ArticleProceedings of the National Academy of Sciences of the United States of America2006
A system for quantifying dynamic protein interactions defines a role for Herceptin in modulating ErbB2 interactions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 84 citations in OpenAlex.
- Multicenter phase II study of neoadjuvant lapatinib and trastuzumab with hormonal therapy and without chemotherapy in patients with human epidermal growth factor receptor 2-overexpressing breast cancer: TBCRC 006.Journal of clinical oncology : official journal of the American Society of Clinical Oncology · 2013Trial
- ERBB Receptors and Their Ligands in the Developing Mammary Glands of Different Species: Fifteen Characters in Search of an Author.Journal of mammary gland biology and neoplasia · 2023Review
- Critical roles for EGFR and EGFR-HER2 clusters in EGF binding of SW620 human carcinoma cells.Journal of the Royal Society, Interface · 2022Article
- Non-phosphorylated Tyr-1248 form of human epidermal growth factor receptor 2 (HER2) predicts resistance to trastuzumab therapy and poor disease-free survival of HER2-positive breast cancer patients.Croatian medical journal · 2022Article
- Flubendazole Plays an Important Anti-Tumor Role in Different Types of Cancers.International journal of molecular sciences · 2022Review
- Physiological Considerations for ModelingFrontiers in pharmacology · 2022Review
- Article
- Trastuzumab Blocks the Receiver Function of HER2 Leading to the Population Shifts of HER2-Containing Homodimers and Heterodimers.Antibodies (Basel, Switzerland) · 2021Article
- EGFR forms ligand-independent oligomers that are distinct from the active state.The Journal of biological chemistry · 2020Article
- Receptor Tyrosine Kinase-Targeted Cancer Therapy.International journal of molecular sciences · 2018Review
- Polyfunctional anti-human epidermal growth factor receptor 3 (anti-HER3) antibodies induced by HER3 vaccines have multiple mechanisms of antitumor activity against therapy resistant and triple negative breast cancers.Breast cancer research : BCR · 2018Article
- Muscling toward therapy with ERBB3 and NGFR.Nature cell biology · 2018Article
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- Article
- A monoclonal antibody targeting ErbB2 domain III inhibits ErbB2 signaling and suppresses the growth of ErbB2-overexpressing breast tumors.Oncogenesis · 2016Article
- The voltage gated Ca(2+)-channel Cav3.2 and therapeutic responses in breast cancer.Cancer cell international · 2016Article
- Tunicamycin enhances the antitumor activity of trastuzumab on breast cancer in vitro and in vivo.Oncotarget · 2015Article
- The Therapeutic Challenge of Targeting HER2 in Endometrial Cancer.The oncologist · 2015Review
- Development of trastuzumab-resistant human gastric carcinoma cell lines and mechanisms of drug resistance.Scientific reports · 2015Article
- Application guide for omics approaches to cell signaling.Nature chemical biology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
The orphan receptor tyrosine kinase ErbB2 is activated by each of the EGFR family members upon ligand binding. However, difficulties monitoring the dynamic interactions of the membrane receptors have hindered the elucidation of the mechanism of ErbB2 activation. We have engineered a system to monitor protein-protein interactions in intact mammalian cells such that different sets of protein interactions can be quantitatively compared. Application of this system to the interactions of the EGFR family showed that ErbB2 interacts stably with the EGFR and ErbB3, but fails to spontaneously homooligomerize. The widely used anti-cancer antibody Herceptin was found to effectively inhibit the interaction of the EGFR and ErbB2 but not to interfere with the interaction of ErbB2-ErbB3. Treatment of cells expressing EGFR and ErbB2 with Herceptin results in increased EGFR homooligomerization in the presence of EGF and a subsequent rapid internalization and down-regulation of the EGFR. In summary, the protein interaction system described here enabled the characterization of ErbB2 interactions within the biological context of the plasma membrane and provides insight into the mechanism of Herceptin action on cells overexpressing ErbB2.
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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.