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内质网未折叠蛋白反应的植物传感器。

Plant transducers of the endoplasmic reticulum unfolded protein response.

机构信息

Division of Chemical and Life Sciences and Engineering, King Abdullah University of Science and Technology, Thuwal 23955-6900, Kingdom of Saudi Arabia.

出版信息

Trends Plant Sci. 2012 Dec;17(12):720-7. doi: 10.1016/j.tplants.2012.06.014. Epub 2012 Jul 14.

Abstract

The unfolded protein response (UPR) activates a set of genes to overcome accumulation of unfolded proteins in the endoplasmic reticulum (ER), a condition termed ER stress, and constitutes an essential part of ER protein quality control that ensures efficient maturation of secretory and membrane proteins in eukaryotes. Recent studies on Arabidopsis and rice identified the signaling pathway in which the ER membrane-localized ribonuclease IRE1 (inositol-requiring enzyme 1) catalyzes unconventional cytoplasmic splicing of mRNA, thereby producing the active transcription factor Arabidopsis bZIP60 (basic leucine zipper 60) and its ortholog in rice. Here we review recent findings identifying the molecular components of the plant UPR, including IRE1/bZIP60 and the membrane-bound transcription factors bZIP17 and bZIP28, and implicating its importance in several physiological phenomena such as pathogen response.

摘要

未折叠蛋白反应 (UPR) 激活了一组基因,以克服内质网 (ER) 中未折叠蛋白的积累,这种情况称为 ER 应激,它构成了 ER 蛋白质量控制的重要组成部分,可确保真核生物中分泌蛋白和膜蛋白的有效成熟。最近对拟南芥和水稻的研究鉴定了信号通路,其中 ER 膜定位的核糖核酸酶 IRE1(肌醇需求酶 1)催化 mRNA 的非规范细胞质剪接,从而产生活性转录因子拟南芥 bZIP60(碱性亮氨酸拉链 60)及其在水稻中的同源物。在这里,我们回顾了最近的发现,这些发现确定了植物 UPR 的分子组成部分,包括 IRE1/bZIP60 和膜结合转录因子 bZIP17 和 bZIP28,并表明其在几种生理现象(如病原体反应)中的重要性。

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