The multifaceted roles of usp15 in signal transduction

Tanuza Das, Eun Joo Song, Eunice Eun Kyeong Kim

Research output: Contribution to journalReview articlepeer-review

20 Scopus citations


Ubiquitination and deubiquitination are protein post-translational modification processes that have been recognized as crucial mediators of many complex cellular networks, including maintaining ubiquitin homeostasis, controlling protein stability, and regulating several signaling pathways. Therefore, some of the enzymes involved in ubiquitination and deubiquitination, particularly E3 ligases and deubiquitinases, have attracted attention for drug discovery. Here, we review recent findings on USP15, one of the deubiquitinases, which regulates diverse signaling pathways by deubiquitinating vital target proteins. Even though several basic previous studies have uncovered the versatile roles of USP15 in different signaling networks, those have not yet been systematically and specifically reviewed, which can provide important information about possible disease markers and clinical applications. This review will provide a comprehensive overview of our current under-standing of the regulatory mechanisms of USP15 on different signaling pathways for which dynamic reverse ubiquitination is a key regulator.

Original languageEnglish
Article number4728
JournalInternational Journal of Molecular Sciences
Issue number9
StatePublished - 1 May 2021

Bibliographical note

Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.


  • BMP
  • CSN
  • IGF
  • NF-κB
  • Nrf2–Keap1
  • P53
  • RNA splicing
  • TGF-β
  • USP15
  • Wnt/β-catenin


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