The DOI matches its Crossref record; 31 of the 31 references it cites were found in a registry or an index.
Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor
Abstract
Epidermal growth factor (EGF) receptor from A-431 cells was purified by affinity chromatography with monoclonal anti-receptor antibodies. The purified radiolabeled receptor was incubated with EGF and then analyzed by gel electrophoresis under nondenaturing conditions. In these gels, the EGF receptor migrates in two forms: a fast-migrating (low) form and an EGF-induced slow-migrating (high) form. On the basis of the various control and calibration experiments described, it is concluded that the low form represents the monomeric 170-kilodalton EGF receptor and the high form represents an EGF receptor dimer. The binding of EGF causes a rapid, temperature-sensitive dimerization of the EGF receptor. Receptor dimerization is fully reversible and involves saturable, noncovalent interactions that are stable at neutral pH and in nonionic detergents. Both the monomeric and dimeric forms of the receptor bind EGF and undergo self-phosphorylation. The dimeric form of the receptor may possess higher ligand binding affinity, and it seems to be phosphorylated earlier than the monomeric form following the addition of EGF and [gamma-32P]ATP. On the basis of these results, it is concluded that receptor oligomerization is an intrinsic property of the occupied EGF receptor and that it may play a role in the activation of the kinase function and the subsequent transmembrane signaling process.
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“Epidermal growth factor receptor (EGFR), a member of the receptor tyrosine kinase family, is a typical transmembrane receptor that initiates signaling cascades upon ligand-stimulated dimerization, thereby activating its tyrosine kinase and multiple downstream effectors.99–101”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [101]
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Dimerization of cell surface receptors in signal transduction
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Graus-Porta, D., Beerli, R. R., Daly, J. M., & Hynes, N. E. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1647 · Cited by 1,617
Epidermal growth factor receptor: Mechanisms of activation and signalling
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Metadata
- Authors
- Yarden, Y., & Schlessinger, J.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1987-03-01
- Volume
- 26
- Issue
- 5
- Pages
- 1443-1451
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2095381863
- Cited by
- 627
- References
- 31
- Citations by year
- 2026: 15 · 2025: 11 · 2024: 8 · 2023: 16 · 2022: 21 · 2021: 5 · 2020: 13 · 2019: 12 · 2018: 14 · 2017: 13 · 2016: 14 · 2015: 19 · 2014: 16 · 2013: 12 · 2012: 11
- FWCI
- 21.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (CA 25820)
- Topics
- Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- epidermal growth factor receptor, receptor dimerization, receptor oligomerization, epidermal growth factor, A431 cells, receptor phosphorylation, ligand binding affinity, kinase activation, transmembrane signaling
- MeSH terms
- Allosteric Regulation, Cell Line, Cross-Linking Reagents, Epidermal Growth Factor, Humans, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Structure-Activity Relationship, Temperature, Macromolecular Substances, ErbB Receptors
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