ATF-1的磷酸化增强了其与DNA的结合以及钠钾ATP酶α1亚基基因启动子的转录。
Phosphorylation of ATF-1 enhances its DNA binding and transcription of the Na,K-ATPase alpha 1 subunit gene promoter.
作者信息
Kobayashi M, Shimomura A, Hagiwara M, Kawakami K
机构信息
Department of Biology, Jichi Medical School, Tochigi, Japan.
出版信息
Nucleic Acids Res. 1997 Feb 15;25(4):877-82. doi: 10.1093/nar/25.4.877.
Abstract
Transcriptional activity of both ATF-1 and CREB is enhanced by protein phosphorylation. While enhancement has been attributed to an increase in binding affinity for a co-activator (CBP), induction of the DNA binding activity by phosphorylation is an open question. Using the Na,K-ATPase alpha1 subunit gene promoter, which has an asymmetrical ATF/CRE site, we analyzed the effect of phosphorylation on DNA binding activity of the ATF-1-CREB heterodimer. Dephosphorylation of the heterodimer in nuclear extracts reduced binding to the ATF/CRE site. Phosphorylation of ATF-1 at Ser63 enhanced its binding to the ATF/CRE site in both the homodimeric and heterodimeric forms. Transcription of the Na,K-ATPase alpha 1 subunit gene promoter was also stimulated by phosphorylated ATF-1 in vitro.
摘要
ATF-1和CREB的转录活性均通过蛋白质磷酸化得到增强。虽然这种增强归因于与共激活因子（CBP）结合亲和力的增加，但磷酸化诱导DNA结合活性仍是一个悬而未决的问题。利用具有不对称ATF/CRE位点的Na,K-ATP酶α1亚基基因启动子，我们分析了磷酸化对ATF-1-CREB异二聚体DNA结合活性的影响。核提取物中异二聚体的去磷酸化降低了其与ATF/CRE位点的结合。ATF-1的Ser63位点磷酸化增强了其在同二聚体和异二聚体形式下与ATF/CRE位点的结合。体外实验中，磷酸化的ATF-1也刺激了Na,K-ATP酶α1亚基基因启动子的转录。
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