Autophosphorylation sites on the epidermal growth factor receptor
摘要：
The epidermal growth factor (EGF) receptor is a tyrosine-specific protein kinase with autophosphorylating activity 1–4 . A 300 amino acid-long region of the receptor's cytoplasmic domain matches (35–90 % homology) sequences of transforming proteins from the src family 5 and includes a putative nucleotide binding site 6 . Several of the src transforming proteins have tyrosine kinase activity 7 , 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 8,9 . 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 activity 10,11 .
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关键词：
Humans Tyrosine Receptor, Epidermal Growth Factor Receptors, Cell Surface Phosphorylation Amino Acid Sequence Epidermal Growth Factor
DOI：
10.1038/311483a0
被引量：
年份：
1984
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