Cited by 629HER2/EGFR in Cancer ResearchReceptor Mechanisms and SignalingProtein Kinase Regulation and GTPase Signaling

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Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor

Yarden, Yosef, Schlessinger, Joseph·1987·Biochemistry

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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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Authors: Yarden, Y., & Schlessinger, J.
ORCID: Yarden, Yosef
Schlessinger, Joseph
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
DOI: 10.1021/bi00379a035
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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Epidermal growth factor induces rapid, reversible aggregation of the purified epidermal growth factor receptor

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