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
UMass Chan AffiliationsHoward Hughes Medical Institute, Program in Molecular Medicine
*Protein Processing, Post-Translational
Medicine and Health Sciences
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AbstractThe 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.
Mol Endocrinol. 1992 Nov;6(11):1849-57.
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/38607