Regulation of pluripotency and differentiation by deubiquitinating enzymes.

Title
Regulation of pluripotency and differentiation by deubiquitinating enzymes.
Author
Ramakrishna, Suresh
Keywords
UBIQUITIN-SPECIFIC PROTEASES; STEM-CELL DIFFERENTIATION; KAPPA-B ACTIVATION; DIRECT CONVERSION; DEFINED FACTORS; POLYUBIQUITIN CHAINS; TRANSCRIPTIONAL ACTIVATION; PROTEIN-DEGRADATION; THERAPEUTIC TARGETS; NEURAL PROGENITORS
Issue Date
2016-08
Publisher
NATURE PUBLISHING GROUP
Citation
CELL DEATH AND DIFFERENTIATION, v. 23, NO. 8, Page. 1257-1264
Abstract
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.
URI
https://www.nature.com/articles/cdd201653http://repository.hanyang.ac.kr/handle/20.500.11754/76100
ISSN
1350-9047; 1476-5403
DOI
10.1038/cdd.2016.53
Appears in Collections:
GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > ETC
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