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Protein Quality Control of the Endoplasmic Reticulum and Ubiquitin–Proteasome-Triggered Degradation of Aberrant Proteins: Yeast Pioneers the Path
Annual Review of Biochemistry ( IF 16.6 ) Pub Date : 2018-06-20 00:00:00 , DOI: 10.1146/annurev-biochem-062917-012749
Nicole Berner 1 , Karl-Richard Reutter 1 , Dieter H. Wolf 1
Affiliation  

Cells must constantly monitor the integrity of their macromolecular constituents. Proteins are the most versatile class of macromolecules but are sensitive to structural alterations. Misfolded or otherwise aberrant protein structures lead to dysfunction and finally aggregation. Their presence is linked to aging and a plethora of severe human diseases. Thus, misfolded proteins have to be rapidly eliminated. Secretory proteins constitute more than one-third of the eukaryotic proteome. They are imported into the endoplasmic reticulum (ER), where they are folded and modified. A highly elaborated machinery controls their folding, recognizes aberrant folding states, and retrotranslocates permanently misfolded proteins from the ER back to the cytosol. In the cytosol, they are degraded by the highly selective ubiquitin–proteasome system. This process of protein quality control followed by proteasomal elimination of the misfolded protein is termed ER-associated degradation (ERAD), and it depends on an intricate interplay between the ER and the cytosol.

中文翻译:


内质网和泛素-蛋白酶体引发的异常蛋白质降解的蛋白质质量控​​制:酵母开拓者之路

细胞必须不断监测其大分子成分的完整性。蛋白质是最通用的大分子类别,但对结构改变敏感。错误折叠的蛋白质结构或异常的蛋白质结构会导致功能障碍并最终聚集。它们的存在与衰老和许多严重的人类疾病有关。因此,错误折叠的蛋白质必须迅速消除。分泌蛋白占真核蛋白质组的三分之一以上。将它们导入内质网(ER),在此处进行折叠和修饰。高度精巧的机器控制它们的折叠,识别异常的折叠状态,并将永久错误折叠的蛋白质从ER逆向转运回到细胞质中。在细胞质中,它们被高度选择性的泛素-蛋白酶体系统降解。

更新日期:2018-06-20
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