Gene interactions and pathways from curated databases and text-mining

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EPHB2 — FGFR1

Text-mined interactions from Literome

Gaubert et al., J Biol Chem 2001 : The expression of a dominant negative FGFR1 did not reduce ERK-1/2 activation by the HMW FGF-2, suggesting that ERK activation does not require FGFR activity
Cailliau et al., Biochim Biophys Acta 2001 : In contrast, FGFR4 stimulation by FGF2 induced an early transient activation of ERK2 and no meiosis reinitiation
Westwood et al., Oncogene 2002 (Bone Neoplasms...) : bFGF-induces phosphorylation of FGFr 1 and activation of Ras/ERK in ESFT cells that die when exposed to bFGF
Kontaridis et al., Mol Cell Biol 2002 : We propose that SHP-2 plays a pivotal role in FGFR signaling in myoblasts via both Erk dependent and Erk independent pathways
Kovalenko et al., J Biol Chem 2003 : Furthermore, mSef inhibits ERK activation mediated by a constitutively activated FGFR1 but not by a constitutively active Ras and decreases FGF but not PDGF mediated activation of Akt
Freeman et al., Cancer Res 2003 (Disease Progression...) : Despite extensive homology and equivalent expression by both chimeric receptors in the ventral prostate gland, only FGFR1 triggers detectable nuclear translocation of Erk and progression to prostatic intraepithelial neoplasia ( PIN )
Yang et al., J Biol Chem 2004 : By inhibiting FGFR1 tyrosine phosphorylation and/or Ras downstream events, Sef inhibits FGF mediated ERK activation and cell proliferation as well as PC12 cell differentiation
Li et al., J Cell Sci 2004 : FRS2 dependent SRC activation is required for fibroblast growth factor receptor induced phosphorylation of Sprouty and suppression of ERK activity
Millette et al., Trends Cardiovasc Med 2006 : We have recently discovered that release of fibroblast growth factor 2 and the subsequent activation of fibroblast growth factor receptor 1 are required for maximal induction by PDGF of ERK and of human smooth muscle cell proliferation
Lao et al., J Biol Chem 2007 : Direct binding of PP2A to Sprouty2 and phosphorylation changes are a prerequisite for ERK inhibition downstream of fibroblast growth factor receptor stimulation
Vincent et al., Osteoarthritis Cartilage 2007 (Mechanotransduction, Cellular) : The loading response was assessed by the activation of ERK , in the presence or absence of a specific FGFR inhibitor
Mori et al., J Biol Chem 2008 : Nevertheless, R50E induced phosphorylation of FGFR1 and FRS2alpha and activation of AKT and ERK1/2
Poliakov et al., J Cell Biol 2008 (MAP Kinase Signaling System) : FGFR1 activation leads to increased phosphorylation of unstimulated EphB2 , which we show is caused by down-regulation of the leukocyte common antigen related tyrosine phosphatase receptor that dephosphorylates EphB2 ... In addition, FGFR1 signaling inhibits further phosphorylation of EphB2 upon stimulation with ephrinB1, and we show that this involves a requirement for the mitogen activated protein kinase ( MAPK ) pathway ... In addition, FGFR1 signaling inhibits further phosphorylation of EphB2 upon stimulation with ephrinB1, and we show that this involves a requirement for the mitogen activated protein kinase ( MAPK ) pathway
Shiang et al., Breast Cancer Res Treat 2010 (Breast Neoplasms) : In cells with amplified FGFR-1 , brivanib decreased receptor autophosphorylation, inhibited bFGF induced tyrosine kinase activity, and reduced phosphorylation of ERK and AKT
Zhou et al., Plasmid 2010 (MAP Kinase Signaling System) : The results demonstrate that taspine can down-regulate phosphorylation of FGFR1 and ERK , and inhibit Hek293/FGFR1 and MCF-7 cell proliferation
Soundararajan et al., J Neurosci 2010 (MAP Kinase Signaling System) : These results indicate that MAPK/ERK activation downstream of FGFR1 is necessary for MMCm motor axon guidance and that ES cell derived neurons provide an important tool for dissecting intracellular pathways required for axon guidance
Zou et al., J Biol Chem 2012 : Whereas FGF ligand induced phosphorylation of FGFR1 preferentially activates ERK , FN-induced phosphorylation of FGFR1 preferentially activates AKT, indicating differential downstream signaling of FGFR1 in response to alternate stimuli
Ono et al., Hum Mol Genet 2013 : The Ras-GTPase activity of neurofibromin restrains ERK dependent FGFR signaling during endochondral bone formation ... We provide here evidence that neurofibromin, via its Ras guanosine triphosphatase -activating activity, controls ERK1/2 dependent fibroblast growth factor receptor ( FGFR ) signaling in chondrocytes
Wang et al., Mol Cell Biol 1994 : Activation of FGFR-1 in transfected L6 myoblasts induced far stronger phosphorylation of phospholipase C gamma, SHC, and ERK proteins than could activation of FGFR-4 in L6 cells, and only FGFR-1 activation induced tyrosine phosphorylation of a characteristic 80-kD protein