Max Planck Institute of Psychiatry, Department of Translational Research in Psychiatry, Munich, Germany.
Biochem Soc Trans. 2020 Apr 29;48(2):441-449. doi: 10.1042/BST20190332.
Adaptation to stress is a fundamental requirement to cope with changing environmental conditions that pose a threat to the homeostasis of cells and organisms. Post-translational modifications (PTMs) of proteins represent a possibility to quickly produce proteins with new features demanding relatively little cellular resources. FK506 binding protein (FKBP) 51 is a pivotal stress protein that is involved in the regulation of several executers of PTMs. This mini-review discusses the role of FKBP51 in the function of proteins responsible for setting the phosphorylation, ubiquitination and lipidation of other proteins. Examples include the kinases Akt1, CDK5 and GSK3β, the phosphatases calcineurin, PP2A and PHLPP, and the ubiquitin E3-ligase SKP2. The impact of FKBP51 on PTMs of signal transduction proteins significantly extends the functional versatility of this protein. As a stress-induced protein, FKBP51 uses re-setting of PTMs to relay the effect of stress on various signaling pathways.
适应压力是应对威胁细胞和生物体内稳态的环境变化的基本要求。蛋白质的翻译后修饰（PTMs）为快速产生具有新特性的蛋白质提供了一种可能，这些新特性只需要相对较少的细胞资源。FK506 结合蛋白（FKBP）51 是一种关键的应激蛋白，参与调节几种 PTMs 的执行者。这篇迷你综述讨论了 FKBP51 在负责设定其他蛋白质磷酸化、泛素化和脂化的蛋白质功能中的作用。例如，包括激酶 Akt1、CDK5 和 GSK3β、磷酸酶钙调神经磷酸酶、PP2A 和 PHLPP，以及泛素 E3 连接酶 SKP2。FKBP51 对信号转导蛋白 PTMs 的影响显著扩展了该蛋白的功能多样性。作为一种应激诱导蛋白，FKBP51 使用 PTMs 的重新设定来传递应激对各种信号通路的影响。
