All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor.
作者： B L Margolis , I Lax , R Kris , M Dombalagian , A M Honegger
DOI: 10.1016/S0021-9258(18)81674-X
关键词:
摘要: Activation of the epidermal growth factor (EGF) receptor kinase leads to autophosphorylation and phosphorylation various cellular substrates. The three known sites EGF are located at carboxyl-terminal tail where they probably act compete with thus modulate substrate phosphorylation. Mutational analysis micro-sequencing techniques have been used localize identify new site(s) receptor. We compared phosphopeptide maps human receptor, two deletion mutants lacking 63 126 amino acids from HER/neu a chimeric containing HER2/neu. HER2/neu is highly homologous it functions as for yet unidentified factor. On basis this analysis, we concluded that all HER2/new in their tails. Utilizing receptors deletions, were also able tyr1086 an additional site Direct microsequencing phosphorylated tryptic peptide confirmed assignment.
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