Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation.
Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation.
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DOI：
10.1016/j.semcdb.2011.12.006
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发表时间：
2012-07
影响因子：
7.3
通讯作者：
Gardner, Richard G.
中科院分区：
文献类型：
--
作者：
Fredrickson, Eric K.;Gardner, Richard G.
错误折叠的蛋白质在细胞中不断产生，如果不进行有效管理，会对细胞生理学造成越来越大的损害。因此，所有生物体都进化出了解决错误折叠蛋白质的机制。真核细胞处理错误折叠蛋白质并发症的一种主要方式是通过泛素蛋白酶体系统破坏它们。为此，真核生物拥有专门的泛素蛋白质连接酶，能够识别错误折叠的蛋白质而不是正常折叠的蛋白质。这些蛋白质质量控制 (PQC) 连接酶用于靶向细胞中各种错误折叠蛋白质的策略可能与泛素蛋白质连接酶所使用的策略不同，泛素蛋白质连接酶通过调节降解来靶向正常折叠的蛋白质。在这篇综述中，我们重点介绍了 PQC 泛素蛋白连接酶如何识别错误折叠蛋白的已知信息。
Misfolded proteins are continuously produced in the cell and present an escalating detriment to cellular physiology if not managed effectively. As such, all organisms have evolved mechanisms to address misfolded proteins. One primary way eukaryotic cells handle the complication of misfolded proteins is by destroying them through the ubiquitin-proteasome system. To do this, eukaryotes possess specialized ubiquitin-protein ligases that have the capacity to recognize misfolded proteins over normally folded proteins. The strategies used by these Protein Quality Control (PQC) ligases to target the wide variety of misfolded proteins in the cell will likely be different than those used by ubiquitin-protein ligases that function in regulated degradation to target normally folded proteins. In this review, we highlight what is known about how misfolded proteins are recognized by PQC ubiquitin-protein ligases.
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影响因子：
4.8
作者：
Dasgupta, A;Ramsey, KL;Auble, DT
通讯作者：
Auble, DT
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作者：
Dimitrova, Lyudmila N.;Kuroha, Kazushige;Inada, Toshifumi
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Patterson, C
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Bays, NW;Gardner, RG;Hampton, RY
通讯作者：
Hampton, RY