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Molecular Endocrinology Vol. 6, No. 11 1849-1857
doi:10.1210/me.6.11.1849
Copyright © 1992 by the Endocrine Society.
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Molecular Endocrinology, Vol 6, 1849-1857, Copyright © 1992 by Endocrine Society

ARTICLES

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

SJ Theroux, K Stanley, DA Campbell and RJ Davis
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.

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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Copyright © 1992 by The Endocrine Society