Title

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

UMMS Affiliation

Howard Hughes Medical Institute, Program in Molecular Medicine

Publication Date

11-1-1992

Document Type

Article

Subjects

Allosteric Regulation; Animals; CHO Cells; Cell Division; Cricetinae; Down-Regulation; Mutagenesis; Phosphorylation; *Phosphoserine; *Protein Processing, Post-Translational; *Signal Transduction

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

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.

Rights and Permissions

Citation: Mol Endocrinol. 1992 Nov;6(11):1849-57.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Molecular endocrinology (Baltimore, Md.)

PubMed ID

1480174