Autophosphorylation Sites on the Epidermal Growth Factor Receptor

Nature. 1984 Oct 4-10;311(5985):483-5. doi: 10.1038/311483a0.

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.

MeSH terms

  • Amino Acid Sequence
  • Epidermal Growth Factor / physiology*
  • ErbB Receptors
  • Humans
  • Phosphorylation
  • Receptors, Cell Surface / metabolism*
  • Tyrosine / metabolism

Substances

  • Receptors, Cell Surface
  • Tyrosine
  • Epidermal Growth Factor
  • ErbB Receptors