Orren David K, Machwe Amrita
Department of Toxicology and Cancer Biology and Markey Cancer Center, University of Kentucky College of Medicine, Lexington, KY, USA.
Methods Mol Biol. 2019;1983:107-130. doi: 10.1007/978-1-4939-9434-2_7.
Posttranslational acetylation modifications of proteins have important consequences for cell biology, including effects on protein trafficking and cellular localization as well as on the interactions of acetylated proteins with other proteins and macromolecules such as DNA. Experiments to uncover and characterize protein acetylation events have historically been more challenging than investigating another common posttranslational modification, protein phosphorylation. More recently, high-quality antibodies that recognize acetylated lysine residues present in acetylated proteins and improved proteomic methodologies have facilitated the discovery that acetylation occurs on numerous cellular proteins and allowed characterization of the dynamics and functional effects of many acetylation events. This article summarizes some established biochemical information about how protein acetylation takes place and is regulated, in order to lay the foundation for subsequent descriptions of strategies used by our lab and others either to directly study acetylation of an individual factor or to identify groups of proteins targeted for acetylation that can then be examined in isolation.
蛋白质的翻译后乙酰化修饰对细胞生物学具有重要影响，包括对蛋白质运输和细胞定位的影响，以及对乙酰化蛋白质与其他蛋白质和大分子（如DNA）相互作用的影响。从历史上看，揭示和表征蛋白质乙酰化事件的实验比研究另一种常见的翻译后修饰——蛋白质磷酸化更具挑战性。最近，能够识别乙酰化蛋白质中乙酰化赖氨酸残基的高质量抗体以及改进的蛋白质组学方法，促进了人们发现许多细胞蛋白质都会发生乙酰化，并使得对许多乙酰化事件的动态变化和功能影响进行表征成为可能。本文总结了一些已确立的关于蛋白质乙酰化如何发生及受调控的生化信息，以便为后续描述我们实验室及其他实验室用于直接研究单个因子乙酰化或识别靶向乙酰化的蛋白质组群（随后可对其进行单独研究）的策略奠定基础。
