Chaperones in control of protein disaggregation
Chaperones in control of protein disaggregation
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DOI：
10.1038/sj.emboj.7601970
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发表时间：
2008-01-23
期刊：
影响因子：
11.4
通讯作者：
Zietkiewicz, Szymon
中科院分区：
文献类型：
--
作者：
Liberek, Krzysztof;Lewandowska, Agnieszka;Zietkiewicz, Szymon
伴侣蛋白网络控制蛋白质的初始折叠和随后的细胞内蛋白质的维持。虽然蛋白质的天然结构主要由其氨基酸序列编码，但体内折叠过程通常需要分子伴侣的帮助。分子伴侣还在翻译后质量控制系统中发挥作用，因此需要在变化的环境条件下保持蛋白质的正确构象。导致蛋白质去折叠和错误折叠的许多因素最终导致蛋白质聚集。高温胁迫是最早研究的诱导聚集的因素之一，至今仍是该领域的主要模型之一。随着大量蛋白质聚集在热暴露的反应中发生，细胞需要分子伴侣来控制和抵消聚集过程。聚集体的消除可以通过聚集体的溶解和释放的多肽的重折叠或其蛋白水解来实现。在这里，我们专注于热休克蛋白70（Hsp70），Hsp100和小的Hsp分子伴侣释放和重折叠蛋白质聚集体中捕获的多肽的分子机制。
The chaperone protein network controls both initial protein folding and subsequent maintenance of proteins in the cell. Although the native structure of a protein is principally encoded in its amino-acid sequence, the process of folding in vivo very often requires the assistance of molecular chaperones. Chaperones also play a role in a post-translational quality control system and thus are required to maintain the proper conformation of proteins under changing environmental conditions. Many factors leading to unfolding and misfolding of proteins eventually result in protein aggregation. Stress imposed by high temperature was one of the first aggregation-inducing factors studied and remains one of the main models in this field. With massive protein aggregation occurring in response to heat exposure, the cell needs chaperones to control and counteract the aggregation process. Elimination of aggregates can be achieved by solubilization of aggregates and either refolding of the liberated polypeptides or their proteolysis. Here, we focus on the molecular mechanisms by which heat-shock protein 70 ( Hsp70), Hsp100 and small Hsp chaperones liberate and refold polypeptides trapped in protein aggregates.