Chaperones and foldases in endoplasmic reticulum stress signaling in plants
Chaperones and foldases in endoplasmic reticulum stress signaling in plants
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DOI：
10.4161/psb.6.2.15490
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发表时间：
2011-01-01
影响因子：
2.9
通讯作者：
Tuteja, Narendra
中科院分区：
文献类型：
--
作者：
Gupta, Dinesh;Tuteja, Narendra
分子伴侣和折叠酶是一组不同的蛋白质，它们在体内与错误折叠或未折叠的蛋白质（非天然或不稳定蛋白质）结合，并在其正确折叠中发挥重要作用。应激条件迫使内质网 (ER) 中的伴侣和折叠酶表达活性发生改变和增强，这突出了这些蛋白质的作用，因此这些类别下的一些蛋白质被鉴定为热休克蛋白。不同的伴侣和折叠酶在不同的细胞区室中活跃，执行特定的任务。该综述将讨论内质网伴侣和折叠酶在胁迫条件下的作用，以维持植物细胞中适当的蛋白质折叠动力学，以及该领域的最新进展。文章中描述的 ER 伴侣和折叠酶是结合蛋白 (BiP)、葡萄糖调节蛋白 (GRP94)、蛋白二硫键异构酶 (PDI)、肽基脯氨酰异构酶 (PPI) 或亲免素、钙联蛋白和钙网蛋白。
Molecular chaperones and foldases are a diverse group of proteins that in vivo bind to misfolded or unfolded proteins (non-native or unstable proteins) and play important role in their proper folding. Stress conditions compel altered and heightened chaperone and foldase expression activity in the endoplasmic reticulum (ER), which highlights the role of these proteins, due to which several of the proteins under these classes were identified as heat shock proteins. Different chaperones and foldases are active in different cellular compartment performing specific tasks. The review will discuss the role of ER chaperones and foldases under stress conditions, to maintain proper protein folding dynamics in the plant cells and recent advances in the field. The ER chaperones and foldases, which are described in article, are binding protein (BiP), glucose regulated protein (GRP94), proteindisulfide isomerase (PDI), peptidyl-prolyl isomerases (PPI) or immunophilins, calnexin and calreticulin.