Abstract
The epidermal growth factor (EGF) receptor is a tyrosine-specific protein kinase with autophosphorylating activity1–4. A 300 amino acid-long region of the receptor's cytoplasmic domain matches (35–90 % homology) sequences of transforming proteins from the src family5 and includes a putative nucleotide binding site6. Several of the src transforming proteins have tyrosine kinase activity7, 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 activity8,9. 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 activity10,11.
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Downward, J., Parker, P. & Waterfield, M. Autophosphorylation sites on the epidermal growth factor receptor. Nature 311, 483–485 (1984). https://doi.org/10.1038/311483a0
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DOI: https://doi.org/10.1038/311483a0
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