◀ Back to ERBB2
ERBB2 — PIK3R1
Pathways - manually collected, often from reviews:
-
KEGG Focal adhesion:
EGFR/ERBB2/FLT1/FLT4/IGF1R/KDR/MET/PDGFRA/PDGFRB
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, activation)
-
KEGG Pathways in cancer:
ERBB2
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, activation)
-
KEGG Pancreatic cancer:
Complex of EGFR-ERBB2
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, indirect effect)
-
KEGG Prostate cancer:
EGFR/ERBB2/FGFR1/FGFR2/IGF1R/INSRR/PDGFRA/PDGFRB
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, activation)
-
KEGG ErbB signaling pathway:
Complex of ERBB2-ERBB4
→
PIK3CA/PIK3CB/PIK3CD/PIK3CG/PIK3R1/PIK3R2/PIK3R3/PIK3R5
(protein-protein, activation)
-
Reactome Reaction:
ERBB2
→
PIK3R1
(reaction)
Jackson et al., Cancer Res 2004, Yang et al., J Cell Sci 2007*, Kaushansky et al., Chem Biol 2008, Cohen et al., J Biol Chem 1996
-
Reactome Reaction:
ERBB2
→
PIK3R1
(indirect_complex)
Jackson et al., Cancer Res 2004, Yang et al., J Cell Sci 2007*, Kaushansky et al., Chem Biol 2008, Cohen et al., J Biol Chem 1996
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
-
IRef Biogrid Interaction:
PIK3R1
—
ERBB2
(physical association, affinity chromatography technology)
Crovello et al., J Biol Chem 1998
-
IRef Biogrid Interaction:
PIK3R1
—
ERBB2
(direct interaction, unspecified method)
Jones et al., Nature 2006
-
IRef Hprd Interaction:
PIK3R1
—
ERBB2
(in vivo)
Peles et al., J Biol Chem 1992*, Wang et al., Cancer Cell 2006
-
IRef Intact Interaction:
Complex of SRC-ERBB2-PIK3R1-ERBB3
(association, anti bait coimmunoprecipitation)
Liang et al., Cancer Cell 2010*
-
IRef Intact Interaction:
Complex of 13 proteins
(association, pull down)
Wang et al., Cancer Cell 2006
-
IRef Intact Interaction:
ERBB2
—
PIK3R1
(direct interaction, protein array)
Jones et al., Nature 2006
-
IRef Intact Interaction:
Complex of ERBB2-PIK3R1-ERBB2-ERBB3-ERBB2-PIK3R1-PIK3R1-ERBB3-ERBB3
(association, anti bait coimmunoprecipitation)
Liang et al., Cancer Cell 2010*
-
IRef Intact Interaction:
Complex of PIK3R1-SHC1-ERBB2-ERBB3-EGFR
(association, pull down)
Wang et al., Cancer Cell 2006
-
IRef Ophid Interaction:
ERBB2
—
PIK3R1
(aggregation, interologs mapping)
Brown et al., Bioinformatics 2005
Text-mined interactions from Literome
Ram et al., J Cell Physiol 2000
(Breast Neoplasms) :
Phosphatidylinositol 3-kinase (PI3K) is activated by
p185(erbB-2) /erbB-3 heterodimers in cells stimulated by HRG, and
PI3K is constitutively
activated by p185(erbB-2) /erbB-3 in breast carcinoma cells that overexpress c-erbB-2 ... Furthermore, erbB-3 principally mediated the direct recruitment of p85 in cells stimulated by HRG or EGF, indicating that, in addition to the high-level
activation of
PI3K by
p185(erbB-2) / erbB-3, EGFR/erbB-3 heterodimer interaction is essential for the weak but significant level of PI3K activated by EGF in cells that express normal EGFR levels
Folgiero et al., Cancer Res 2007
(Breast Neoplasms...) :
Given that
ErbB-2 can
activate PI3K only when it heterodimerizes with other members of the epidermal growth factor receptor family, these data imply that other receptors cooperate in this process
Porzia et al., J Immunol 2010
(Mammary Neoplasms, Experimental) :
In conclusion, vaccine induced anti-ErbB2 Abs directly affected the transformed phenotype of rat ErbB2 ( + ) tumors by impairing
ErbB2 mediated
PI3K/Akt signaling