ArticleThe EMBO journal1996
ErbB-2 is a common auxiliary subunit of NDF and EGF receptors: implications for breast cancer.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 214 papers.
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Who cites it
214 citing papers in PubMed, 672 citations in OpenAlex.
- Inverse prognostic impact of ErbB2 mRNA and protein expression level in tumors of soft tissue sarcoma patients.Strahlentherapie und Onkologie : Organ der Deutschen Rontgengesellschaft ... [et al] · 2014Trial
- Differential ErbB receptor dimerization modulates the ability of EGF receptor ligands to regulate metabolic flux.The Journal of biological chemistry · 2026Article
- Features of tumor microenvironment in HER2-positive urothelial carcinoma and its implications for immunotherapy resistance.BMC cancer · 2026Article
- X-ray crystal structure and in silico investigation of Tetrabromo thia-bridged diquinoline including anticancer mechanisms via target prediction and molecular docking.Scientific reports · 2026Article
- Research on Targeted Therapy for Malignant Tumors of the Biliary Tract.OncoTargets and therapy · 2026Review
- Virosomes: Beyond Vaccines.Life (Basel, Switzerland) · 2025Review
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- Investigating incidence of RAS/RAF and PIK3CA alterations in HER2-amplified colorectal cancer: a comprehensive analysis.The oncologist · 2025Article
- Investigating and evaluating potential antigen binding sites for monoclonal anti-HER2 antibodies: The LightDock approach.Computational and structural biotechnology journal · 2025Article
- Personalized therapy in oncology: melanoma as a paradigm for molecular-targeted treatment approaches.Clinical & experimental metastasis · 2024Review
- Targeting solid tumor antigens with chimeric receptors: cancer biology meets synthetic immunology.Trends in cancer · 2024Review
- Are There More HER2 FISH in the Sea? An Institution's Experience in Identifying HER2 Positivity Using Fluorescent In Situ Hybridization in Patients with HER2 Negative Immunohistochemistry.Annals of surgical oncology · 2024Article
- The impact of nitric oxide on HER family post-translational modification and downstream signaling in cancer.Frontiers in physiology · 2024Review
- Mild Cardiotoxicity and Continued Trastuzumab Treatment in the Context of HER2-Positive Breast Cancer.Journal of clinical medicine · 2023Article
- Irreversible tyrosine kinase inhibitors induce the endocytosis and downregulation of ErbB2.Biochemistry and biophysics reports · 2023Article
- MicroRNAs as biomarkers for trastuzumab-based therapy in HER2-positive advanced oesophago-gastric cancer patients.Frontiers in oncology · 2023Article
- Busting the Breast Cancer with AstraZeneca's Gefitinib.Advances in pharmacological and pharmaceutical sciences · 2023Review
- First-line treatment of patients with HER2-positive metastatic gastric and gastroesophageal junction cancer.Bosnian journal of basic medical sciences · 2022Article
- Clustering Molecular Subtypes in Breast Cancer, Immunohistochemical Parameters and Risk of Axillary Nodal Involvement.Journal of personalized medicine · 2022Article
- Ligand-induced transmembrane conformational coupling in monomeric EGFR.Nature communications · 2022Article
154 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Overexpression of the erbB-2 gene contributes to aggressive behavior of various human adenocarcinomas, including breast cancer, through an unknown molecular mechanism. The erbB-2-encoded protein is a member of the ErbB family of growth factor receptors, but no direct ligand of ErbB-2 has been reported. We show that in various cells ErbB-2 can form heterodimers with both EGF receptor (ErbB-1) and NDF receptors (ErbB-3 and ErbB-4), suggesting that it may affect the action of heterologous ligands without the involvement of a direct ErbB-2 ligand. This possibility was addressed in breast cancer cells through either overexpression of ErbB-2 or by blocking its delivery to the cell surface by means of an endoplasmic reticulum-trapped antibody. We report that ErbB-2 overexpression enhanced binding affinities to both EGF and NDF, through deceleration of ligand dissociation rates. Likewise, removal of ErbB-2 from the cell surface almost completely abolished ligand binding by accelerating dissociation of both growth factors. The kinetic effects resulted in enhancement and prolongation of the stimulation of two major cytoplasmic signaling pathways, namely: MAP kinase (ERK) and c-Jun kinase (SAPK), by either ligand. Our results imply that ErbB-2 is a pan-ErbB subunit of the high affinity heterodimeric receptors for NDF and EGF. Therefore, the oncogenic action of ErbB-2 in human cancers may be due to its ability to potentiate in trans growth factor signaling.
Indexed as
Identifiers
8617201PMC449940W1601571585What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.