The Hsp70 chaperone network.,Nature Reviews Molecular Cell Biology

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The Hsp70 chaperone network.
Nature Reviews Molecular Cell Biology ( IF 81.3 ) Pub Date : 2019-11-01 , DOI: 10.1038/s41580-019-0133-3
Rina Rosenzweig ₁ , Nadinath B Nillegoda _{2,

3,

4,

5} , Matthias P Mayer _{2,

4} , Bernd Bukau _{2,

3,

4}

Affiliation

The 70-kDa heat shock proteins (Hsp70s) are ubiquitous molecular chaperones that act in a large variety of cellular protein folding and remodelling processes. They function virtually at all stages of the life of proteins from synthesis to degradation and are thus crucial for maintaining protein homeostasis, with direct implications for human health. A large set of co-chaperones comprising J-domain proteins and nucleotide exchange factors regulate the ATPase cycle of Hsp70s, which is allosterically coupled to substrate binding and release. Moreover, Hsp70s cooperate with other cellular chaperone systems including Hsp90, Hsp60 chaperonins, small heat shock proteins and Hsp100 AAA+ disaggregases, together constituting a dynamic and functionally versatile network for protein folding, unfolding, regulation, targeting, aggregation and disaggregation, as well as degradation. In this Review we describe recent advances that have increased our understanding of the molecular mechanisms and working principles of the Hsp70 network. This knowledge showcases how the Hsp70 chaperone system controls diverse cellular functions, and offers new opportunities for the development of chemical compounds that modulate disease-related Hsp70 activities.

中文翻译：

Hsp70伴侣网络。

70 kDa热激蛋白（Hsp70s）是普遍存在的分子伴侣，可在多种细胞蛋白折叠和重塑过程中发挥作用。它们实际上在蛋白质生命的所有阶段都起作用，从合成到降解，因此对于维持蛋白质稳态至关重要，对人类健康有直接影响。包含J结构域蛋白和核苷酸交换因子的大量辅助分子伴侣调节Hsp70s的ATPase循环，该循环与底物的结合和释放发生了变构偶联。此外，Hsp70与其他细胞伴侣系统（包括Hsp90，Hsp60伴侣蛋白，小型热激蛋白和Hsp100 AAA +分解蛋白）合作，共同构成了一个动态且功能多样的网络，用于蛋白质折叠，展开，调节，靶向，聚集和分解，以及退化。在这篇综述中，我们描述了最近的进展，这些进展增加了我们对Hsp70网络的分子机制和工作原理的理解。这些知识展示了Hsp70分子伴侣系统如何控制多种细胞功能，并为调节与疾病相关的Hsp70活性的化学化合物的开发提供了新的机会。

更新日期：2019-11-18

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