Department of Cell and Chemical Biology, Chemical Immunology, Oncode Institute, Leiden University Medical Centre, 2333 ZC, Leiden, The Netherlands.
Curr Top Microbiol Immunol. 2019;420:111-130. doi: 10.1007/82_2018_134.
Ubiquitination is a frequently occurring and very diverse posttranslational modification influencing a wide scope of cellular processes. Ubiquitin (Ub) has the unique ability to form eight different lysine-linked polymeric chains, mixed chains and engages with ubiquitin-like (Ubl) molecules. The distinct signals evoked by specific enzymes play a crucial role in, for instance, proteasome-mediated protein degradation, cell cycle regulation, and DNA damage responses. Due to the large variety of cellular functions that this posttranslational modification influences, the enzymes that construct such Ub modifications, and subsequently controle and degrade these signals, is enormous. In this chapter, we will discuss the current state-of-the-art of activity-based probes, reporter substrates, and other relevant tools based on Ub as recognition element, to study the enzymes involved in the complex system of ubiquitination.
泛素化是一种常见且多样化的翻译后修饰,影响着广泛的细胞过程。泛素 (Ub) 具有形成八种不同赖氨酸连接的聚合链、混合链和与泛素样 (Ubl) 分子结合的独特能力。特定酶引发的不同信号在蛋白酶体介导的蛋白质降解、细胞周期调控和 DNA 损伤反应等方面起着至关重要的作用。由于这种翻译后修饰影响着大量的细胞功能,因此构建这种 Ub 修饰的酶,以及随后控制和降解这些信号的酶,数量巨大。在本章中,我们将讨论基于 Ub 作为识别元件的活性探针、报告底物和其他相关工具的最新进展,以研究参与泛素化复杂系统的酶。