Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.

Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.
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DOI:
10.1016/j.tibs.2011.11.005
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发表时间:
2012-03
影响因子:
13.8
通讯作者:
Vierling, Elizabeth
Vierling, Elizabeth
中科院分区:
生物学1区
文献类型:
--
作者:
Basha, Eman;O'Neill, Heather;Vierling, Elizabeth

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小分子热休克蛋白(small heat shock proteins,sHSP)及其相关的α-晶体蛋白(α-crystallin,αCs)是一种普遍存在的蛋白质,在各种应激条件下都能被强烈诱导,而且在许多生物体的多种细胞类型中都具有组成性功能。大量研究表明,大多数sHSPs和αCs可作为ATP非依赖性分子伴侣,与变性蛋白结合,从而保护细胞免受不可逆蛋白聚集的损伤。由于它们多样的进化历史,它们与遗传性人类疾病的联系,以及它们新颖的蛋白质动力学,sHSPs和αCs在生物学和生物化学的许多领域都具有重要意义。然而,越来越清楚的是,没有一个单一的模型足以描述sHSPs和αCs的结构,功能或作用机制。在这篇综述中,我们讨论了最近的数据,这些蛋白质的各种结构,它们的动态行为,它们如何识别底物,以及它们的许多可能的细胞作用。
The small heat shock proteins (sHSPs) and the related α-crystallins (αCs) are virtually ubiquitous proteins that are strongly induced by a variety of stresses, but that also function constitutively in multiple cell types in many organisms. Extensive research demonstrates that a majority of sHSPs and αCs can act as ATP-independent molecular chaperones by binding denaturing proteins and thereby protecting cells from damage due to irreversible protein aggregation. Because of their diverse evolutionary history, their connection to inherited human diseases, and their novel protein dynamics, sHSPs and αCs are of significant interest to many areas of biology and biochemistry. However, it is increasingly clear that no single model is sufficient to describe the structure, function or mechanism of action of sHSPs and αCs. In this review, we discuss recent data that provide insight into of the variety of structures of these proteins, their dynamic behavior, how they recognize substrates, and their many possible cellular roles.
DOI: 10.1074/jbc.m109.074088
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影响因子: 4.8
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