Cellular response to unfolded proteins in the endoplasmic reticulum of plants
Cellular response to unfolded proteins in the endoplasmic reticulum of plants
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DOI：
10.1111/j.1742-4658.2007.05664.x
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发表时间：
2007-03
期刊：
影响因子：
--
通讯作者：
R. Urade
中科院分区：
文献类型：
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作者：
R. Urade
分泌和跨膜蛋白在真核细胞的内质网（ER）中合成。在粗糙ER上翻译的新生多肽链易位到ER腔并折叠成其天然构象。当蛋白质折叠由于异源寡聚蛋白亚基的突变或不平衡比率而受到抑制时，未折叠或错误折叠的蛋白质在称为ER应激的事件中在ER中积累。由于ER应激经常干扰正常的细胞功能，信号转导途径被激活以试图维持ER的稳态。这些途径统称为未折叠蛋白反应（UPR）。在过去的二十年里，我们对酵母和哺乳动物中UPR的分子机制的理解有了很大的进展。在植物中，类似于酵母和哺乳动物中的UPR已经被认识到，并且最近引起了相当大的关注。本综述将总结植物普遍定期审议的最新进展，并强调尚未解决的剩余问题。
Secretory and transmembrane proteins are synthesized in the endoplasmic reticulum (ER) in eukaryotic cells. Nascent polypeptide chains, which are translated on the rough ER, are translocated to the ER lumen and folded into their native conformation. When protein folding is inhibited because of mutations or unbalanced ratios of subunits of hetero‐oligomeric proteins, unfolded or misfolded proteins accumulate in the ER in an event called ER stress. As ER stress often disturbs normal cellular functions, signal‐transduction pathways are activated in an attempt to maintain the homeostasis of the ER. These pathways are collectively referred to as the unfolded protein response (UPR). There have been great advances in our understanding of the molecular mechanisms underlying the UPR in yeast and mammals over the past two decades. In plants, a UPR analogous to those in yeast and mammals has been recognized and has recently attracted considerable attention. This review will summarize recent advances in the plant UPR and highlight the remaining questions that have yet to be addressed.