Haglund Kaisa, Dikic Ivan
Institute for Biochemistry II, University Hospital of Goethe University, Frankfurt am Main, Germany.
EMBO J. 2005 Oct 5;24(19):3353-9. doi: 10.1038/sj.emboj.7600808. Epub 2005 Sep 8.
Ubiquitylation is an emerging mechanism implicated in a variety of nonproteolytic cellular functions. The attachment of a single ubiquitin (Ub) or poly-Ub (lysine 63) chains to proteins control gene transcription, DNA repair and replication, intracellular trafficking and virus budding. In these processes, protein ubiquitylation exhibits inducibility, reversibility and recognition by specialized domains, features similar to protein phosphorylation, which enable Ub to act as a signaling device. Here, we highlight several recent examples on how Ub regulates signaling and how signaling regulates ubiquitylation during physiological and pathological cellular processes.
泛素化是一种涉及多种非蛋白水解细胞功能的新兴机制。单个泛素（Ub）或多聚泛素（赖氨酸63）链与蛋白质的连接可控制基因转录、DNA修复与复制、细胞内运输以及病毒出芽。在这些过程中，蛋白质泛素化表现出诱导性、可逆性以及被特定结构域识别的特性，这些特性与蛋白质磷酸化相似，使得泛素能够作为一种信号传导装置发挥作用。在此，我们重点介绍几个近期的例子，说明泛素在生理和病理细胞过程中如何调节信号传导以及信号传导如何调节泛素化。
