Gene interactions and pathways from curated databases and text-mining

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BMP10 — EPHB2

Text-mined interactions from Literome

Fan et al., J Cell Physiol 2006 (Cholestasis, Extrahepatic...) : Furthermore, BMP4 stimulated phosphorylation of Smad1 and ERK1/2 in HSCs
Ghayor et al., Biochem Biophys Res Commun 2009 : On the other hand, BMP2 induced Erk phosphorylation ( p44/p42 ) and cell proliferation were suppressed in the presence of cAMP
Jun et al., J Biol Chem 2010 : Because BMP signaling induces Erk activation in osteoblasts, we sought to investigate whether BMP induced Erk signaling regulates Runx2 acetylation and stability
Takeda et al., Mol Cell Endocrinol 2012 (MAP Kinase Signaling System) : Thus, the difference between BMP-6 and BMP-7 in enhancing GnRH induced FSHß transcription may be due to the differential effects of BMP ligands on GnRH induced ERK signaling
Ge et al., J Bone Miner Res 2012 (MAP Kinase Signaling System) : Significantly, in the presence of AA, BMP2/7 synergistically stimulated RUNX2 S319 phosphorylation and transcriptional activity without affecting total RUNX2 and this response was totally dependent on ERK/MAPK activity ... Based on this work, we conclude that extracellular matrix and BMP regulation of RUNX2 phosphorylation and transcriptional activity in osteoblasts is predominantly mediated by ERK rather than p38 MAPKs
Li et al., Cell stem cell 2012 : Here, we show that, whereas LIF sustains relatively high ERK activity, BMP4 can steadily attenuate ERK activity by upregulating ERK-specific dual-specificity phosphatase 9 (DUSP9)
Li et al., Protein Cell 2012 : We recently found that while LIF signaling augments ERK activity, BMP signaling inhibits ERK activity in mouse ES cells via direct upregulation of an ERK phosphatase-dual-specificity phosphatase 9