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Autophosphorylation sites on the epidermal growth factor receptor

Downward, J., Parker, P., Waterfield, M. D.·1984·Nature

DOI 10.1038/311483a0

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Abstract

The epidermal growth factor (EGF) receptor is a tyrosine-specific protein kinase with autophosphorylating activity. A 300 amino acid-long region of the receptor's cytoplasmic domain matches (35-90% homology) sequences of transforming proteins from the src family and includes a putative nucleotide binding site. Several of the src transforming proteins have tyrosine kinase activity, but v-erb-B, which appears to be a truncated EGF receptor, is virtually identical to the receptor over this region and yet lacks detectable kinase activity. To locate possible acceptor sites in the v-erb-B protein, we have mapped these sites in the human EGF receptor. We report here that three tyrosine sites near the C-terminus are phosphorylated in vitro. In intact cells, we find that EGF stimulates phosphorylation of several sites, the tyrosine 14 residues from the C-terminus being modified the most extensively. The equivalent site is absent in the v-erb-B protein of avian erythroblastosis virus (AEV) and may influence tyrosine kinase activity.

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Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells
Ullrich, A., Coussens, L. M., Hayflick, J. S., Dull, T. J., Gray, A., Tam, A. W., Lee, J., Yarden, Y., Libermann, T. A., Schlessinger, J., et al. (1984) · Nature · doi:10.1038/309418a0 · Cited by 2,751
Self-citation
Close similarity of epidermal growth factor receptor and v-erb-B oncogene protein sequences
Downward, J., Yarden, Y., Mayes, E., Scrace, G., Totty, N., Stockwell, P., Ullrich, A., Schlessinger, J., & Waterfield, M. D. (1984) · Nature · doi:10.1038/307521a0 · Cited by 2,516
Self-citation
A gas-liquid solid phase peptide and protein sequenator.
Hewick, R. M., Hunkapiller, M. W., Hood, L., & Dreyer, W. J. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43377-7 · Cited by 2,218
CELLULAR ONCOGENES AND RETROVIRUSES
Bishop, J. M. (1983) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.52.070183.001505 · Cited by 1,666
Identification of phosphotyrosine as a product of epidermal growth factor-activated protein kinase in A-431 cell membranes.
Ushiro, H., & Cohen, S. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43497-7 · Cited by 1,184
[42] Detection and quantification of phosphotyrosine in proteins
Cooper, J. A., Sefton, B. M., & Hunter, T. R. (1983) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(83)99075-4 · Cited by 1,109
A native 170,000 epidermal growth factor receptor-kinase complex from shed plasma membrane vesicles.
Cohen, S., Ushiro, H., Stoscheck, C. M., & Chinkers, M. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)68224-4 · Cited by 776
Epidermal growth factor induces rapid tyrosine phosphorylation of proteins in A431 human tumor cells
Hunter, T. R., & Cooper, J. A. (1981) · Cell · doi:10.1016/0092-8674(81)90100-8 · Cited by 670
The erbB gene of avian erythroblastosis virus is a member of the src gene family
Yamamoto, T. S., Nishida, T., Miyajima, N., Kawai, S., Ooi, T., & Toyoshima, K. (1983) · Cell · doi:10.1016/0092-8674(83)90209-x · Cited by 371
Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src).
Smart, J. E., Oppermann, H., Czernilofsky, A. P., Purchio, A. F., Erikson, R. L., & Bishop, J. M. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6013 · Cited by 358

Show all 22 references

Research works printed but not linked: 2

Waterfield, M. D., Scrace, G. & Totty, N. in Practical Protein Biochemistry (ed. Darbre, A.) (Wiley, New York, in the press).
Hunter, T. & Cooper, J. A. UCLA Symp. molec. cell. Biol. 6, 360 (1983).

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Retracted
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Livneh, E., Glazer, L., Segal, D., Schlessinger, J., & Shilo, B. (1985) · Cell · doi:10.1016/0092-8674(85)90208-9 · Cited by 200
Expression of the c‐erbB‐2 protein in normal and transformed cells
Gullick, W. J., Berger, M. S., Bennet, P., Rothbard, J. B., & Waterfield, M. D. (1987) · International Journal of Cancer · doi:10.1002/ijc.2910400221 · Cited by 197
Self-citation
Epidermal growth factor and its receptor
Gill, G. N., Bertics, P. J., & Santon, J. B. (1987) · Molecular and Cellular Endocrinology · doi:10.1016/0303-7207(87)90027-x · Cited by 192
Signal transduction by epidermal growth factor occurs through the subclass of high affinity receptors.
Defize, L. H. K., Boonstra, J., Meisenhelder, J., Kruijer, W., Tertoolen, L. G. J., Tilly, B. C., Hunter, T. R., Henegouwen, P. M. P. V. B. E., Moolenaar, W. H., & de Laat, S. W. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.5.2495 · Cited by 194
Analysis of deletions of the carboxyl terminus of the epidermal growth factor receptor reveals self-phosphorylation at tyrosine 992 and enhanced in vivo tyrosine phosphorylation of cell substrates.
Walton, G. M., Chen, W. S., Rosenfeld, M. G., & Gill, G. N. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)40080-x · Cited by 192
Systems analysis of EGF receptor signaling dynamics with microwestern arrays
Ciaccio, M. F., Wagner, J. P., Chuu, C., Lauffenburger, D. A., & Jones, R. B. (2010) · Nature Methods · doi:10.1038/nmeth.1418 · Cited by 189
Crosstalk Between Epidermal Growth Factor Receptor- and Insulin-Like Growth Factor-1 Receptor Signaling: Implications for Cancer Therapy
van der Veeken, J., Oliveira, S., Schiffelers, R. M., Storm, G., Henegouwen, P. M. P. V. B. E., & Roovers, R. C. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909789271495 · Cited by 190
Evidence that autophosphorylation of solubilized receptors for epidermal growth factor is mediated by intermolecular cross-phosphorylation.
Honegger, A., Kris, R., Ullrich, A., & Schlessinger, J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.3.925 · Cited by 189
Co‐regulation of B‐Myb expression by E2F1 and EGF receptor
Hanada, N., Lo, H., Day, C., Pan, Y., Nakajima, Y., & Hung, M. (2005) · Molecular Carcinogenesis · doi:10.1002/mc.20147 · Cited by 188
EGFR as a clinical marker in glioblastomas and other gliomas
Saadeh, F. S., Mahfouz, R. A., & Assi, H. I. (2017) · The International Journal of Biological Markers · doi:10.5301/ijbm.5000301 · Cited by 190
Hydrogen peroxide preferentially enhances the tyrosine phosphorylation of epidermal growth factor receptor
Gamou, S., & Shimizu, N. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01335-x · Cited by 188
Epidermal growth factor, its receptor, and related proteins
Carpenter, G. F., & Zendegui, J. G. (1986) · Experimental Cell Research · doi:10.1016/0014-4827(86)90449-0 · Cited by 187
E-Cadherin Homophilic Ligation Inhibits Cell Growth and Epidermal Growth Factor Receptor Signaling Independently of Other Cell Interactions
Perrais, M., Chen, X., Perez-Moreno, M., & Gumbiner, B. M. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-04-0348 · Cited by 219
Novel quinazoline-based EGFR kinase inhibitors: A review focussing on SAR and molecular docking studies (2015-2019)
Bhatia, P., Sharma, V., Alam, O., Manaithiya, A., Alam, P., Kahksha, Alam, M. T., & Imran, M. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112640 · Cited by 185
Tyrosine Phosphorylation Mapping of the Epidermal Growth Factor Receptor Signaling Pathway
Steen, H., Küster, B., Fernandez, M. M., Pandey, A., & Mann, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109992200 · Cited by 185
The clinical significance of epidermal growth factor receptor (EGF-R) in human breast cancer: a review on 5232 patients
Klijn, J. G. M. (1992) · Endocrine Reviews · doi:10.1210/er.13.1.3 · Cited by 185
Tyrosine kinase activity is essential for the association of phospholipase C-gamma with the epidermal growth factor receptor.
Margolis, B. L., Bellot, F., Honegger, A., Ullrich, A., Schlessinger, J., & Zilberstein, A. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.2.435 · Cited by 184
Growth factors: The epidermal growth factor receptor gene and its product
Hunter, T. R. (1984) · Nature · doi:10.1038/311414a0 · Cited by 184
The epidermal growth factor receptors and their family of ligands: Their putative role in atherogenesis
Dreux, A. C., Lamb, D. J., Modjtahedi, H., & Ferns, G. A. (2005) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2005.06.038 · Cited by 183
Activated type I phosphatidylinositol kinase is associated with the epidermal growth factor (EGF) receptor following EGF stimulation.
Bjorge, J. D., Chan, T. O., Antczak, M., Kung, H. J., & Fujita, D. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.10.3816 · Cited by 180
Selective Inhibition of Ras, Phosphoinositide 3 Kinase, and Akt Isoforms Increases the Radiosensitivity of Human Carcinoma Cell Lines
Kim, I., Bae, S.-S., Fernandes, A., Wu, J., Muschel, R. J., McKenna, W. G., Birnbaum, M. J., & Bernhard, E. J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0513 · Cited by 179
Structure and Localization of Genes Encoding Aberrant and Normal Epidermal Growth Factor Receptor RNAs from A431 Human Carcinoma Cells
Merlino, G. T., Ishii, S., Whang‐Peng, J., Knutsen, T., Xu, Y. H., Clark, A., Stratton, R. H., Wilson, R. K., Ma, D. P., Roe, B. A., et al. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.7.1722 · Cited by 175
The bovine papillomavirus E5 transforming protein can stimulate the transforming activity of EGF and CSF-1 receptors
Martin, P., Vass, W. C., Schiller, J. T., Lowy, D. R., & Velu, T. J. (1989) · Cell · doi:10.1016/0092-8674(89)90866-0 · Cited by 174
The Epidermal Growth Factor Family
Carpenter, G., & Wahl, M. I. (1990) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-49295-2_4 · Cited by 173
Brain tumors in mice are susceptible to blockade of epidermal growth factor receptor (EGFR) with the oral, specific, EGFR-tyrosine kinase inhibitor ZD1839 (iressa).
Heimberger, A. B., Learn, C. A., Archer, G. E., McLendon, R. E., Chewning, T. A., Tuck, F. L., Pracyk, J. B., Friedman, A. H., Friedman, H. S., Bigner, D. D., et al. (2002) · PubMed · Cited by 169
Epidermal growth factor binding induces a conformational change in the external domain of its receptor.
Greenfield, C., Hiles, I., Waterfield, M. D., Federwisch, M., Wollmer, A., Blundell, T. L., & McDonald, N. Q. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08596.x · Cited by 169
Self-citation
Evaluation of epidermal growth factor receptors in bladder tumours
Berger, M. S., Greenfield, C., Gullick, W., Haley, J. D., Downward, J., Neal, D. E., Harris, A. L., & Waterfield, M. D. (1987) · British Journal of Cancer · doi:10.1038/bjc.1987.238 · Cited by 165
Self-citation

Authors: Downward, J., Parker, P., & Waterfield, M. D.
ORCID: Downward, J.
Parker, P.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1984-10
Volume: 311
Issue: 5985
Pages: 483-485
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/311483a0
OpenAlex: W2056681493
Cited by: 704
References: 22
Citations by year: 2026: 2 · 2025: 7 · 2024: 5 · 2023: 5 · 2022: 11 · 2021: 14 · 2020: 9 · 2019: 9 · 2018: 11 · 2017: 16 · 2016: 15 · 2015: 13 · 2014: 17 · 2013: 18 · 2012: 15
FWCI: 22.58
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Health Sciences › Medicine › Oncology › HER2/EGFR in Cancer Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Pulmonary and Respiratory Medicine › Lung Cancer Treatments and Mutations
Keywords: epidermal growth factor receptor, autophosphorylation, tyrosine kinase, autophosphorylation sites, avian erythroblastosis virus, receptor cytoplasmic domain, kinase activity, transforming protein
MeSH terms: Amino Acid Sequence, Epidermal Growth Factor, Humans, Phosphorylation, Receptors, Cell Surface, Tyrosine, ErbB Receptors

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Autophosphorylation sites on the epidermal growth factor receptor

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