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Updated: Apr 20, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
Published on: March 21, 2022
USP11 regulates p53 stability by deubiquitinating p53.
Jia-ying Ke1, Cong-jie Dai, Wen-lin Wu
1College of Chemistry and Life Science, Quanzhou Normal University, Quanzhou 36200, China; The Higher Educational Key Laboratory for Molecular Biology and Pharmacology of Fujian Province, Quanzhou 36200, China; Xiamen Women and Children Health Hospital, Xiamen 361005, China; Shouguang People's Hospital, Shouguang 262700, China; Department of Orthopedics, Central Hospital of Zibo, Zibo 255000, China; Department of Pathology, University of Chicago, Chicago 60102, Illinois, USA; Department of Pathology, the Second Affiliated Hospital of Fujian Medical University, Quanzhou 36200, China.
Ubiquitin-specific protease 11 (USP11) stabilizes the p53 tumor suppressor protein by removing ubiquitin tags. USP11 is crucial for activating p53 in response to DNA damage.
Area of Science:
- Molecular Biology
- Cancer Research
- Cellular Stress Response
Background:
- p53 is a critical tumor suppressor protein.
- p53 stability is regulated by ubiquitin-dependent degradation, mainly via Mdm2.
- Understanding p53 regulation is key to cancer research.
Purpose of the Study:
- To investigate the interaction between p53 and USP11.
- To determine USP11's role in p53 stability and function.
Main Methods:
- Co-immunoprecipitation assays were used to test p53-USP11 interaction.
- Ubiquitin-specific protease activity was assessed.
- p53 induction was measured following USP11 down-regulation.
Main Results:
- USP11 forms specific complexes with p53.
- USP11 stabilizes p53 through deubiquitination.
- Down-regulation of USP11 impairs p53 induction after DNA damage.
Conclusions:
- USP11 is a novel regulator of p53.
- USP11 is essential for p53 activation in response to DNA damage.
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