Molecular Recognition Research Center, Korea Institute of Science and Technology, Seoul 02792, Korea.
BMB Rep. 2018 Jun;51(6):261-262. doi: 10.5483/bmbrep.2018.51.6.110.
Aurora B is an important kinase involved in dynamic cellular events in mitosis. Aurora B activity is controlled by several post-translational modifications (PTMs). Among them, E3 ubiquitin ligase-mediated ubiquitination plays crucial roles in controlling the relocation and degradation of Aurora B. Aurora B, ubiquitinated by different E3 ligases, moves to the exact site for its mitotic function during metaphase-anaphase transition and is then degraded for cell cycle progression at the end of mitosis. However, how the stability of Aurora B is maintained until its degradation has been poorly understood. Recently, we have found that USP35 acts as a deubiquitinating enzyme (DUB) for Aurora B and affects its stability during cell division, thus being involved in the regulation of mitosis. In this review, we discuss the USP35-mediated deubiquitination of Aurora B and the regulation of mitotic progression by USP35. [BMB Reports 2018; 51(6): 261-262].
极光 B 是一种在有丝分裂中参与动态细胞事件的重要激酶。极光 B 的活性受到几种翻译后修饰（PTMs）的控制。其中，E3 泛素连接酶介导的泛素化在控制极光 B 的重定位和降解中起着至关重要的作用。极光 B 被不同的 E3 连接酶泛素化后，在中期-后期过渡期间移动到其有丝分裂功能的确切位置，然后在有丝分裂结束时降解以促进细胞周期进程。然而，直到其降解之前，极光 B 的稳定性是如何维持的，这一点还知之甚少。最近，我们发现 USP35 作为极光 B 的去泛素化酶（DUB）发挥作用，并影响其在细胞分裂过程中的稳定性，从而参与有丝分裂的调节。在这篇综述中，我们讨论了 USP35 介导的极光 B 的去泛素化以及 USP35 对有丝分裂进程的调节。[BMB 报告 2018;51(6):261-262]。
