未折叠蛋白反应在植物病毒感染中的作用。
Role of unfolded protein response in plant virus infection.
机构信息
Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK, USA.
出版信息
Plant Signal Behav. 2011 Aug;6(8):1212-5. doi: 10.4161/psb.6.8.16048. Epub 2011 Aug 1.
Abstract
A new study of Potato virus X (PVX) revealed that a viral movement protein, named TGBp3, triggers the unfolded protein response (UPR) which monitors accumulation of aberrant proteins the endoplasmic reticulum (ER) and targets them for degradation. The PVX TGBp3 resides in ER and activates bZIP60, a transcription factor involved in the UPR pathway. Knockdown of bZIP60 hampers virus infection in protoplasts and whole plants. Preliminary evidence indicates that UPR regulates cellular cytotoxicity that could otherwise lead to cell death if the PVX TGBp3 reaches high levels in the ER. SKP1 expression appears to be linked to bZIP60 and is a component of the SCF-complex mediating proteasomal degradation of cellular substrates. SKP1 expression is induced by PVX TGBp3 and plays a role in regulating PVX spread in whole plants. We propose that SKP1 might be linked to TGBp1-mediated degradation of AGO1.
摘要
一项关于马铃薯 X 病毒（PVX）的新研究表明，一种名为 TGBp3 的病毒运动蛋白触发未折叠蛋白反应（UPR），该反应监测内质网（ER）中异常蛋白的积累，并将其靶向降解。PVX TGBp3 位于 ER 中，并激活 bZIP60，这是一种参与 UPR 途径的转录因子。bZIP60 的敲低会阻碍质体和整个植物中的病毒感染。初步证据表明，UPR 调节细胞毒性，如果 PVX TGBp3 在 ER 中达到高水平，这种毒性可能导致细胞死亡。SKP1 的表达似乎与 bZIP60 相关，并且是介导细胞底物蛋白酶体降解的 SCF 复合物的一个组成部分。PVX TGBp3 诱导 SKP1 的表达，并在调节整个植物中 PVX 的传播中发挥作用。我们提出 SKP1 可能与 TGBp1 介导的 AGO1 降解有关。
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