Jinyoung Park Song, Eunjoo 2024-01-19T22:33:54Z 2024-01-19T22:33:54Z 2021-09-03 2018-06 1976-6696 https://pubs.kist.re.kr/handle/201004/121346 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 ads 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. English 생화학분자생물학회 Deubiquitinase USP35 as a novel mitotic regulator via maintenance of Aurora B stability Article 10.5483/BMBRep.2018.51.6.110 1 BMB Reports, v.51, no.6, pp.261 - 262 BMB Reports 51 6 261 262 Y scie scopus kci ART002356526 000439689200001 2-s2.0-85049465714 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article APC(CDH1) Aurora B Mitotic progression USP35