The Endoplasmic Reticulum Role in the Plant Response to Abiotic Stress.
The Endoplasmic Reticulum Role in the Plant Response to Abiotic Stress.
复制标题
内质网在植物对非生物胁迫反应中的作用。
DOI：
10.3389/fpls.2021.755447
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发表时间：
2021
影响因子：
5.6
通讯作者：
Moreno AA
中科院分区：
文献类型：
--
作者：
Reyes-Impellizzeri S;Moreno AA
内质网（ER）是细胞中三分之一的蛋白质合成的细胞器。这些蛋白质中的一些参与细胞、组织或有机体对环境的信号传导和反应。为了确保这些蛋白质的正确合成和折叠，或处理未折叠或错误折叠的蛋白质，内质网具有不同的相互作用和调节机制。这些机制被称为内质网质量控制（ERQC），内质网相关降解（ERAD）和未折叠蛋白反应（UPR），它们都是维持内质网蛋白稳态或蛋白质稳态的三个参与者。考虑到这些内质网机制的客户蛋白在植物对环境的反应中的重要性，预计其成分的变化或改变会影响植物对环境线索或胁迫的反应。本文主要综述了ERQC、ERAD和UPR基因在植物对干旱、高温、渗透、盐和辐照等非生物胁迫响应中的作用。此外，我们总结了最近出版物的发现，寻找这些过程与其可能的客户蛋白之间的联系。由此，我们观察到ERAD和UPR机制之间已经建立了明确的联系，但是将ERQC成分与这两个过程或其可能的客户蛋白联系起来的证据仍然缺乏。作为一项建议，我们建议使用蛋白质组学方法来揭示这些蛋白质的身份及其与内质网蛋白停滞的联系。
The endoplasmic reticulum (ER) is the organelle where one third of the proteins of a cell are synthetized. Several of these proteins participate in the signaling and response of cells, tissues, or from the organism to the environment. To secure the proper synthesis and folding of these proteins, or the disposal of unfolded or misfolded proteins, the ER has different mechanisms that interact and regulate each other. These mechanisms are known as the ER quality control (ERQC), ER-associated degradation (ERAD) and the unfolded protein response (UPR), all three participants of the maintenance of ER protein homeostasis or proteostasis. Given the importance of the client proteins of these ER mechanisms in the plant response to the environment, it is expected that changes or alterations on their components have an impact on the plant response to environmental cues or stresses. In this mini review, we focus on the impact of the alteration of components of ERQC, ERAD and UPR in the plant response to abiotic stresses such as drought, heat, osmotic, salt and irradiation. Also, we summarize findings from recent publications looking for a connection between these processes and their possible client(s) proteins. From this, we observed that a clear connection has been established between the ERAD and UPR mechanisms, but evidence that connects ERQC components to these both processes or their possible client(s) proteins is still lacking. As a proposal, we suggest the use of proteomics approaches to uncover the identity of these proteins and their connection with ER proteostasis.
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