Evolution of the unfolded protein response
Evolution of the unfolded protein response
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DOI：
10.1016/j.bbamcr.2013.01.016
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发表时间：
2013-11-01
影响因子：
5.1
通讯作者：
Hollien, Julie
中科院分区：
文献类型：
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作者：
Hollien, Julie
未折叠蛋白反应 (UPR) 是响应内质网 (ER) 应激的信号通路网络。 UPR 的一般输出是上调参与 ER 功能的基因，从而恢复和/或增加 ER 折叠和加工蛋白质的能力。与此同时，许多生物体具有通过减弱翻译或降解内质网靶向 mRNA 来限制内质网负荷的机制。尽管这些信号通路在真核生物中广泛保守，但有趣的变化表明了管理内质网应激的多种机制。当早期分化的原生动物缺乏传统的转录调控时，它们如何应对压力？内质网应激传感器 Ire1 在缺少其主要目标的真菌物种中发挥什么作用？在这里，我描述了不同物种如何优化 UPR 以满足其需求。本文是题为“内质网功能和结构多样性”的特刊的一部分。 (c) 2013 Elsevier B.V. 保留所有权利。
The unfolded protein response (UPR) is a network of signaling pathways that responds to stress in the endoplasmic reticulum (ER). The general output of the UPR is to upregulate genes involved in ER function, thus restoring and/or increasing the capacity of the ER to fold and process proteins. In parallel, many organisms have mechanisms for limiting the load on the ER by attenuating translation or degrading ER-targeted mRNAs. Despite broad conservation of these signaling pathways across eukaryotes, interesting variations demonstrate a variety of mechanisms for managing ER stress. How do early-diverging protozoa respond to stress when they lack traditional transcriptional regulation? What is the role of the ER stress sensor Ire1 in fungal species that are missing its main target? Here I describe how diverse species have optimized the UPR to fit their needs. This article is part of a Special Issue entitled: Functional and structural diversity of endoplasmic reticulum. (c) 2013 Elsevier B.V. All rights reserved.