From the Department of Chemistry, Technical University of Munich, 85747 Garching, Germany
J Biol Chem. 2019 Feb 8;294(6):2074-2075. doi: 10.1074/jbc.REV118.006739. Epub 2019 Jan 9.
Protein folding is a spontaneous process. However, under physiological conditions, proteins are inherently unstable, and the protein concentrations in living cells favor unspecific interactions between partially folded proteins. Thus, the cellular proteome requires the assistance of helper factors, the molecular chaperones, for quality control and the maintenance of protein homeostasis. This series of reviews delves into how these molecular machines work in the eukaryotic cell, how they convey resilience to life, how these functions have allowed expansion of the protein universe, and how we can target them for therapeutic purposes. Together, they present the progress made in recent years in our understanding of one of the most fundamental aspects of life.
蛋白质折叠是一个自发的过程。然而,在生理条件下,蛋白质本质上是不稳定的,活细胞中的蛋白质浓度有利于部分折叠的蛋白质之间的非特异性相互作用。因此,细胞中的蛋白质组需要辅助因子(分子伴侣)的协助来进行质量控制和维持蛋白质的动态平衡。这一系列综述深入探讨了这些分子机器在真核细胞中是如何工作的,它们如何赋予生命弹性,这些功能如何使蛋白质宇宙得以扩展,以及我们如何将它们作为治疗靶点。它们共同展示了近年来我们在理解生命的一个最基本方面所取得的进展。