Vlasova-St Louis Irina, Bohjanen Paul R
Department of Medicine, University of Minnesota, Minneapolis, MN 55455, USA.
Department of Microbiology, University of Minnesota, Minneapolis, MN 55455, USA.
Cells. 2016 Jan 25;5(1):4. doi: 10.3390/cells5010004.
In response to environmental signals, kinases phosphorylate numerous proteins, including RNA-binding proteins such as the AU-rich element (ARE) binding proteins, and the GU-rich element (GRE) binding proteins. Posttranslational modifications of these proteins lead to a significant changes in the abundance of target mRNAs, and affect gene expression during cellular activation, proliferation, and stress responses. In this review, we summarize the effect of phosphorylation on the function of ARE-binding proteins ZFP36 and ELAVL1 and the GRE-binding protein CELF1. The networks of target mRNAs that these proteins bind and regulate include transcripts encoding kinases and kinase signaling pathways (KSP) components. Thus, kinase signaling pathways are involved in feedback regulation, whereby kinases regulate RNA-binding proteins that subsequently regulate mRNA stability of ARE- or GRE-containing transcripts that encode components of KSP.
作为对环境信号的响应,激酶会使众多蛋白质发生磷酸化,其中包括富含AU元件(ARE)结合蛋白和富含GU元件(GRE)结合蛋白等RNA结合蛋白。这些蛋白质的翻译后修饰会导致靶mRNA丰度发生显著变化,并在细胞激活、增殖和应激反应过程中影响基因表达。在本综述中,我们总结了磷酸化对ARE结合蛋白ZFP36和ELAVL1以及GRE结合蛋白CELF1功能的影响。这些蛋白质结合并调控的靶mRNA网络包括编码激酶和激酶信号通路(KSP)组分的转录本。因此,激酶信号通路参与反馈调节,即激酶调节RNA结合蛋白,而这些RNA结合蛋白随后调节编码KSP组分的含ARE或GRE转录本的mRNA稳定性。