Regulation of pluripotency and differentiation by deubiquitinating enzymes

B. Suresh, J. Lee, H. Kim, S. Ramakrishna

Research output: Contribution to journalReview articlepeer-review

49 Citations (Scopus)


Post-translational modifications (PTMs) of stemness-related proteins are essential for stem cell maintenance and differentiation. In stem cell self-renewal and differentiation, PTM of stemness-related proteins is tightly regulated because the modified proteins execute various stem cell fate choices. Ubiquitination and deubiquitination, which regulate protein turnover of several stemness-related proteins, must be carefully coordinated to ensure optimal embryonic stem cell maintenance and differentiation. Deubiquitinating enzymes (DUBs), which specifically disassemble ubiquitin chains, are a central component in the ubiquitin-proteasome pathway. These enzymes often control the balance between ubiquitination and deubiquitination. To maintain stemness and achieve efficient differentiation, the ubiquitination and deubiquitination molecular switches must operate in a balanced manner. Here we summarize the current information on DUBs, with a focus on their regulation of stem cell fate determination and deubiquitinase inhibition as a therapeutic strategy. Furthermore, we discuss the possibility of using DUBs with defined stem cell transcription factors to enhance cellular reprogramming efficiency and cell fate conversion. Our review provides new insight into DUB activity by emphasizing their cellular role in regulating stem cell fate. This role paves the way for future research focused on specific DUBs or deubiquitinated substrates as key regulators of pluripotency and stem cell differentiation.

Original languageEnglish
Pages (from-to)1257-1264
Number of pages8
JournalCell Death and Differentiation
Issue number8
Publication statusPublished - 2016 Aug 1

Bibliographical note

Funding Information:
We would like to thank all of Suri's laboratory members for their helpful discussions. This study was supported by a grant of the National Research Foundation of Korea (201500000002885, 2015R1D1A1A01060907, and 2015H1D3A1036065 for HK).

Publisher Copyright:
© 2016 Macmillan Publishers Limited.

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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