Mutational removal of the major site of serine phosphorylation of the epidermal growth factor receptor causes potentiation of signal transduction: role of receptor down-regulation
Howard Hughes Medical Institute, Program in Molecular Medicine
Allosteric Regulation; Animals; CHO Cells; Cell Division; Cricetinae; Down-Regulation; Mutagenesis; Phosphorylation; *Phosphoserine; *Protein Processing, Post-Translational; *Signal Transduction
Life Sciences | Medicine and Health Sciences
The major site of epidermal growth factor receptor (EGF-R) serine phosphorylation is located within the COOH-terminal domain of the receptor at Ser1046/7. We have previously demonstrated that this phosphorylation site accounts for the acute desensitization of the EGF-R observed in EGF-treated cells. Here we show that the mutational removal of this negative regulatory phosphorylation site causes potentiation of signal transduction by the EGF-R. This potentiation can be accounted for in part by a block in the EGF-stimulated down-regulation of the EGF-R. These data indicate that the SER1046/7 phosphorylation site may have a regulatory role during long term incubation of cells with mitogenic concentrations of EGF.
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Citation: Mol Endocrinol. 1992 Nov;6(11):1849-57.
Molecular endocrinology (Baltimore, Md.)
Theroux, Steven J.; Stanley, Krista; Campbell, Debra A.; and Davis, Roger J., "Mutational removal of the major site of serine phosphorylation of the epidermal growth factor receptor causes potentiation of signal transduction: role of receptor down-regulation" (1992). Open Access Articles. 1470.