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EPHB2 — GRB2
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Blaukat et al., J Biol Chem 1999
:
Expression of a
Grb2 mutant with a deletion of the amino-terminal Src homology 3 domain or the carboxyl-terminal tail of Sos strongly
reduced Pyk2 induced
ERK activation, with no apparent effect on JNK activity ...
Grb2 with a deleted carboxyl-terminal Src homology 3 domain partially
blocked Pyk2 induced
ERK and JNK pathways, whereas expression of dominant interfering mutants of p130Cas or Crk specifically inhibited JNK but not ERK activation by Pyk2
Hashimoto et al., J Biol Chem 1999
:
These findings strongly support distinct
roles for
Grb2 and Shc in controlling
ERK and JNK activation after EGF stimulation
Caverzasio et al., J Bone Miner Res 2000
:
In contrast to their implication in epidermal growth factor (EGF) receptor tyrosine kinase signaling, the adaptor protein Shc, the
Grb2/Sos complex, and the small G protein Ras were not
involved in the activation of
Erk induced by either LPA or PGF2alpha in MC3T3-E1 cells, suggesting that activation of Erk by Gi and Gq protein coupled receptors is Ras independent in these cells
Frantsve et al., Mol Cell Biol 2001
(Cell Transformation, Neoplastic) :
TEL-JAK2, in addition to activating Stat5, associates with Shc and
Grb2 and
induces activation of
Erk2 , and expression of Socs-1 inhibits engagement of each of these signaling molecules
Cailliau et al., Biochim Biophys Acta 2001
:
Early phosphorylation of
ERK2 was
blocked by the dominant negative form of
growth factor bound protein 2 (Grb2) and Ras, for FGF1-FGFR4 and FGF2-FGFR4
Shen et al., FEBS Lett 2001
:
Biochemical analyses correlated
Erk activation by
Grb2-FAT with its stimulation of cell cycle progression
Nakamura et al., Oncogene 2002
(MAP Kinase Signaling System) :
Here we determined the efficacy of Shc and N-Shc toward Erk activation in NGF treated PC12 cells, and found that N-Shc transduced
Grb2/Sos/Ras dependent
Erk activation less efficiently than Shc
Leshem et al., Exp Cell Res 2002
(MAP Kinase Signaling System) :
Whereas enhanced
Grb2 binding
increased the phosphorylation of the mitogen activated protein kinase/extracellular signal regulated protein kinases (
MAPK/ERK ) and abrogated that of p38 MAPK, PI3K had the opposite effect
Correa-Meyer et al., Am J Physiol Lung Cell Mol Physiol 2002
(MAP Kinase Signaling System) :
The inhibition of
Grb2-SOS interaction with an SH3 binding sequence peptide, Ras with a farnesyl transferase inhibitor, and Raf-1 with forskolin did not
affect the stretch induced
ERK1/2 phosphorylation
He et al., J Virol 2002
:
NS5A containing mutations within the C-terminal proline-rich motif neither bound
Grb2 nor
inhibited ERK1/2 activation by EGF, demonstrating that NS5A-Grb2 binding and downstream effects were due to direct interactions
Faisal et al., J Biol Chem 2004
:
In this present study using the small interfering RNA technique, we have found that ShcA adapter proteins play a rather active role in CSR induced Erk activation, contrary to their mostly redundant role in other signaling pathways, e.g. growth factor induced Erk activation, where
Grb2 can bind directly to the receptor tyrosine kinase and
activate Erk in the absence of ShcA
Simoncic et al., Mol Cell Biol 2006
:
Tcptp-/- macrophages also have increased tyrosine phosphorylation and recruitment of a
Grb2/Gab2/Shp2 complex to the CSF-1R and enhanced
activation of
Erk after CSF-1 stimulation, which are important molecular events in CSF-1 induced differentiation
Shinoda et al., J Neurosci 2007
:
These results suggest that DISC1 is
required for NT-3 induced axon elongation and
ERK activation at the distal part of axons by recruiting
Grb2 to axonal tips
Kraut-Cohen et al., J Biol Chem 2008
(Breast Neoplasms...) :
PTPepsilon binds and dephosphorylates Shc in vivo, reducing the association of Shc with
Grb2 and
inhibiting downstream
ERK activation
Warnecke et al., EMBO Rep 2012
:
We found that T-cell antigen receptor ( TCR ) -mediated
Erk activation
requires RasGRP1, but not
Grb2/Sos
Samoylenko et al., Carcinogenesis 2012
(Adenocarcinoma...) :
Thereby, Ruk ( l )
/CIN85 led to a more rapid and prolonged epidermal growth factor dependent activation of Src, Akt and
ERK1/2 and treatment with the Src inhibitor PP2 and the PI3K inhibitor LY294002 abolished the Ruk ( l ) /CIN85 dependent changes in cell motility
Tanaka et al., Mol Cell Biol 1995
:
These results suggest that both Crk and
Grb2 may
contribute to the activation of
Erk by oncogenic Abl, whereas Nck is unlikely to participate in this pathway ... In contrast to results with Abl,
Erk activation by EGF was strongly
inhibited only by
Grb2 mutants ; Crk and Nck mutants had little or no effect
Schlaepfer et al., J Biol Chem 1997
:
Expression of the
Grb2 binding site Phe-925 mutant of FAK
enhanced activation of
ERK2 , whereas a kinase-inactive Arg-454 mutant FAK did not
Chen et al., Mol Cell Biol 1998
:
The arsenite induced tyrosine phosphorylation of Shc, enhancement of Shc and
Grb2 interactions, and
activation of
ERK were all drastically reduced by treatment of cells with either the general growth factor receptor poison suramin or the EGFR-selective inhibitor tyrphostin AG1478
Hashimoto et al., J Exp Med 1998
:
Here we demonstrate that the BCR induced
ERK activation is
reduced by loss of
Grb2 or expression of a dominant negative form of Ras, RasN17, whereas this response is not affected by loss of Shc
Sieg et al., EMBO J 1998
:
Increased Pyk2 tyrosine phosphorylation paralleled the time-course of
Grb2 binding to Shc and
activation of
ERK2 in FAK- cells
Gupta et al., Oncogene 1998
:
We also show that dominant negative mutants of
Grb2 and Nck can
inhibit eFGF induced
Erk1 activation in Xenopus animal caps, and that targeting the first two SH3 domains of Nck to the membrane can activate Erk1 in the absence of eFGF ... Furthermore, combinations of the dominant negative Grb2 mutants with the inhibitory Nck mutant synergistically inhibited Erk1 activation by eFGF in Xenopus animal caps, suggesting that the dominant negative Nck and
Grb2 mutants
inhibit Erk1 activation by binding to different proteins ... By contrast only
Grb2 mutants could
inhibit eFGF induced
Erk1 activation in human 293 cells, demonstrating diversity in the specific mechanisms of signaling from FGF to MAP kinases in different cells