Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
Degradation of misfolded protein in the cytoplasm is mediated by the ubiquitin ligase Ubr1
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DOI：
10.1016/j.febslet.2008.11.015
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发表时间：
2008-12-24
期刊：
影响因子：
3.5
通讯作者：
Wolf, Dieter H.
中科院分区：
文献类型：
--
作者：
Eisele, Frederik;Wolf, Dieter H.
蛋白质质量控制和随后消除末端错误折叠的蛋白质是通过泛素-蛋白酶体系统进行的。用泛素标记错误折叠的蛋白质以进行降解依赖于一系列涉及泛素活化酶(E1)、泛素结合酶(E2)和泛素连接酶(E3)的反应。虽然已发现泛素连接酶可将错误折叠的分泌蛋白靶向蛋白酶体降解(ERAD)，但还没有发现这样的E3酶用于消除酵母中错误折叠的细胞质蛋白。在这里，我们报告了Ubr1的发现，它是N端规则通路的E3连接酶，负责将错误折叠的细胞质蛋白靶向蛋白酶体降解。(C)2008年欧洲生化学会联合会。爱思唯尔出版，版权所有。
Protein quality control and subsequent elimination of terminally misfolded proteins occurs via theubiquitin-proteasome system. Tagging of misfolded proteins with ubiquitin for degradation depends on a cascade of reactions involving an ubiquitin activating enzyme (E1), ubiquitin conjugating enzymes (E2) and ubiquitin ligases (E3). While ubiquitin ligases responsible for targeting misfolded secretory proteins to proteasomal degradation (ERAD) have been uncovered, no such E3 enzymes have been found for elimination of misfolded cytoplasmic proteins in yeast. Here we report on the discovery of Ubr1, the E3 ligase of the N-end rule pathway, to be responsible for targeting misfolded cytosoplasmic protein to proteasomal degradation. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.