The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
All ErbB Receptors Other Than the Epidermal Growth Factor Receptor Are Endocytosis Impaired
Open accessAbstract
Four transmembrane tyrosine kinases constitute the ErbB receptor family: the epidermal growth factor (EGF) receptor, ErbB-2, ErbB-3, and ErbB-4. We have measured the endocytic capacities of all four members of the EGF receptor family, including ErbB-3 and ErbB-4, which have not been described previously. EGF-responsive chimeric receptors containing the EGF receptor extracellular domain and different ErbB cytoplasmic domains (EGFR/ErbB) have been employed. The capacity of these growth factor-receptor complexes to mediate 125I-EGF internalization, receptor down-regulation, receptor degradation, and receptor co-immunoprecipitation with AP-2 was assayed. In contrast to the EGF receptor, all EGFR/ErbB receptors show impaired ligand-induced rapid internalization, down-regulation, degradation, and AP-2 association. Also, we have analyzed the heregulin-responsive wild-type ErbB-4 receptor, which does not mediate the rapid internalization of 125I-heregulin, demonstrates no heregulin-regulated receptor degradation, and fails to form association complexes with AP-2. Despite the substantial differences in ligand-induced receptor trafficking between the EGF and ErbB-4 receptors, EGF and heregulin have equivalent capacities to stimulate DNA synthesis in quiescent cells. These results show that the ligand-dependent down-regulation mechanism of the EGF receptor, surprisingly, is not a property of any other known ErbB receptor family member. Since endocytosis is thought to be an attenuation mechanism for growth factor-receptor complexes, these data imply that substantial differences in attenuation mechanisms exist within one family of structurally related receptors.
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Cites
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Self-citationRECEPTORS FOR EPIDERMAL GROWTH FACTOR AND OTHER POLYPEPTIDE MITOGENS
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Self-citationEpidermal Growth Factor and a New Derivative
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Cited by
Untangling the ErbB signalling network
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Nanoparticle-mediated cellular response is size-dependent
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ErbB Receptors: Directing Key Signaling Networks Throughout Life
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The ErbB/HER receptor protein-tyrosine kinases and cancer
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Metadata
- Authors
- Baulida, J., Kraus, M. H., Alimandi, M., Fiore, P. P. D., & Carpenter, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1996-03
- Volume
- 271
- Issue
- 9
- Pages
- 5251-5257
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2028496807
- Cited by
- 454
- References
- 41
- FWCI
- 8.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Baulida, J., Kraus, M. H., Alimandi, M., Fiore, P. P. D., & Carpenter, G. (1996). All ErbB Receptors Other Than the Epidermal Growth Factor Receptor Are Endocytosis Impaired. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.271.9.5251
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