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Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus

机译：分泌途径的质量控制：错误折叠的病毒膜糖蛋白的保留涉及内质网，中隔室和高尔基体之间的循环

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Proteins synthesized in the ER are generally transported to the Golgi complex and beyond only when they have reached a fully folded and assembled conformation. To analyze how the selective retention of misfolded proteins works, we monitored the long-term fate of a membrane glycoprotein with a temperature-dependent folding defect, the G protein of tsO45 vesicular stomatitis virus. We used indirect immunofluorescence, immunoelectron microscopy, and a novel Nycodenz gradient centrifugation procedure for separating the ER, the intermediate compartment, and the Golgi complex. We also employed the folding and recycling inhibitors dithiothreitol and AIF4-, and coimmunoprecipitation with calnexin antibodies. The results showed that the misfolded G protein is not retained in the ER alone; it can move to the intermediate compartment and to the cis-Golgi network but is then recycled back to the ER. In the ER it is associated with calnexin and BiP/GRP78. Of these two chaperones, only BiP/GRP78 seems to accompany it through the recycling circuit. Thus, the retention of this misfolded glycoprotein is the result of multiple mechanisms including calnexin binding in the ER and selective retrieval from the intermediate compartment and the cis-Golgi network.
机译：在ER中合成的蛋白质通常仅在达到完全折叠和组装的构象后才转运到高尔基复合体中。为了分析错折叠蛋白的选择性保留是如何工作的，我们监测了具有温度依赖性折叠缺陷的膜糖蛋白（tsO45水疱性口炎病毒的G蛋白）的长期命运。我们使用间接免疫荧光，免疫电子显微镜和新颖的Nycodenz梯度离心程序来分离ER，中间腔室和高尔基体。我们还使用了折叠和回收抑制剂二硫苏糖醇和AIF4-，并与钙粘蛋白抗体共免疫沉淀。结果表明，错误折叠的G蛋白不能仅保留在ER中。它可以移至中间隔室和顺式-高尔基网络，但随后被循环回ER。在急诊室，它与钙粘蛋白和BiP / GRP78有关。在这两个分子伴侣中，似乎只有BiP / GRP78伴随着它通过循环回路。因此，这种错误折叠的糖蛋白的保留是多种机制的结果，这些机制包括在内质网中钙结合蛋白的结合以及从中间区室和顺式-高尔基体网络的选择性检索。

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