Theroux S J, Stanley K, Campbell D A, Davis R J
Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, University of Massachusetts Medical School, Worcester 01605.
Mol Endocrinol. 1992 Nov;6(11):1849-57. doi: 10.1210/mend.6.11.1480174.
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.
表皮生长因子受体（EGF-R）丝氨酸磷酸化的主要位点位于受体的COOH末端结构域内的Ser1046/7处。我们之前已经证明，该磷酸化位点是EGF处理的细胞中观察到的EGF-R急性脱敏的原因。在此我们表明，通过突变去除这个负性调节磷酸化位点会导致EGF-R信号转导增强。这种增强部分可归因于EGF刺激的EGF-R下调受阻。这些数据表明，在有丝分裂原浓度的EGF长期培养细胞的过程中，SER1046/7磷酸化位点可能具有调节作用。
