SERINE-167 IS THE MAJOR ESTRADIOL-INDUCED PHOSPHORYLATION SITE ON THE HUMAN ESTROGEN-RECEPTOR
SERINE-167 IS THE MAJOR ESTRADIOL-INDUCED PHOSPHORYLATION SITE ON THE HUMAN ESTROGEN-RECEPTOR
复制标题
DOI：
10.1210/me.8.9.1208
复制
发表时间：
1994-09-01
影响因子：
--
通讯作者：
NOTIDES, AC
中科院分区：
文献类型：
--
作者：
ARNOLD, SF;OBOURN, JD;NOTIDES, AC
丝氨酸167已被确定为主要的雌激素诱导的磷酸化位点的人乳腺癌细胞MCF-7的人雌激素受体（hER）。hER在丝氨酸167上的磷酸化是雌激素依赖性的，在MCF-7细胞的雌二醇处理后增加4倍，并且几乎占掺入来自Sf 9昆虫细胞的重组hER和来自MCF-7细胞的天然hER的总[P-32]磷酸的一半。酪蛋白激酶II被发现在体外磷酸化纯化的重组hER丝氨酸167。此外，雌二醇结合增强了2倍的磷酸化纯化的重组人雌激素受体酪蛋白激酶II在体外。蛋白质印迹分析和[P-32]磷酸掺入证实了Sf 9细胞中存在酪蛋白激酶II。这些结果表明，hER是磷酸化丝氨酸167酪蛋白激酶II在一个酶依赖性的方式。
Serine 167 has been identified by radiolabel and amino acid sequencing as the major estrogen-induced phosphorylation site on the human estrogen receptor (hER) from human MCF-7 mammary carcinoma cells. The phosphorylation of the hER on serine 167 was estrogen-dependent, increasing 4-fold upon estradiol treatment of MCF-7 cells and accounted for almost half of the total [P-32]phosphate incorporated into the recombinant hER from Sf9 insect cells and the native hER from MCF-7 cells. Casein kinase II was found to phosphorylate the purified recombinant hER on serine 167 in vitro. In addition, estradiol binding enhanced by 2-fold the phosphorylation of the purified recombinant hER by casein kinase II in vitro. Western blot analysis and [P-32]phosphate incorporation confirmed the presence of casein kinase II in Sf9 cells. These results demonstrate that the hER is phosphorylated on serine 167 by casein kinase II in a hormone-dependent manner.