Signal Transduction by the Epidermal Growth Factor Receptor Is Attenuated by a COOH-terminal Domain Serine Phosphorylation Site*
作者： S.J. Theroux , D.A. Latour , K Stanley , D.L. Raden , R.J. Davis
DOI: 10.1016/S0021-9258(18)42048-0
关键词:
摘要: It has been proposed that the acute desensitization of epidermal growth factor receptor (EGF-R) function can be accounted for, in part, by effect EGF to increase phosphorylation at Ser1046/7 (Countaway, J.L., Nairn, A.C., and Davis, R.J. (1992) J. Biol. Chem. 267, 1129-1140). Here, we show mutational removal this site causes an activation EGF-R a potentiation signal transduction. The mechanism results from 1) defective down-regulation when cells are incubated with high concentrations EGF; 2) increased EGF-stimulated tyrosine phosphorylation. is associated alteration apparent specificity independent defect. Together, these data strongly support hypothesis biologically significant regulatory EGF-R.
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