Incorporation of the Endoplasmic Reticulum Stress-Induced Spliced Form of XBP1 mRNA in the Exosomes.
Incorporation of the Endoplasmic Reticulum Stress-Induced Spliced Form of XBP1 mRNA in the Exosomes.
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DOI：
10.3389/fphys.2018.01357
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发表时间：
2018
影响因子：
4
通讯作者：
Ozawa K
中科院分区：
文献类型：
--
作者：
Hosoi T;Nakashima M;Ozawa K
众所周知，内质网(ER)和细胞核之间相互通信以应对内质网应激。然而，内质网应激的细胞外传导机制尚不清楚。当内质网应激诱导的未折叠蛋白反应(UPR)被激活时，X盒结合蛋白1(XBP1mRNA)被肌醇需要酶-1α(IRE1α)剪接，产生剪接形式的XBP1sXBP1。在本研究中，我们发现细胞中的sXBP1 mRNA可能被整合到外切体中，并被释放到细胞外。我们发现在MIN6小鼠胰腺β细胞外体中sXBP1m RNA水平与未剪接XBP1m RNA水平的比值高于细胞。在HEK293T细胞中过表达IRE1α诱导XBP1DNA剪接时，也观察到类似的效应。这些结果表明，将sXBP1掺入外体是UPR传递到细胞外的一种新机制，这种机制可能在细胞暴露于应激时被触发。
It is known that endoplasmic reticulum (ER) and nucleus communicate with each other to cope with ER stress. However, the mechanisms through which extracellular transmission of ER stress occurs remain unexplored. When the ER stress-induced unfolded protein response (UPR) is activated, the X-box binding protein 1 (XBP1) mRNA is spliced by inositol-requiring enzyme-1α (IRE1α) to produce the spliced form of XBP1 (sXBP1). In the present study, we found that sXBP1 mRNA in the cell may be incorporated into the exosomes and was released extracellularly. We found that the ratio of the mRNA levels of sXBP1 to unspliced XBP1 (uXBP1) in the exosome was higher than that of cells in MIN6 mouse pancreatic β cells. A similar effect was observed when XBP1 splicing was induced by overexpressing IRE1α in HEK293T cells. These results suggest that the incorporation of sXBP1 into the exosomes is a novel mechanism of UPR transmitted to extracellularly, which would be triggered when cells are exposed to stress.
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