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EGFR — JAK2

Protein-Protein interactions - manually collected from original source literature:

Studies that report less than 10 interactions are marked with *

• IRef Biogrid Interaction: EGFR — JAK2 (direct interaction, unspecified method) Jones et al., Nature 2006
• IRef Biogrid Interaction: EGFR — JAK2 (physical association, affinity chromatography technology) Olayioye et al., J Biol Chem 1999
• IRef Hprd Interaction: EGFR — JAK2 (in vitro) Levkowitz et al., Mol Cell 1999, Yamauchi et al., Nature 1997*
• IRef Hprd Interaction: EGFR — JAK2 (in vivo) Levkowitz et al., Mol Cell 1999, Yamauchi et al., Nature 1997*
• IRef Innatedb Interaction: EGFR — JAK2 (unknown, -) Andl et al., Am J Physiol Gastrointest Liver Physiol 2004
• IRef Intact Interaction: EGFR — JAK2 (direct interaction, protein array) Jones et al., Nature 2006
• IRef Ophid Interaction: EGFR — JAK2 (aggregation, interologs mapping) Brown et al., Bioinformatics 2005

Text-mined interactions from Literome

Shida et al., Cancer Res 2005 (MAP Kinase Signaling System...) : These findings indicate the involvement of EGFR transactivation in the activation of JAK2 and ERK1/2
Lee et al., Mol Cancer Ther 2006 (Carcinoma, Squamous Cell...) : We conclude that SOCS-1 methylation status can differentially affect STAT3 activation by IL-6R and EGFR through JAK or MEK in different HNSCC and response to pharmacologic antagonists
Coaxum et al., Biochim Biophys Acta 2009 : The EGFR kinase inhibitor, AG1478, blocked activation of NHE-1, but did not block EGF induced phosphorylation of Jak2 or CaM ... These results suggest that EGF induces NHE-1 activity in podocytes through two pathways : ( 1 ) EGF -- > EGFR -- > Jak2 activation ( independent of EGFR tyrosine kinase activity ) -- > tyrosine phosphorylation of CaM -- > CaM binding to NHE-1 -- > conformational change of NHE-1 -- > activation of NHE-1 ; and ( 2 ) EGF -- > EGFR -- > EGFR kinase activation -- > association of CaM with NHE-1 ( independent of Jak2 ) -- > conformational change of NHE-1 -- > activation of NHE-1
Bauer et al., Cell Host Microbe 2012 : We find that hBD3 is highly active against H. pylori in vitro and is rapidly induced during early infection via EGFR dependent activation of MAP kinase and JAK/STAT signaling
He et al., Science signaling 2013 : We found that EGFR signaling was blocked by a small molecule ( G5-7 ) that selectively inhibited Janus kinase 2 (JAK2) mediated phosphorylation and activation of EGFR and STAT3 ( signal transducer and activator of transcription 3 ) by binding to JAK2 , thereby decreasing the activity of downstream signaling by mTOR ( mammalian target of rapamycin ) and inducing cell cycle arrest