Van Hoewyk Doug
a Coastal Carolina University , Biology Department , Conway , South Carolina , USA.
Plant Signal Behav. 2018 Apr 3;13(4):e1171451. doi: 10.1080/15592324.2016.1171451. Epub 2018 Apr 16.
Stress can impair protein folding in the endoplasmic reticulum (ER). Minimizing the accumulation of misfolded proteins in the ER is achieved by ER-associated degradation (ERAD), which involves the retrograde transport and proteasomal removal of aberrant proteins. Recently, the proteasome has been implicated in a selenium stress response. However, it remains unknown if selenium causes ER stress in plants similar to animals, and if ERAD is associated with optimal selenium tolerance. This deficiency was addressed by monitoring selenate-treated Arabidopsis plants with mutations in HRD1 and SeL1L, participants of ERAD. hrd1a/hrd1b and sel1l mutants treated with selenate demonstrate decreased tolerance and ER stress, as judged by BiP2 accumulation. The data indicate that optimal plant growth during selenate stress requires ERAD.
应激可损害内质网（ER）中的蛋白质折叠。通过内质网相关降解（ERAD）可将内质网中错误折叠蛋白质的积累降至最低，这一过程涉及异常蛋白质的逆向转运和蛋白酶体清除。最近，蛋白酶体与硒应激反应有关。然而，尚不清楚硒是否会像在动物中那样在植物中引发内质网应激，以及ERAD是否与最佳硒耐受性相关。通过监测经硒酸盐处理的内质网相关降解参与者HRD1和SeL1L发生突变的拟南芥植物，解决了这一不足。经硒酸盐处理的hrd1a/hrd1b和sel1l突变体表现出耐受性降低和内质网应激，这通过BiP2积累来判断。数据表明，在硒酸盐胁迫期间植物的最佳生长需要内质网相关降解。
