The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activation
Abstract
The membrane receptor for epidermal growth factor (EGF) is a 170,000-dalton glycoprotein composed of an extracellular EGF-binding domain and a cytoplasmic kinase domain connected by a stretch of 23 amino acids traversing the plasma membrane. The binding of EGF to the extracellular domain activates the cytoplasmic kinase function even in highly purified preparations of EGF receptor, suggesting that the activation occurs exclusively within the EGF receptor moiety. Conceivably, kinase activation may require the transfer of a conformational change through the single transmembrane region from the ligand binding domain to the cytoplasmic kinase region. Alternatively, ligand-induced receptor-receptor interactions may activate the kinase and thus bypass this requirement. Both mechanisms were contrasted by employing independent experimental approaches. The following lines of evidence support an intermolecular mechanism for the activation of the detergent-solubilized receptor: the EGF-induced receptor self-phosphorylation has a parabolic dependence on the concentration of EGF receptor, cross-linking of EGF receptors by antibodies or lectins stimulates receptor self-phosphorylation, immobilization of EGF receptor on various solid matrices prevents EGF from activating the kinase function, and cross-linking of EGF receptors increases their affinity toward EGF. On the basis of these results, an allosteric aggregation model is formulated for the activation of the cytoplasmic kinase function of the receptor by EGF. This model may be relevant to the mechanism by which the mitogenic signal of EGF is transferred across the membrane.
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Cites
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Self-citationClose similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
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Cited by
Signal transduction by receptors with tyrosine kinase activity
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Self-citationEpidermal Growth Factor Receptor Cell Proliferation Signaling Pathways
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An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
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Epidermal growth factor receptor: Mechanisms of activation and signalling
Jorissen, R. (2003) · Experimental Cell Research · doi:10.1016/s0014-4827(02)00098-8 · Cited by 1,565
Identification of Heregulin, a Specific Activator of p185 erbB2
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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
- 1434-1442
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2062706311
- Cited by
- 507
- References
- 42
- FWCI
- 19.63
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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