State Key Laboratory of Plant Physiology and Biochemistry, Department of Plant Sciences, College of Biological Sciences, China Agricultural University, Beijing, China.
Plant Signal Behav. 2011 Jan;6(1):77-9. doi: 10.4161/psb.6.1.14019. Epub 2011 Jan 1.
Accumulation of unfolded protein or misfolded protein causes endoplasmic reticulum (ER) stress. Increased salt concentration activates a stress response pathway in the ER in Arabidopsis thaliana to induce the expression of several salt stress response genes, leading to a more optimal protein folding environment in the ER. In addition, some salt stress-regulated proteins require zinc for their activity, including some zinc-dependent DNA binding proteins and zinc-finger proteins. In a recent study, we reported that ZTP29, a putative zinc transporter at the ER membrane, is involved in the response to salt stress through regulation of zinc level in the ER to induce the UPR pathway. In this addendum, we propose a testable hypothesis for the role of ZTP29 in the response to salt stress via the regulation of zinc levels in the ER.
未折叠蛋白或错误折叠蛋白的积累会导致内质网（ER）应激。在拟南芥中，盐浓度的增加会激活 ER 中的应激反应途径，诱导几种盐应激反应基因的表达，从而在 ER 中形成更适合蛋白质折叠的环境。此外，一些盐胁迫调节蛋白的活性需要锌，包括一些锌依赖性 DNA 结合蛋白和锌指蛋白。在最近的一项研究中，我们报道了内质网膜上的假定锌转运蛋白 ZTP29 通过调节 ER 中的锌水平诱导 UPR 途径，参与对盐胁迫的反应。在本增补中，我们提出了一个可测试的假设，即 ZTP29 通过调节 ER 中的锌水平在盐胁迫反应中的作用。
