OsDER1 Is an ER-Associated Protein Degradation Factor That Responds to ER Stress
OsDER1 Is an ER-Associated Protein Degradation Factor That Responds to ER Stress
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OsDER1 是一种与 ER 相关的蛋白质降解因子，可响应 ER 应激
DOI：
10.1104/pp.18.00375
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发表时间：
2018
期刊：
影响因子：
7.4
通讯作者：
Qu Le Qing
中科院分区：
文献类型：
--
作者：
Qian D;an;Chen Guoqiang;Tian Lihong;Qu Le Qing
内质网相关蛋白降解（ERAD）在内质网（ER）质量控制中起着重要作用。到目前为止，很少有人知道在植物ERAD途径中的逆易位机制。我们获得了一个ERLIN样蛋白（OsDER 1）通过SWATH为基础的定量蛋白质组学分析ER膜蛋白提取的ER胁迫水稻（Oryza sativa）种子。OsDER1是酵母和哺乳动物DER1的同源物，定位于ER中，并在ER应激下显著积累。OsDER 1在水稻中的过表达或抑制导致未折叠蛋白反应的激活和对内质网应激的超敏反应，并且抑制导致面粉状、皱缩的种子。此外，OsDER 1过表达或抑制转基因水稻中多聚泛素化蛋白的表达量显著增加。免疫共沉淀实验表明OsDER1与经典ERAD途径的重要组分OsHRD 1、OsHRD 3和OsCDC 48相互作用。此外，OsDER1与信号肽肽酶，最近在酵母和哺乳动物中发现的替代ERAD途径的一个组成部分的同源物。我们的数据表明OsDER1与ERAD通路有关。
Endoplasmic reticulum-associated protein degradation (ERAD) plays an important role in endoplasmic reticulum (ER) quality control. To date, little is known about the retrotranslocation machinery in the plant ERAD pathway. We obtained a DERLIN-like protein (OsDER1) through a SWATH-based quantitative proteomic analysis of ER membrane proteins extracted from ER-stressed rice (Oryza sativa) seeds. OsDER1, a homolog of yeast and mammal DER1, is localized in the ER and accumulates significantly under ER stress. Overexpression or suppression of OsDER1 in rice leads to activation of the unfolded protein response and hypersensitivity to ER stress, and suppression results in floury, shrunken seeds. In addition, the expression levels of polyubiquitinated proteins increased markedly inOsDER1overexpression or suppression transgenic rice. Coimmunoprecipitation experiments demonstrated that OsDER1 interacted with OsHRD1, OsHRD3, and OsCDC48, the essential components of the canonical ERAD pathway. Furthermore, OsDER1 associated with the signal peptide peptidase, a homolog of a component of the alternative ERAD pathway identified recently in yeast and mammals. Our data suggest that OsDER1 is linked to the ERAD pathway.