Deubiquitinase USP35 as a novel mitotic regulator via maintenance of Aurora B stability

Jinyoung Park, Eun Joo Song

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


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.

Original languageEnglish
Pages (from-to)261-262
Number of pages2
JournalBMB Reports
Issue number6
StatePublished - 2018

Bibliographical note

Publisher Copyright:
© 2018 by the The Korean Society for Biochemistry and Molecular Biology.


  • Aurora B
  • Mitotic progression
  • USP35


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