Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1

Stable Identifier
R-HSA-9665704
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol, plasma membrane
ReviewStatus
5/5
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Phosphorylated heterodimers of ERBB2 TMD/JMD mutants and EGFR phosphorylate PLCG1
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Activation of downstream PLCG1 signaling was demonstrated for ERBB2 R678Q, through activating tyrosine phosphorylation on PLCG1 (Bose et al. 2013). It is assumed that the heterodimer of ERBB2 R678Q and EGFR, like the wild type ERBB2:EGFR heterodimer, binds to and phosphorylates PLCG1, leading to activation of PLCgamma1 signaling.
Literature References
PubMed ID Title Journal Year
23220880 Activating HER2 mutations in HER2 gene amplification negative breast cancer

Bose, R, Kavuri, SM, Searleman, AC, Shen, W, Shen, D, Koboldt, DC, Monsey, J, Goel, N, Aronson, AB, Li, S, Ma, CX, Ding, L, Mardis, ER, Ellis, MJ

Cancer Discov 2013
Participants
Input
Output
Participates
as an event of
Catalyst Activity

protein tyrosine kinase activity of p-6Y-ERBB2 R678Q:EGF:p-6Y-EGFR:PLCG1 [plasma membrane]

Physical Entity
p-6Y-ERBB2 R678Q:EGF:p-6Y-EGFR:PLCG1 [plasma membrane] (Homo sapiens)
Activity
protein tyrosine kinase activity (GO:0004713)
Normal reaction
PLCG1 phosphorylation by p-EGFR:p-ERBB2 (Homo sapiens)
Functional status

Gain of function of p-6Y-ERBB2 R678Q:EGF:p-6Y-EGFR:PLCG1 [plasma membrane]

Normal Entity
Disease Entity
Status
Disease
Name Identifier Synonyms
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
Cross References
Mondo
Authored
Orlic-Milacic, M  (2019-10-31)
Reviewed
Bose, R  (2019-10-25)
Krishna, A  (2019-10-25)
Kancha, RK  (2019-11-03)
Created
Orlic-Milacic, M  (2019-10-31)
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