Regulation of deubiquitinating enzymes by post-translational modifications

Tanuza Das, Sang Chul Shin, Eun Joo Song, Eunice Eunkyeong Kim

Research output: Contribution to journalReview articlepeer-review

33 Scopus citations


Ubiquitination and deubiquitination play a critical role in all aspects of cellular processes, and the enzymes involved are tightly regulated by multiple factors including posttranslational modifications like most other proteins. Dysfunction or misregulation of these enzymes could have dramatic physiological consequences, sometimes leading to diseases. Therefore, it is important to have a clear understanding of these regulatory processes. Here, we have reviewed the posttranslational modifications of deubiquitinating enzymes and their consequences on the catalytic activity, stability, abundance, localization, and interaction with the partner proteins.

Original languageEnglish
Article number4028
JournalInternational Journal of Molecular Sciences
Issue number11
StatePublished - 1 Jun 2020

Bibliographical note

Funding Information:
This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Ministry of Science and ICT (2017R1A2B3007224 and 2019R1A2C2004052). Tanuza Das was supported by Korea Research Fellowship Program through the National Research Foundation of Korea funded by the Ministry of Science and ICT (2017HID3A1A02054608).

Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.


  • Activity
  • Deubiquitinase (DUB)
  • Deubiquitinating enzyme
  • Disease
  • Interaction
  • Localization
  • Post-translational modification (PTM)


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