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Activation of Mammalian Unfolded Protein Response Is Compatible with the Quality Control System Operating in the Endoplasmic Reticulum

机译：哺乳动物展开的蛋白质反应的激活与在内质网中运行的质量控制系统兼容

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Newly synthesized secretory and transmembrane proteins are folded and assembled in the endoplasmic reticulum (ER) where an efficient quality control system operates so that only correctly folded molecules are allowed to move along the secretory pathway. The productive folding process in the ER has been thought to be supported by the unfolded protein response (UPR), which is activated by the accumulation of unfolded proteins in the ER. However, a dilemma has emerged; activation of ATF6, a key regulator of mammalian UPR, requires intracellular transport from the ER to the Golgi apparatus. This suggests that unfolded proteins might be leaked from the ER together with ATF6 in response to ER stress, exhibiting proteotoxicity in the secretory pathway. We show here that ATF6 and correctly folded proteins are transported to the Golgi apparatus via the same route and by the same mechanism under conditions of ER stress, whereas unfolded proteins are retained in the ER. Thus, activation of the UPR is compatible with the quality control in the ER and the ER possesses a remarkable ability to select proteins to be transported in mammalian cells in marked contrast to yeast cells, which actively utilize intracellular traffic to deal with unfolded proteins accumulated in the ER.
机译：新合成的分泌蛋白和跨膜蛋白在内质网（ER）中折叠和组装，在此处运行有效的质量控制系统，从而仅允许正确折叠的分子沿分泌途径移动。 ER中的生产性折叠过程被认为是由未折叠的蛋白质反应（UPR）所支持的，该反应由未折叠的蛋白质在ER中的积累所激活。但是，出现了两难选择。哺乳动物UPR的关键调节因子ATF6的激活需要从ER到高尔基体的细胞内转运。这表明未折叠的蛋白可能会响应ER应激而与ET一起与ATF6一起从ER泄漏，在分泌途径中表现出蛋白毒性。我们在这里显示，在ER应激条件下，ATF6和正确折叠的蛋白质通过相同的途径和机制通过高尔基体运输，而未折叠的蛋白质保留在ER中。因此，UPR的激活与ER中的质量控制兼容，并且ER具有显着的能力来选择要在哺乳动物细胞中运输的蛋白质，这与酵母细胞形成了鲜明的对比，酵母细胞积极利用细胞内运输来处理积累的未折叠蛋白质。 ER。

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