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Cited by 454

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 access
Baulida, Josep, Kraus, Matthias H., Alimandi, Maurizio, Fiore, Pier Paolo Di, Carpenter, Graham·1996·Journal of Biological Chemistry

Abstract

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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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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CoChat. (2026). Citation check: All ErbB Receptors Other Than the Epidermal Growth Factor Receptor Are Endocytosis Impaired. https://app.cochat.ai/papers/10.1074/jbc.271.9.5251
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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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