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EPHB2 — GRM5

Text-mined interactions from Literome

Karim et al., J Neurosci 2001 (Inflammation) : We show that activation of mGluR1 and mGluR5 leads to activation of ERK1 and ERK2 in the spinal cord
Peavy et al., J Neurosci 2001 : Interestingly, our studies suggest that mGluR5 mediated ERK2 phosphorylation is dependent on the activation of G ( alphaq ) but is not mediated by the activation of phospholipase Cbeta1, activation of protein kinase C, or increases in intracellular calcium ... These data suggest that mGluR5 increases ERK2 phosphorylation in astrocytes by a novel mechanism involving the activation of G ( alphaq ) and both receptor and nonreceptor tyrosine kinases but that is independent of the activation of phospholipase Cbeta1
Yang et al., J Neurosci 2004 (Calcium Signaling) : This was demonstrated by the findings that the synergistic phosphorylation of ERK induced by coactivation of NMDA receptors and mGluR5 was blocked by either a Tat peptide that disrupts NMDA receptor/PSD-95 binding or small interfering RNAs that selectively reduce cellular levels of Homer1b/c
Mao et al., J Biol Chem 2005 : Role of protein phosphatase 2A in mGluR5 regulated MEK/ERK phosphorylation in neurons ... Together, we have identified a novel, mGluR5 triggered signaling mechanism involving use- and Src dependent inactivation of PP2A, which contributes to mGluR5 activation of MEK1/2 and ERK1/2
Mao et al., J Neurosci 2005 (MAP Kinase Signaling System) : We found that selective activation of mGluR5 , but not mGluR1, increased ERK1/2 phosphorylation ... This was demonstrated by the findings that the mGluR5 mediated ERK1/2 phosphorylation was mostly reduced by a cell-permeable Tat-fusion peptide that selectively disrupted the interaction of mGluR5 with the Homer1b/c and by small interfering RNAs that selectively knocked down cellular levels of Homer1b/c proteins
Jong et al., J Biol Chem 2009 (Calcium Signaling) : Specifically, activation of either cell surface or intracellular mGluR5 leads to JNK, Ca ( 2+ ) /calmodulin dependent protein kinase ( CaMK ), and cyclic adenosine 3',5'-monophosphate-responsive element binding protein phosphorylation, whereas activation of only intracellular mGluR5 leads to ERK1/2 and Elk-1 phosphorylation
Ribeiro et al., J Neurosci 2010 (Disease Models, Animal...) : Moreover, mGluR5 activation leads to higher levels of ERK activation in Hdh ( Q111/Q111 ) than in Hdh ( Q20/Q20 ) striatum
Li et al., J Neurosci 2011 (Pain) : Mitochondrial reactive oxygen species are activated by mGluR5 through IP3 and activate ERK and PKA to increase excitability of amygdala neurons and pain behavior
Peavy et al., J Neurochem 1998 : Taken together, these results suggest that mGluR5 stimulation results in tyrosine phosphorylation of ERK1/2 and other glial proteins