| 张丽萍 戚欣 李静.辅分子伴侣调控热休克蛋白HSP90 功能的研究[J].现代生物医学进展英文版,2014,14(21):4168-4172. |
| 辅分子伴侣调控热休克蛋白HSP90 功能的研究 |
| Investigation of Regulatory Roles of Co-Chaperones on HSP90 Function |
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| DOI： |
| 中文关键词: 辅分子伴侣 HSP90 ATP |
| 英文关键词: Co-chaperones Heat shock protein 90 ATP |
| 基金项目:国家高技术研究发展（863）计划项目（2011AA09070104） |
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| 中文摘要: |
| 热休克蛋白90（HSP90）是一类ATPase 依赖性蛋白，作为分子伴侣，可在辅分子伴侣协助下，通过自身构象改变，参与众多
细胞的生物学事件，从而协助新合成蛋白的正确折叠、成功装配、功能稳定及异常蛋白的降解过程。HSP90 功能的发挥依赖于辅
分子伴侣及氨基末端结合的核苷酸。辅分子伴侣是一类可与分子伴侣（如，HSP90）结合并调节其功能的蛋白，通过参与ATPase 循
环从而调节HSP90 分子伴侣的功能。近年来，辅分子伴侣的研究得到越来越多的关注，本文就辅分子伴侣调控HSP90 功能的作
用进行综述。 |
| 英文摘要: |
| Heat shock protein 90 (HSP90) interacts with its client proteins in a dynamic ATP-dependent cycle. As a molecular
chaperone, this protein plays a critical role in intracellular biological events, including proteins folding, transport/assembling as well as
stabilizing proteins against heat shock and aiding in proteins degradation. HSP90 function is regulated by co-chaperones-HSP90
complexes and adenine nucleotides binding to the HSP90 amino terminus. Co-chaperones are non-client-binding partners of molecular
chaperones (such as HSP90), and may be initially defined as proteins that take part in regulation function of chaperones, most of
co-chaperones do not interact with clients directly, they can play a pivotal role in ATPase cycle by causing conformational change of
HSP90 and thus regulating interactions between HSP90 and its client proteins. The functions of co-chaperones have been thoroughly
investigated in the past decade, this review will focus on the regulatory roles of co-chaperones on HSP90 function. |
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