Shao Linxin, Guo Mengqi, Kou Qianrui, Guo Ya, Li Xin, Li Fang
Yan'an Medical College, Yan'an University, Yan'an, China.
Front Mol Biosci. 2025 Aug 20;12:1650908. doi: 10.3389/fmolb.2025.1650908. eCollection 2025.
Ubiquitination and deubiquitination are common forms of protein post-translational modifications that play crucial roles in the regulation of intracellular homeostasis. As a member of deubiquitination enzyme USP family, USP36 maintains the stability of substrate proteins by mediating their deubiquitination, thereby playing a significant role in various pathophysiological processes. Here we focus on discussing how USP36 participates in regulating ribosome biosynthesis and responds to ribotoxic stress response. Furthermore, this review has elucidated the role of USP36 in regulating DNA replication stress, hypoxia adaptation, oxidative stress, and selective autophagy, as well as the related molecular mechanisms. This review is very helpful for understanding the role of USP36 in pathophysiological process and exploring the possibility of USP36 as a target for disease treatment.
泛素化和去泛素化是蛋白质翻译后修饰的常见形式，在细胞内稳态调节中发挥关键作用。作为去泛素化酶USP家族的成员，USP36通过介导底物蛋白的去泛素化来维持其稳定性，从而在各种病理生理过程中发挥重要作用。本文重点讨论USP36如何参与核糖体生物合成的调控以及对核糖体毒性应激反应的响应。此外，本综述阐明了USP36在调节DNA复制应激、缺氧适应、氧化应激和选择性自噬中的作用以及相关分子机制。本综述对于理解USP36在病理生理过程中的作用以及探索USP36作为疾病治疗靶点的可能性非常有帮助。
