Phosphorylation of Ser(211) in the chicken progesterone receptor modulates its transcriptional activity
Phosphorylation of Ser(211) in the chicken progesterone receptor modulates its transcriptional activity
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DOI：
10.1074/jbc.271.22.12801
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发表时间：
1996-05-31
影响因子：
4.8
通讯作者：
Weigel, NL
中科院分区：
文献类型：
--
作者：
Bai, WL;Weigel, NL
鸡孕酮受体已被证明是在体内磷酸化的四个主要网站。先前的研究已经表明，在配体受限的条件下，将丝氨酸依赖性磷酸化位点之一Ser（530）突变为丙氨酸会降低受体的转录活性。在这里，我们提出了另一个磷酸化位点Ser（211）的功能意义的证据。Set-211突变为丙氨酸导致受体转录活性降低，并影响SDS-聚丙烯酰胺凝胶电泳中受体迁移率的磷酸化依赖性降低。转录活性的降低程度取决于研究中使用的细胞类型和报告基因，但与激素浓度无关，表明Ser（211）磷酸化通过与Ser（530）磷酸化不同的机制调节受体活性。
The chicken progesterone receptor has been shown to be phosphorylated in vivo at four major sites. Previous studies have shown that mutation of one of the hormone-dependent phosphorylation sites, Ser(530), to alanine decreases the transcriptional activity of the receptor under conditions where ligand is limited. Here, we present evidence for the functional significance of another phosphorylation site, Ser(211). Mutation of Set-211 to alanine results in a decrease in the transcriptional activity of the receptor and affects the phosphorylation-dependent decrease in mobility of the receptor in SDS-polyacrylamide gel electrophoresis. The degree of reduction in transcriptional activity is dependent on both the cell type and the reporters used in the studies but is independent of hormone concentration, suggesting that phosphorylation at Ser(211) regulates the activity of the receptor through a mechanism distinct from Ser(530) phosphorylation.