Echtenkamp Frank J, Freeman Brian C
Department of Cell and Development Biology, University of Illinois, Urbana, IL, USA.
Biochim Biophys Acta. 2012 Mar;1823(3):668-73. doi: 10.1016/j.bbamcr.2011.08.011. Epub 2011 Aug 24.
Cellular environments are highly complex and contain a copious variety of proteins that must operate in unison to achieve homeostasis. To guide and preserve order, multifaceted molecular chaperone networks are present within each cell type. To handle the vast client diversity and regulatory demands, a wide assortment of chaperones are needed. In addition to the classic heat shock proteins, cochaperones with inherent chaperoning abilities (e.g., p23, Hsp40, Cdc37, etc.) are likely used to complete a system. In this review, we focus on the HSP90-associated cochaperones and provide evidence supporting a model in which select cochaperones are used to differentially modulate target proteins, contribute to combinatorial client regulation, and increase the overall reach of a cellular molecular chaperone network. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).
细胞环境高度复杂，包含大量种类繁多的蛋白质，这些蛋白质必须协同作用以实现体内平衡。为了引导和维持秩序，每种细胞类型中都存在多方面的分子伴侣网络。为了应对大量不同的客户需求和调节需求，需要各种各样的伴侣蛋白。除了经典的热休克蛋白外，具有内在伴侣功能的共伴侣蛋白（如p23、Hsp40、Cdc37等）可能也被用于完善一个系统。在本综述中，我们聚焦于与HSP90相关的共伴侣蛋白，并提供证据支持一个模型，即选择特定的共伴侣蛋白来差异性地调节靶蛋白，促进对客户蛋白的组合调节，并扩大细胞分子伴侣网络的整体作用范围。本文是名为“热休克蛋白90（HSP90）”的特刊的一部分。
