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引用次数: 0
摘要
小热休克蛋白(sHsps)是在生理和应激条件下维持蛋白质平衡的细胞系统的重要组成部分。作为分子伴侣,它们以不依赖 ATP 的方式与不同的非本源蛋白质形成复合物。许多 sHsps 形成了能量相似但大小不同的寡聚体组合。通过改变这些组合体的平衡来调节伴侣活性。这使得 sHsps 成为一种多功能的适应性系统,可将非本地蛋白质困在复合物中,并在 ATP 依赖性伴侣的帮助下进行回收。在这篇综述中,我们将讨论对 sHsp 寡聚体结构原理及其功能原理的理解进展,以及它们在衰老和眼睛晶状体透明度中的作用。
Catchers of folding gone awry: a tale of small heat shock proteins.
Small heat shock proteins (sHsps) are an important part of the cellular system maintaining protein homeostasis under physiological and stress conditions. As molecular chaperones, they form complexes with different non-native proteins in an ATP-independent manner. Many sHsps populate ensembles of energetically similar but different-sized oligomers. Regulation of chaperone activity occurs by changing the equilibrium of these ensembles. This makes sHsps a versatile and adaptive system for trapping non-native proteins in complexes, allowing recycling with the help of ATP-dependent chaperones. In this review, we discuss progress in our understanding of the structural principles of sHsp oligomers and their functional principles, as well as their roles in aging and eye lens transparency.
期刊介绍:
For over 40 years, Trends in Biochemical Sciences (TIBS) has been a leading publication keeping readers informed about recent advances in all areas of biochemistry and molecular biology. Through monthly, peer-reviewed issues, TIBS covers a wide range of topics, from traditional subjects like protein structure and function to emerging areas in signaling and metabolism. Articles are curated by the Editor and authored by top researchers in their fields, with a focus on moving beyond simple literature summaries to providing novel insights and perspectives. Each issue primarily features concise and timely Reviews and Opinions, supplemented by shorter articles including Spotlights, Forums, and Technology of the Month, as well as impactful pieces like Science & Society and Scientific Life articles.