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DUSP5 — EPHB2

Text-mined interactions from Literome

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
Mandl et al., Mol Cell Biol 2005 : Moreover, we demonstrate that the expression of DUSP5 causes both nuclear translocation and sequestration of inactive ERK2
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
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
Seifert et al., Int J Oncol 2009 (Breast Neoplasms) : Silencing of Dusp5 by simultaneous exposure of TCDD and hypoxia or by RNAi led to increased phosphorylation of ERK1/2
Kucharska et al., Cell Signal 2009 (MAP Kinase Signaling System) : In addition, expression of DUSP5 causes nuclear translocation of ERK2 indicating that it may act as a nuclear anchor for the inactive kinase ... Using a combination of pharmacological inhibitors and phospho-site mutants we can find no evidence that phosphorylation of DUSP5 by ERK2 significantly affects either the half-life of the DUSP5 protein or its ability to bind to, inactivate or anchor ERK2 in the nucleus
Wang et al., Molecular vision 2010 : DUSP5 and DUSP6 selectively control ERK pathway activity and proliferation
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