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Updated: Feb 24, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
Published on: March 21, 2022
p53 stability is regulated by diverse deubiquitinating enzymes
Seul-Ki Kwon1, Madhuri Saindane1, Kwang-Hyun Baek1
1Department of Biomedical Science, CHA University, Gyeonggi-Do 13488, Republic of Korea.
Abstract:
The tumor suppressor protein p53 has a variety of roles in responses to various stress signals. In such responses, p53 activates specific transcriptional targets that control cell cycle arrest, DNA repair, angiogenesis, autophagy, metabolism, migration, aging, senescence, and apoptosis. Since p53 has been identified as the most frequently altered gene in human cancers, regulation and stabilization of its normal functions are important. Stability of p53 is regulated by the ubiquitin-proteasome pathway (UPP). Furthermore, it is readjusted by deubiquitination via deubiquitinating enzymes (DUBs) that can eliminate ubiquitin from p53. Diverse DUBs directly or indirectly affect the ubiquitination of p53 and, consequently, regulate various cellular processes associated with p53. As maintenance of p53 is regulated by a variety of DUBs, the interaction of DUBs and p53 can affect diseases such as cancer. Currently, DUBs have a central role in our understanding of various cancers, and some have potential in the development of effective therapeutic strategies. This review summarizes the current knowledge of p53 and of the interconnection between p53 and DUBs.
Insights
The tumor suppressor protein p53 is crucial for cellular health and is often altered in cancer. Deubiquitinating enzymes (DUBs) regulate p53 stability, offering potential therapeutic targets for cancer treatment.
Area of Science:
- Molecular Biology
- Cancer Research
- Biochemistry
Background:
- The tumor suppressor protein p53 plays vital roles in cellular stress responses, including DNA repair, apoptosis, and cell cycle arrest.
- p53 is the most frequently altered gene in human cancers, making its regulation critical.
- p53 stability is primarily controlled by the ubiquitin-proteasome pathway (UPP) and deubiquitinating enzymes (DUBs).
Purpose of the Study:
- To review the current understanding of the tumor suppressor protein p53.
- To explore the intricate relationship between p53 and deubiquitinating enzymes (DUBs).
- To highlight the implications of the p53-DUBs interaction in cancer pathogenesis and therapeutic strategies.
Main Methods:
- Literature review of studies on p53, ubiquitin-proteasome pathway, and DUBs.
- Analysis of the regulatory mechanisms of p53 ubiquitination and deubiquitination.
- Synthesis of information on the role of DUBs in p53 stabilization and function.
Main Results:
- Diverse DUBs directly or indirectly influence p53 ubiquitination status.
- Regulation of p53 stability by DUBs impacts various cellular processes controlled by p53.
- The interaction between DUBs and p53 is implicated in the development and progression of various cancers.
Conclusions:
- DUBs are key regulators of p53 stability and function.
- The interplay between p53 and DUBs is central to understanding cancer biology.
- Targeting DUBs presents a promising avenue for developing novel cancer therapeutics.
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