Ontology type: schema:ScholarlyArticle
1984-10
AUTHORSJ Downward, P Parker, M D Waterfield
ABSTRACTThe 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. More... »
PAGES483-485
http://scigraph.springernature.com/pub.10.1038/311483a0
DOIhttp://dx.doi.org/10.1038/311483a0
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/6090945
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