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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