Department of Life Science, College of Natural Sciences, Hanyang University, Seoul, South Korea.
Graduate School of Biomedical Science and Engineering, Hanyang University, Seoul, South Korea
Open Biol. 2017 Jun;7(6). doi: 10.1098/rsob.170016.
Deubiquitylating enzymes (DUBs) reverse the ubiquitylation of target proteins, thereby regulating diverse cellular functions. In contrast to the plethora of research being conducted on the ability of DUBs to counter the degradation of cellular proteins or auto-ubiquitylated E3 ligases, very little is known about the mechanisms of DUB regulation. In this review paper, we summarize a novel possible mechanism of DUB deubiquitylation by other DUBs. The available data suggest the need for further experiments to validate and characterize this notion of 'Dubbing DUBs'. The current studies indicate that the idea of deubiquitylation of DUBs by other DUBs is still in its infancy. Nevertheless, future research holds the promise of validation of this concept.
去泛素化酶（DUBs）可以逆转靶蛋白的泛素化，从而调节多种细胞功能。与大量研究 DUB 能够阻止细胞蛋白降解或自身泛素化 E3 连接酶的能力形成鲜明对比的是，人们对 DUB 调节的机制知之甚少。在这篇综述论文中，我们总结了一种 DUB 通过其他 DUB 进行去泛素化的新的可能机制。现有数据表明，需要进一步的实验来验证和描述这种“DUBbing DUBs”的概念。目前的研究表明，DUB 被其他 DUB 去泛素化的观点仍处于起步阶段。然而，未来的研究有望验证这一概念。
