College of Grassland Science and Technology, China Agricultural University, Beijing, 100083, China.
New Phytol. 2024 Apr;242(2):424-430. doi: 10.1111/nph.19639. Epub 2024 Feb 26.
Understanding the complexities of protein ubiquitination is crucial, as it plays a multifaceted role in controlling protein stability, activity, subcellular localization, and interaction, which are central to diverse biological processes. Deubiquitinases (DUBs) serve to reverse ubiquitination, but research progress in plant DUBs is noticeably limited. Among existing studies, UBIQUITIN-SPECIFIC PROTEASE 12 (UBP12) and UBP13 have garnered attention for their extensive role in diverse biological processes in plants. This review systematically summarizes the recent advancements in UBP12/13 studies, emphasizing their function, and their substrate specificity, their relationship with E3 ubiquitin ligases, and the similarities and differences with their mammalian orthologue, USP7. By unraveling the molecular mechanisms of UBP12/13, this review offers in-depth insights into the ubiquitin-proteasome system (UPS) in plants and aims to catalyze further explorations and comprehensive understanding in this field.
理解蛋白质泛素化的复杂性至关重要，因为它在控制蛋白质稳定性、活性、亚细胞定位和相互作用方面发挥着多方面的作用，这些都是各种生物过程的核心。去泛素化酶（DUBs）用于逆转泛素化，但植物 DUBs 的研究进展明显有限。在现有的研究中，泛素特异性蛋白酶 12（UBP12）和 UBP13 因其在植物中广泛参与各种生物过程而受到关注。本综述系统总结了 UBP12/13 研究的最新进展，强调了它们的功能和底物特异性，它们与 E3 泛素连接酶的关系，以及与它们的哺乳动物同源物 USP7 的相似性和差异性。通过揭示 UBP12/13 的分子机制，本综述深入了解了植物中的泛素-蛋白酶体系统（UPS），并旨在促进该领域的进一步探索和全面理解。
