Dusp1 , a specific ERK inhibitor , increased only in BN rat lesions, leading to modest ERK activation, whereas a progressive Dusp1 decline occurred in corresponding lesions from F344 rats and was accompanied by elevated ERK activation
Marie-Claire et al., Brain Res 2008 : The increase of Dusp1 and Dusp5 mRNAs is not controlled by ERK activation while that of Dusp14 is a direct negative-feedback mechanism of MDMA induced ERK signalling
Feo et al., World J Gastroenterol 2008 (Carcinoma, Hepatocellular...) : Unrestrained extracellular signal regulated kinase ( ERK ) activity linked to proteasomal degradation of dual-specificity phosphatase 1 (DUSP1) , a specific ERK inhibitor , by the CKS1-SKP2 ubiquitin ligase complex occurs in more aggressive HCC of F344 rats and humans
Bladh et al., Biochim Biophys Acta 2009 (MAP Kinase Signaling System) : Previous reports have shown GC-mediated inhibition of ERK1/2 phosphorylation to involve GC induction of MAPK phosphatase-1 (MKP-1)
Romero-Sandoval et al., Molecular pain 2009 (Inflammation) : We found that the selective inhibition of MKP-1 by Ro-31-8220 and PSI2106, did not affect p-ERK expression in LPS+JWH015 treated microglia ... 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
Datta et al., Cell Signal 2010 : In this study we investigate the role of MAPK phosphatase-1 (MKP-1) in PTHrP regulation of ERK1/2 activity in relation to osteoblast proliferation, differentiation and bone formation
Newton et al., Biochem J 2010 (Lung Neoplasms) : Glucocorticoids inhibit IL-1beta induced GM-CSF expression at multiple levels : roles for the ERK pathway and repression by MKP-1 ... Since MKP-1 prevented GM-CSF expression by transcriptional, post-transcriptional and translational processes, we propose that glucocorticoids induce MKP-1 expression to reduce both MEK/ERK activation and GM-CSF protein synthesis
Tomasi et al., Hepatology 2010 : ERK phosphorylates DUSP1, facilitating its proteasomal degradation, whereas DUSP1 inhibits ERK activity
Buzzi et al., Biochim Biophys Acta 2010 (Adenocarcinoma...) : Moreover, ERK1/2 and p38 MAPK are involved in the phosphorylation of MKP-1 in Caco-2 cells
Valente et al., Cell Signal 2012 (Fibrosis...) : Here we show that the proinflammatory cytokine interleukin (IL)-17A induces adult mouse primary cardiac fibroblast ( CF ) proliferation and migration via IL-17 receptor A//IL-17 receptor C-dependent MKP-1 suppression, and activation of p38 MAPK and ERK1/2 ... IL-17A mediated p38 MAPK and ERK1/2 activation is inhibited by MKP-1 overexpression, but prolonged by MKP-1 knockdown ... These results indicate that IL-17A stimulates CF proliferation and migration via Akt/miR-101/MKP-1 dependent p38 MAPK and ERK1/2 activation
Zhang et al., Cardiovasc Res 2012 (Endotoxemia...) : MKP1 attenuates ERK1/2 and p38 activation, inhibits myocardial TNF-a expression, and improves cardiac function in endotoxemia
Reuter et al., PloS one 2012 (Inflammation...) : These differences in epithelial restitution were TGF-ß independent but Dex inhibited the EGF/ERK1/2/MAPK-pathway important for intestinal epithelial wound healing by induction of MKP-1 and Annexin-1 which was not affected by CpdA or ZK216348
Leyva-Illades et al., Infect Immun 2012 : DUSP1 inhibition by triptolide showed that ERK and p38 phosphorylation is regulated by DUSP1 , while JNK phosphorylation is not
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
Ayush et al., J Invest Dermatol 2013 (Dermatitis, Contact...) : These results suggest that Gln suppresses DNFB induced CD via deactivation of p38 MAPK through the early induction of MKP-1 , the negative regulator of p38, in an ERK dependent manner
Cook et al., J Biol Chem 1997 : Inhibition of LPA stimulated MEK and ERK activation with PD98059 and pertussis toxin, a selective inhibitor of Gi-protein coupled signaling pathways, reduced LPA stimulated MKP-1 expression by only 50 %, suggesting the presence of additional MEK- and ERK independent pathways for MKP-1 expression
Franklin et al., J Biol Chem 1997 : Conditional expression of MKP-1 inhibited PMA induced ERK2 , SAPK, and p38 MAPK activity ... This negative feedback regulatory mechanism is likely due to MKP-1 mediated inhibition of ERK2 , as studies utilizing the MEK1/2 inhibitor PD98059 suggest that ERK2 activation is required for PMA induced MKP-1 expression ... These findings suggest that ERK2 mediated induction of MKP-1 may play an important role in preferentially attenuating signaling through the p38 MAPK and SAPK signal transduction pathways
Bennett et al., Science 1997 : Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression
Bokemeyer et al., Hypertension 1998 : In addition, PD 098059, an antagonist of MEK ( MAP kinase/ERK kinase ), the upstream kinase of ERK, significantly reduced the PDGF induced activation of ERK and potently inhibited the expression of MKP-1 after stimulation with PDGF, thereby demonstrating the induction of MKP-1 in response to activation of the ERK signaling cascade
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