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.
DOI of Published Version
Mol Endocrinol. 1992 Nov;6(11):1849-57.
Molecular endocrinology (Baltimore, Md.)
Theroux SJ, Stanley K, Campbell DA, Davis RJ. (1992). 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. Open Access Publications by UMass Chan Authors. https://doi.org/10.1210/mend.6.11.1480174. Retrieved from https://escholarship.umassmed.edu/oapubs/1470