Center for Research on Green Sustainable Chemistry, Tottori University, Tottori 680-8552, Japan.
Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori 680-8552, Japan.
J Biochem. 2022 Jun 28;172(1):1-7. doi: 10.1093/jb/mvac031.
Ubiquitination is a post-translational modification system essential for regulating a wide variety of biological processes in eukaryotes. Ubiquitin (Ub) itself undergoes post-translational modifications, including ubiquitination. All seven lysine residues and one N-terminal amino group of Ub can act as acceptors for further ubiquitination, producing eight types of Ub chains. Ub chains of different linkage types have different cellular functions and are referred to as the 'ubiquitin code'. Decoder molecules that contain linkage-specific Ub-binding domains (UBDs) recognize the Ub chains to regulate different cellular functions. On the other hand, deubiquitinases (DUBs) cleave Ub chains to reverse ubiquitin signals. This review discusses the molecular mechanisms of linkage-specific recognitions of Ub chains by UBDs and DUBs, which have been revealed by structural studies.
泛素化是一种翻译后修饰系统，对于真核生物中各种生物过程的调节至关重要。泛素 (Ub) 本身也经历了翻译后修饰，包括泛素化。Ub 的七个赖氨酸残基和一个 N 末端氨基都可以作为进一步泛素化的受体，产生八种类型的 Ub 链。不同连接类型的 Ub 链具有不同的细胞功能，被称为“泛素码”。含有特定连接 Ub 结合域 (UBD) 的解码分子识别 Ub 链以调节不同的细胞功能。另一方面，去泛素化酶 (DUBs) 切割 Ub 链以逆转泛素信号。本文综述了结构研究揭示的 UBDs 和 DUBs 对 Ub 链的特异性识别的分子机制。
