Autophosphorylation sites on the epidermal growth factor receptor
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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POS phagocytosis induced activation of EGFR (p-EGFR) at tyrosine residue 1068 (Tyr1068).
“First, we observed that POS phagocytosis induced activation of EGFR (p-EGFR), as indicated by phosphorylation of its tyrosine residue 1068 (Tyr1068) (Fig. 6A), a major autophosphorylation site of the receptor.36”
From RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye (2017) · cites this paper as [36]
p-EGFR at Tyr1068 is a major autophosphorylation site of the receptor.
“a major autophosphorylation site of the receptor.36”
From RUBCN/rubicon and EGFR regulate lysosomal degradative processes in the retinal pigment epithelium (RPE) of the eye (2017) · cites this paper as [36]
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Self-citationEvaluation of epidermal growth factor receptors in bladder tumours
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Self-citation
- Authors
- Downward, J., Parker, P., & Waterfield, M. D.
- Venue
- Nature
- Published
- 1984-10
- Volume
- 311
- Issue
- 5985
- Pages
- 483-485
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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