◀ Back to EGFR
EGFR — ERBB2
Pathways - manually collected, often from reviews:
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OpenBEL Selventa BEL large corpus:
EGFR
→
Heregulin beta1/ERBB2 complex (ERBB2)
(increases, ERBB2 Activity)
Evidence: studies of MCF-7 breast cancer cells stimulated with heregulin showed increased HIF-1a protein synthesis that was inhibited by treatment with rapamycin a macrolide antibiotic that inhibits mammalian target of rapamycin (mTOR; a kinase that functions downstream of PI3K and AKT). The effect of heregulin was mediated via the 5-untranslated region of HIF-1a mRNA47. The known targets for phosphorylation by mTOR are regulators of protein synthesis (FIG. 1).
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OpenBEL Selventa BEL large corpus:
EGFR
→
Complex of EGFR-ERBB2
(directlyIncreases, EGFR/ERBB2 Activity)
Evidence: The dimerization of two EGFR family molecules leads to phosphorylation of C-terminal tyrosine residues either by autophosphorylation or by a SRC-related kinase followed by binding of GRB2, a RAS adaptor protein, at the SH2 domain of the receptor; binding of the proline-rich C-terminus of SOS, a guanine nucleotide exchange factor, to the SH3 domain of the receptor; exchange of a GTP from the receptor complex for a GDP from the RAS protein to form activated RAS; activation of phosphatidylinositol-...
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OpenBEL Selventa BEL large corpus:
EGFR
→
Complex of EGFR-ERBB2
(directlyIncreases, EGFR/ERBB2 Activity)
Evidence: The first group includes EGF, amphiregulin (AR), and transforming growth factor-alpha (TGF-alpha), which bind specifically to ErbB1; the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4. The third group is composed of the neuregulins (NRG) and forms two subgroups based upon their capacity to bind ErbB3 and ErbB4 (NRG-1 and NRG-2) or only ErbB4 (NRG-3 and NRG-4). ErbB2 has no direct ligand and nee...
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OpenBEL Selventa BEL large corpus:
EGFR
→
Complex of EGFR-ERBB2
(directlyIncreases, EGFR/ERBB2 Activity)
Evidence: Figure 1 , ERBB receptors, ligands, dimers and downstream signalling pathways. a , Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the ...
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OpenBEL Selventa BEL large corpus:
ERBB2
→
Complex of EGFR-ERBB2
(directlyIncreases, EGFR/ERBB2 Activity)
Evidence: The first group includes EGF, amphiregulin (AR), and transforming growth factor-alpha (TGF-alpha), which bind specifically to ErbB1; the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4. The third group is composed of the neuregulins (NRG) and forms two subgroups based upon their capacity to bind ErbB3 and ErbB4 (NRG-1 and NRG-2) or only ErbB4 (NRG-3 and NRG-4). ErbB2 has no direct ligand and nee...
-
OpenBEL Selventa BEL large corpus:
ERBB2
→
Complex of EGFR-ERBB2
(directlyIncreases, EGFR/ERBB2 Activity)
Evidence: Figure 1 , ERBB receptors, ligands, dimers and downstream signalling pathways. a , Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the ...
-
OpenBEL Selventa BEL large corpus:
PIK3C2A
→
Complex of EGFR-ERBB2
(increases, EGFR/ERBB2 Activity, PIK3C2A Activity)
Arcaro et al., Mol Cell Biol 2000*
Evidence: Stimulation of quiescent cultures with EGF resulted in the rapid recruitment of both enzymes to a phosphotyrosine signaling complex that contained the EGF receptor and Erb-B2.
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OpenBEL Selventa BEL large corpus:
PIK3C2B
→
Complex of EGFR-ERBB2
(increases, EGFR/ERBB2 Activity, PIK3C2B Activity)
Arcaro et al., Mol Cell Biol 2000*
Evidence: Stimulation of quiescent cultures with EGF resulted in the rapid recruitment of both enzymes to a phosphotyrosine signaling complex that contained the EGF receptor and Erb-B2.
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OpenBEL Selventa BEL large corpus:
Complex of EGFR-ERBB2
→
EGFR/EGFR Ligand Family complex (EGFR)
(directlyIncreases)
Evidence: The first group includes EGF, amphiregulin (AR), and transforming growth factor-alpha (TGF-alpha), which bind specifically to ErbB1; the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4. The third group is composed of the neuregulins (NRG) and forms two subgroups based upon their capacity to bind ErbB3 and ErbB4 (NRG-1 and NRG-2) or only ErbB4 (NRG-3 and NRG-4). ErbB2 has no direct ligand and nee...
-
OpenBEL Selventa BEL large corpus:
Complex of EGFR-ERBB2
→
BTC
(directlyIncreases)
Evidence: the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4.
-
OpenBEL Selventa BEL large corpus:
Complex of EGFR-ERBB2
→
EGF
(directlyIncreases)
Evidence: Figure 1 , ERBB receptors, ligands, dimers and downstream signalling pathways. a , Members of the epidermal growth factor (EGF) family of growth factors are ligands for the ERBB receptors. Ligand binding to ERBB receptors induces the formation of receptor homo- and heterodimers and the activation of the intrinsic kinase domain, resulting in phosphorylation on specific tyrosine residues within the cytoplasmic tail. These phosphorylated residues serve as docking sites for a range of proteins, the ...
-
OpenBEL Selventa BEL large corpus:
ERBB2
→
EGFR
(directlyIncreases, ERBB2 Activity)
Evidence: The first group includes EGF, amphiregulin (AR), and transforming growth factor-alpha (TGF-alpha), which bind specifically to ErbB1; the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4. The third group is composed of the neuregulins (NRG) and forms two subgroups based upon their capacity to bind ErbB3 and ErbB4 (NRG-1 and NRG-2) or only ErbB4 (NRG-3 and NRG-4). ErbB2 has no direct ligand and nee...
-
OpenBEL Selventa BEL large corpus:
ERBB2
→
EGFR
(increases, ERBB2 Activity)
Evidence: This is taken from supplemental table 2 from PMID 15951569 Cut-offs were 2.25 for increase and 0.5 for decrease LLID were found by converting from GI assession numbers in DAVID Spreadsheet is saved in the project folder for Cell Signaling Project # bduckworth
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OpenBEL Selventa BEL large corpus:
Complex of EGFR-ERBB2
→
EREG
(directlyIncreases)
Evidence: the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4.
-
OpenBEL Selventa BEL large corpus:
Complex of EGFR-ERBB2
→
HBEGF
(directlyIncreases)
Evidence: the second group betacellulin (BTC), heparin-binding EGF (HB-EGF), and epiregulin (EPR), which exhibit dual specificity in that they bind ErbB1 and ErbB4.
-
BioCarta trefoil factors initiate mucosal healing:
TFFs/ErbB1/ERBB2 complex (EGFR-ERBB2-TFF3_TFF2_TFF1)
→
beta-catenin (CTNNB1)
(modification, activates)
-
BioCarta role of erbb2 in signal transduction and oncology:
ERBB2/ERBB 1/3/4 complex (ERBB2-ERBB4_ERBB3_EGFR)
→
ERBB ligand/ERBB2/ERBB 1/3/4 complex (ERBB2-ERBB4_ERBB3_EGFR)
(modification, collaborate)
-
BioCarta trefoil factors initiate mucosal healing:
TFFs/ErbB1/ERBB2 complex (EGFR-ERBB2-TFF3_TFF2_TFF1)
→
SHC/GRB2/SOS-1 complex (SOS1-GRB2-SHC1)
(modification, activates)
-
BioCarta trefoil factors initiate mucosal healing:
TFFs (TFF3/TFF2/TFF1)
→
TFFs/ErbB1/ERBB2 complex (EGFR-ERBB2-TFF3_TFF2_TFF1)
(modification, collaborate)
-
BioCarta trefoil factors initiate mucosal healing:
TFFs (TFF3/TFF2/TFF1)
→
ErbB1/ERBB2 complex (EGFR-ERBB2)
(modification, collaborate)
-
BioCarta trefoil factors initiate mucosal healing:
TFFs/ErbB1/ERBB2 complex (EGFR-ERBB2-TFF3_TFF2_TFF1)
→
ErbB1/ERBB2 complex (EGFR-ERBB2)
(modification, collaborate)
-
BioCarta role of erbb2 in signal transduction and oncology:
ERBB ligand/ERBB2/ERBB 1/3/4 complex (ERBB2-ERBB4_ERBB3_EGFR)
→
SHC/GRB2/SOS-1 complex (SOS1-GRB2-SHC1)
(modification, activates)
-
KEGG Pancreatic cancer:
EGFR
→
ERBB2
(protein-protein, binding/association)
-
KEGG Pancreatic cancer:
Complex of EGFR-ERBB2
→
JAK1
(protein-protein, activation)
-
KEGG Pancreatic cancer:
Complex of EGFR-ERBB2
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, indirect effect)
-
NCI Pathway Database ErbB receptor signaling network:
EGF (EGF)
→
EGFR/ErbB2/EGF complex (EGFR-ERBB2-EGF)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
HSP90 (dimer) complex (HSP90AA1)
→
EGFR/ErbB2/EGF complex (EGFR-ERBB2-EGF)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
ErbB2/ErbB2/HSP90 (dimer) complex (ERBB2-HSP90AA1)
→
EGFR/ErbB2/EGF complex (EGFR-ERBB2-EGF)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
ErbB2/ErbB2/HSP90 (dimer) complex (ERBB2-HSP90AA1)
→
EGFR (EGFR)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
ErbB2 (ERBB2)
→
EGFR/ErbB2/EGF complex (EGFR-ERBB2-EGF)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
ErbB2 (ERBB2)
→
EGFR (EGFR)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/EGF complex (EGFR-ERBB2-EGF)
→
EGFR (EGFR)
(modification, collaborate)
Citri et al., EMBO Rep 2004, Hazan et al., Cell Growth Differ 1990, Stern et al., EMBO J 1988*, Qian et al., Proc Natl Acad Sci U S A 1994, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database a6b1 and a6b4 Integrin signaling:
EGF/EGFR complex (EGF-EGFR)
→
ErbB2 (ERBB2)
(modification, activates)
Russell et al., J Cell Sci 2003, Yoon et al., Cancer Res 2006
Evidence: assay
-
NCI Pathway Database ErbB receptor signaling network:
betacellulin (BTC)
→
EGFR/ErbB2/betacellulin complex (EGFR-ERBB2-BTC)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
EGFR/ErbB2/betacellulin complex (EGFR-ERBB2-BTC)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
ErbB2 (ERBB2)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/betacellulin complex (EGFR-ERBB2-BTC)
→
ErbB2 (ERBB2)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
EGFR/ErbB2/amphiregulin complex (EGFR-ERBB2-AREGB)
(modification, collaborate)
Jones et al., FEBS Lett 1999*, Johnson et al., J Biol Chem 1993*, Riese et al., J Biol Chem 1996
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
ErbB2 (ERBB2)
(modification, collaborate)
Jones et al., FEBS Lett 1999*, Johnson et al., J Biol Chem 1993*, Riese et al., J Biol Chem 1996
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
amphiregulin (AREGB)
→
EGFR/ErbB2/amphiregulin complex (EGFR-ERBB2-AREGB)
(modification, collaborate)
Jones et al., FEBS Lett 1999*, Johnson et al., J Biol Chem 1993*, Riese et al., J Biol Chem 1996
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/amphiregulin complex (EGFR-ERBB2-AREGB)
→
ErbB2 (ERBB2)
(modification, collaborate)
Jones et al., FEBS Lett 1999*, Johnson et al., J Biol Chem 1993*, Riese et al., J Biol Chem 1996
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
EGFR/ErbB2/epiregulin complex (EGFR-ERBB2-EREG)
(modification, collaborate)
Komurasaki et al., Oncogene 1997
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
ErbB2 (ERBB2)
(modification, collaborate)
Komurasaki et al., Oncogene 1997
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/epiregulin complex (EGFR-ERBB2-EREG)
→
ErbB2 (ERBB2)
(modification, collaborate)
Komurasaki et al., Oncogene 1997
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/epiregulin complex (EGFR-ERBB2-EREG)
→
epiregulin (EREG)
(modification, collaborate)
Komurasaki et al., Oncogene 1997
Evidence: physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/HBEGF complex (EGFR-ERBB2-HBEGF)
→
EGFR (EGFR)
(modification, collaborate)
Hazan et al., Cell Growth Differ 1990, Qian et al., Proc Natl Acad Sci U S A 1994, Riese et al., J Biol Chem 1996, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/HBEGF complex (EGFR-ERBB2-HBEGF)
→
HBEGF (HBEGF)
(modification, collaborate)
Hazan et al., Cell Growth Differ 1990, Qian et al., Proc Natl Acad Sci U S A 1994, Riese et al., J Biol Chem 1996, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/HBEGF complex (EGFR-ERBB2-HBEGF)
→
ErbB2 (ERBB2)
(modification, collaborate)
Hazan et al., Cell Growth Differ 1990, Qian et al., Proc Natl Acad Sci U S A 1994, Riese et al., J Biol Chem 1996, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
ErbB2 (ERBB2)
(modification, collaborate)
Hazan et al., Cell Growth Differ 1990, Qian et al., Proc Natl Acad Sci U S A 1994, Riese et al., J Biol Chem 1996, Graus-Porta et al., EMBO J 1997
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/TGFA complex (EGFR-ERBB2-TGFA)
→
EGFR (EGFR)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/TGFA complex (EGFR-ERBB2-TGFA)
→
TGFA (TGFA)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR/ErbB2/TGFA complex (EGFR-ERBB2-TGFA)
→
ErbB2 (ERBB2)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
NCI Pathway Database ErbB receptor signaling network:
EGFR (EGFR)
→
ErbB2 (ERBB2)
(modification, collaborate)
Riese et al., J Biol Chem 1996
Evidence: assay, physical interaction
-
Reactome Reaction:
EGFR
→
ERBB2
(reaction)
Borg et al., Nat Cell Biol 2000, Xu et al., J Biol Chem 2001, Vijapurkar et al., Exp Cell Res 2003, Citri et al., EMBO Rep 2004, Xu et al., Nature structural & molecular biology 2005, Fazioli et al., Mol Cell Biol 1991*, Walton et al., J Biol Chem 1990, Li et al., Cell Signal 2007, Xu et al., Mol Cell Biol 2007, Hazan et al., Cell Growth Differ 1990, Kaushansky et al., Chem Biol 2008, Wada et al., Cell 1990, Helin et al., J Biol Chem 1991, Margolis et al., J Biol Chem 1989, Ricci et al., Oncogene 1995, Wallasch et al., EMBO J 1995, Prigent et al., EMBO J 1994, Soler et al., Oncogene 1994, Segatto et al., Oncogene 1993, Karunagaran et al., EMBO J 1996, Cohen et al., J Biol Chem 1996, Pinkas-Kramarski et al., EMBO J 1996, Cohen et al., J Biol Chem 1996*
-
Reactome Reaction:
EGFR
→
ERBB2
(indirect_complex)
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Bind_translation Interaction:
EGFR
—
ERBB2
(coimmunoprecipitation)
Ling et al., Cancer Cell 2005*
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Haslekås et al., Mol Biol Cell 2005*
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Riedemann et al., Biochem Biophys Res Commun 2007*
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Scaltriti et al., Oncogene 2009*
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Burke et al., Mol Biol Cell 2001
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Meijer et al., Cell Signal 2011*
-
IRef Biogrid Interaction:
EGFR
—
ERBB2
(physical association, affinity chromatography technology)
Shtiegman et al., Oncogene 2007*
-
MIPS CORUM EGFR-containing signaling complex:
EGFR-containing signaling complex complex (EGFR-ERBB2-PIK3C2A-PIK3C2B)
Arcaro et al., Mol Cell Biol 2000*
-
IRef Corum Interaction:
Complex of ERBB2-EGFR-PIK3C2B-PIK3C2A
(association, coimmunoprecipitation)
Arcaro et al., Mol Cell Biol 2000*
-
IRef Dip Interaction:
ERBB2
—
EGFR
(physical association, anti bait coimmunoprecipitation)
Gijsen et al., PLoS Biol 2010*
-
IRef Hprd Interaction:
EGFR
—
ERBB2
(in vivo)
Dankort et al., J Biol Chem 2001*, Brockhoff et al., Cytometry 2001*, Dittmar et al., FASEB J 2002*, Wang et al., Cancer Cell 2006, Hazan et al., Cell Growth Differ 1990, Maegawa et al., Mol Cancer Res 2007*
-
IRef Hprd Interaction:
EGFR
—
ERBB2
(in vitro)
Dankort et al., J Biol Chem 2001*, Brockhoff et al., Cytometry 2001*, Dittmar et al., FASEB J 2002*, Wang et al., Cancer Cell 2006, Hazan et al., Cell Growth Differ 1990, Maegawa et al., Mol Cancer Res 2007*
-
IRef Intact Interaction:
Complex of 23 proteins
(association, anti bait coimmunoprecipitation)
Thelemann et al., Mol Cell Proteomics 2005
-
IRef Intact Interaction:
Complex of 14 proteins
(association, tandem affinity purification)
Li et al., Molecular systems biology 2013
-
IRef Intact Interaction:
Complex of 64 proteins
(association, tandem affinity purification)
Li et al., Molecular systems biology 2013
-
IRef Intact Interaction:
Complex of 59 proteins
(association, tandem affinity purification)
Li et al., Molecular systems biology 2013
-
IRef Intact Interaction:
Complex of 26 proteins
(association, tandem affinity purification)
Li et al., Molecular systems biology 2013
-
IRef Intact Interaction:
Complex of UBASH3B-CDC37-EGFR-ERBB3-ERRFI1-SHC1-ERBB2-STAT3
(association, anti bait coimmunoprecipitation)
Li et al., Molecular systems biology 2013
-
IRef Intact Interaction:
ERBB2
—
EGFR
(physical association, anti bait coimmunoprecipitation)
Fernandes et al., Am J Respir Cell Mol Biol 1999*
-
IRef Intact Interaction:
ERBB2
—
EGFR
(physical association, anti bait coimmunoprecipitation)
Beier et al., FEBS Lett 2006*
-
IRef Intact Interaction:
ERBB2
—
EGFR
(physical association, protein kinase assay)
Wang et al., Cancer Cell 2006
-
IRef Intact Interaction:
ERBB2
—
EGFR
(physical association, protein cross-linking with a bifunctional reagent)
Serra et al., Oncogene 2011*
-
IRef Intact Interaction:
Complex of 13 proteins
(association, pull down)
Wang et al., Cancer Cell 2006
-
IRef Intact Interaction:
Complex of 70 proteins
(association, anti bait coimmunoprecipitation)
Thelemann et al., Mol Cell Proteomics 2005
-
IRef Intact Interaction:
Complex of PIK3R1-SHC1-ERBB2-ERBB3-EGFR
(association, pull down)
Wang et al., Cancer Cell 2006
-
IRef Ophid Interaction:
ERBB2
—
EGFR
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Chen et al., Biochem Biophys Res Commun 2000
(Breast Neoplasms) :
Together, our results suggest that coexpression of
EGFR or ErbB3 with ErbB2
induces high phosphorylation of
ErbB2 and renders the cells more resistant to various anti-cancer drugs
Egeblad et al., Int J Cancer 2001
(Breast Neoplasms) :
Truncated
ErbB2 receptor
enhances ErbB1 signaling and induces reversible, ERK independent loss of epithelial morphology
Bei et al., J Pathol 2001
(Carcinoma, Squamous Cell...) :
Among invasive and in situ carcinoma,
EGFR expression was the most prevalent ( in 29/32 and 8/11 cases, respectively )
followed by
ErbB2 ( 17/32 and 2/11 ) and ErbB4 ( 9/32 and 1/10 ), while ErbB3 was only detected in invasive tumours ( 12/32 )
Feroz et al., Cell Signal 2002
:
Thus, we hypothesized that
ErbB2 enhances ligand induced
ErbB family receptor signalling through mass action
Lin et al., Prostate 2003
:
Because the pressor peptide Ang II signals through GPCRs, we tested the possibility that
Ang II could
transactivate ErbB1/ErbB2 in human prostate stromal ( hPS ) cells
Iivanainen et al., FASEB J 2003
:
3 ) Consistent with their known receptor specificities, recombinant HB-EGF, but not neuregulin-1, stimulated tyrosine phosphorylation of
ErbB1 and ErbB2 and migration in SMCs. 4 ) Neutralization of HB-EGF or inhibition of ErbB1 or
ErbB2 blocked 70-90 % of the potential of ECs to stimulate SMC migration
Gillgrass et al., Oncogene 2003
(Disease Progression...) :
To directly assess whether the catalytic activity of
EGFR is
required for
ErbB-2 induction of mammary tumors, we have interbred transgenic mice expressing ErbB-2 oncogene under the transcriptional control of the mouse mammary tumor virus ( MMTV ) promoter/enhancer to a naturally occurring mouse mutant carrying a catalytically impaired EGFR ( waved-2 mice )
Kani et al., J Biol Chem 2005
:
ErbB receptors associate in a ligand dependent or -independent manner, and overexpression of epidermal growth factor receptor ( ErbB1 ) or
ErbB2 results in ligand independent activation
Haslekås et al., Mol Biol Cell 2005
:
We have demonstrated that
ErbB2 does not
inhibit phosphorylation or ubiquitination of the
EGFR
Yoon et al., Cancer Res 2006
(Breast Neoplasms...) :
ErbB2 , a binding partner of epidermal growth factor receptor (EGFR), and EGFR modulated Ras activity, and integrin alpha(6)beta ( 4 )
regulated phospho-EGFR level without affecting EGFR expression
Beier et al., FEBS Lett 2006
:
Activation of
ErbB2 by 2-methyl-1,4-naphthoquinone ( menadione ) in human keratinocytes : role of
EGFR and protein tyrosine phosphatases
Zandi et al., Cell Signal 2007
(Neoplasms) :
Heterodimerization of EGFR with
ErbB2 inhibits downregulation of
EGFR and thereby prolongs growth factor signaling
Landau et al., Biochim Biophys Acta 2008
(Neoplasms) :
That finding enabled us to elucidate, in molecular terms, the directionality observed in the activation process of ErbB heterodimers ; it can explain, for example, the preferential
activation of
ErbB2 by
ErbB1 over activation of ErbB1 by ErbB2
Martin et al., Mol Pharmacol 2008
:
Coexpression of dominant negative ERBB1 and dominant negative
ERBB2 inhibited basal and EGF stimulated
ERBB1 and ERBB2 phosphorylation in parental and adapted cells
Hughes et al., Mol Cancer Ther 2009
:
Epidermal growth factor receptor (EGFR) and
ErbB2 readily form heterodimers when both are expressed in the same cell and the
EGFR is
activated by one of its ligands
Lokeshwar et al., Cancer Res 2010
(Neoplasm Invasiveness...) :
4-MU
induced caspase-8, caspase-9, and caspase-3 activation, PARP cleavage, upregulation of Fas-L, Fas, FADD and DR4, and downregulation of bcl-2, phosphorylated bad, bcl-XL, phosphorylated Akt, phosphorylated IKB, phosphorylated
ErbB2 , and phosphorylated
epidermal growth factor receptor
Grassian et al., J Biol Chem 2011
:
ErbB2 stabilizes
epidermal growth factor receptor (EGFR) expression via Erk and Sprouty2 in extracellular matrix detached cells
Li et al., J Biol Chem 2012
:
Quantitation of the
effect of
ErbB2 on
epidermal growth factor receptor binding and dimerization
Sak et al., Carcinogenesis 2013
(Breast Neoplasms) :
Overexpression of
ErbB2 has been demonstrated to
inhibit epidermal growth factor induced internalization and degradation of
epidermal growth factor receptor
Sasaoka et al., J Biol Chem 1996
:
In Delta973-EGFR cells,
ErbB2 was tyrosine phosphorylated in the basal state and EGFR
stimulated further phosphorylation of
ErbB2
Gulliford et al., Oncogene 1997
(Carcinoma, Squamous Cell) :
Here we use both an ErbB2 phosphoantibody ( aPY1222 ) and an activation-specific EGFR antibody to show that low concentrations of EGF
induce more efficient tyrosine phosphorylation of
ErbB2 in A431 cells than does equimolar TGFalpha, while
EGFR is more potently activated by TGFalpha