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CPD — EPHB2
Text-mined interactions from Literome
Wang et al., J Cell Physiol 2000
:
Both EGF and
Cpd 5
caused an induction of
phospho-extracellular response kinase (ERK) , which was also more sustained with Cpd 5 ... Moreover, whereas
Cpd 5
induced a striking translocation of phosphorylated
ERK from cytosol to the nucleus, no significant nuclear translocation occurred after stimulation with EGF
Kar et al., J Cell Physiol 2002
:
U0126 and PD 098059, specific inhibitors of MEK1/2, the ERK1/2 kinases, antagonized both cell growth inhibition and
ERK1/2 phosphorylation
mediated by
Cpd5
Adachi et al., J Cell Physiol 2002
:
Furthermore,
Cpd 5 action
caused a strong nuclear
phospho-ERK signal and induced phospho-Elk-1, a nuclear target of ERK activation, in contrast to the weak effects of EGF ... The MEK inhibitors PD098056 and U0126 abrogated both the
induction by
Cpd 5 of
phospho-ERK , its nuclear translocation and phospho-Elk-1 and also antagonized its growth inhibitory effects
Carr et al., J Cell Physiol 2002
(Carcinoma, Hepatocellular) :
Cpd 5 could
activate ERK1/2 either by signaling from an activated EGFR, which is upstream in the signaling cascade, or by direct inhibition of ERK1/2 phosphatase ( s ) ... The growth inhibitory effect during liver regeneration and transplantable tumor growth is also correlated with
ERK1/2 phosphorylation
induced by
Cpd 5
Wang et al., J Cell Physiol 2005
:
We now report that
Cpd 5 can directly
cause ERK phosphorylation by inhibiting Cdc25A activity independently of the EGFR pathway ... In EGFR-devoid NR6 fibroblasts and MEK ( ERK kinase ) mutated MCF7 cells, Cpd 5 treatment also resulted in ERK phosphorylation, providing support for the idea that
Cpd 5 can directly
act on
ERK phosphorylation by inhibiting Cdc25A activity
Wang et al., J Cell Physiol 2006
(Carcinoma, Hepatocellular...) :
We previously showed that prolonged and strong
ERK phosphorylation
induced by
Compound 5 (Cpd 5) , a Cdc25A protein phosphatase inhibitor, was involved in its mechanism of cell growth inhibition