Aggregation of SND1 in Stress Granules is Associated with the Microtubule Cytoskeleton During Heat Shock Stimulus.

Aggregation of SND1 in Stress Granules is Associated with the Microtubule Cytoskeleton During Heat Shock Stimulus.
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应激颗粒中 SND1 的聚集与热休克刺激期间的微管细胞骨架相关。

DOI:
10.1002/ar.23642
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发表时间:
2017-12
期刊:
Anatomical record (Hoboken, N.J. : 2007)
影响因子:
--
通讯作者:
Gao X
Gao X
中科院分区:
其他
文献类型:
--
作者:
Shao J;Gao F;Zhang B;Zhao M;Zhou Y;He J;Ren L;Yao Z;Yang J;Su C;Gao X

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应激颗粒是细胞质中的一种动态致密结构,在各种环境应激刺激下形成。葡萄球菌核酸酶和Tudor结构域1(SND 1)是一种RNA结合蛋白,已被鉴定为转录共激活因子。我们以前的研究表明,SND 1是应激颗粒的一个组成部分,在应激条件下形成。在这里,我们观察到SND 1颗粒在45°C处理的HeLa细胞中在15 min时通常被微管蛋白微管包围,或者在30或45 min时与微管共定位。此外,诺考达唑介导的微管解聚可以显著影响SND 1蛋白在热休克应激期间向SG的有效募集。此外,45°C热休克介导了eIF 2 α磷酸化的增强,这不受诺考达唑(一种破坏细胞骨架的药物)处理的影响。完整的微管细胞骨架轨道对于SND 1颗粒在热休克应激下的有效组装是重要的,并且可以促进SND 1在细胞质RNA焦点之间穿梭。Anat Rec,300:2192-2199,2017。© 2017 The Authors The Anatomical Record由Wiley Periodicals,Inc.出版。代表美国解剖学家协会
Stress granules (SGs) are dynamic dense structures in the cytoplasm that form in response to a variety of environmental stress stimuli. Staphylococcal nuclease and Tudor domain containing 1 (SND1) is a type of RNA‐binding protein and has been identified as a transcriptional co‐activator. Our previous studies have shown that SND1 is a component of the stress granule, which forms under stress conditions. Here, we observed that SND1 granules were often surrounded by ɑ‐tubulin‐microtubules in 45°C‐treated HeLa cells at 15 min or colocalized with microtubules at 30 or 45 min. Furthermore, Nocodazole‐mediated microtubule depolymerization could significantly affect the efficient recruitment of SND1 proteins to the SGs during heat shock stress. In addition, the 45°C heat shock mediated the enhancement of eIF2α phosphorylation, which was not affected by treatment with Nocodazole, an agent that disrupts the cytoskeleton. The intact microtubule cytoskeletal tracks are important for the efficient assembly of SND1 granules under heat shock stress and may facilitate SND1 shuttling between cytoplasmic RNA foci. Anat Rec, 300:2192–2199, 2017. © 2017 The Authors The Anatomical Record published by Wiley Periodicals, Inc. on behalf of American Association of Anatomists.
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