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
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
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DOI：
10.1210/me.6.11.1849
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发表时间：
1992-11-01
影响因子：
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通讯作者：
DAVIS, RJ
中科院分区：
文献类型：
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作者：
THEROUX, SJ;STANLEY, K;DAVIS, RJ
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Ser 1046/7。我们以前已经证明，这个磷酸化位点占急性脱敏的EGF-受体观察EGF处理的细胞。在这里，我们表明，这种负调控磷酸化位点的突变去除导致增强EGF-R的信号转导。这种增强作用可以部分地通过阻断EGF刺激的EGF-R下调来解释。这些数据表明，Ser 1046/7磷酸化位点可能具有调节作用，在长期培养的细胞与促有丝分裂浓度的EGF。
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.