Poly(A)+ mRNA-binding protein Tudor-SN regulates stress granules aggregation dynamics
Poly(A)+ mRNA-binding protein Tudor-SN regulates stress granules aggregation dynamics
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Poly(A)( ) mRNA 结合蛋白 Tudor-SN 调节应激颗粒聚集动态
DOI：
10.1111/febs.13186
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发表时间：
2015-03-01
期刊：
影响因子：
5.4
通讯作者：
Yang, Jie
中科院分区：
文献类型：
--
作者：
Gao, Xingjie;Fu, Xue;Yang, Jie
应激颗粒（SG）和加工体（PB）构成了应激期间细胞质RNA焦点的主要类型。我们以前的数据表明，敲低人Tudor葡萄球菌核酸酶（Tudor-SN）影响SG的聚集。然而，精确的分子机制尚未完全确定。在本研究中，我们证明了Tudor-SN与SG的许多核心组分结合并共定位，如poly（A）（+）mRNA结合蛋白1、T细胞内部抗原-1相关蛋白和poly（A）（+）mRNA，以及SG/PB共享蛋白Argonaute 1/2，但不与PB核心蛋白结合并共定位，如脱帽酶1 a/B，从而证实了Tudor-SN是SG特异性蛋白。我们还表明，Tudor-SN颗粒积极沟通的核和胞质池在应力条件下。Tudor-SN可以调节含有poly（A）（+）mRNA的SG的聚集动力学，并在细胞应激期间选择性地稳定SG相关的mRNA。
Stress granules (SGs) and processing bodies (PBs) comprise the main types of cytoplasmic RNA foci during stress. Our previous data indicate that knockdown of human Tudor staphylococcal nuclease (Tudor-SN) affects the aggregation of SGs. However, the precise molecular mechanism has not been determined fully. In the present study, we demonstrate that Tudor-SN binds and colocalizes with many core components of SGs, such as poly(A)(+) mRNA binding protein 1, T-cell internal antigen-1-related protein and poly(A)(+) mRNA, and SG/PB sharing proteins Argonaute 1/2, but not PB core proteins, such as decapping enzyme 1 a/b, confirming that Tudor-SN is an SG-specific protein. We also demonstrate that the Tudor-SN granule actively communicates with the nuclear and cytosolic pool under stress conditions. Tudor-SN can regulate the aggregation dynamics of poly(A)(+) mRNA-containing SGs and selectively stabilize the SG-associated mRNA during cellular stress.