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Updated: Feb 13, 2026
10:54
Studying Proteolysis of Cyclin B at the Single Cell Level in Whole Cell Populations
Published on: September 17, 2012
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USP27-mediated Cyclin E stabilization drives cell cycle progression and hepatocellular tumorigenesis
Ling Dong1, Le Yu1, Chunrong Bai1
1Laboratory of Pathology, School of Life Sciences, Chongqing University, Chongqing, 401331, China.
Oncogene
|March 3, 2018
Summary
Ubiquitin-specific peptidase 27 (USP27) stabilizes Cyclin E, promoting hepatocellular carcinoma growth and invasion. Targeting USP27 may offer a new cancer therapy strategy.
Area of Science:
- Oncology
- Molecular Biology
- Biochemistry
Background:
- Overexpression of Cyclin E is implicated in various cancers, but the mechanisms are unclear.
- Ubiquitin-specific peptidase 27 (USP27) is a potential regulator of protein stability.
Purpose of the Study:
- To investigate the role of USP27 in hepatocellular carcinoma (HCC) pathogenesis.
- To identify USP27 as a potential therapeutic target for cancers with high Cyclin E levels.
Main Methods:
- Identified USP27 as a Cyclin E interactor using co-immunoprecipitation.
- Assessed the effect of USP27 suppression on HCC cell proliferation, migration, and invasion.
- Analyzed the correlation between USP27 and Cyclin E expression in HCC tissues.
- Investigated the impact of USP27 depletion on sensitivity to 5-fluorouracil (5-FU).
Main Results:
- USP27 directly interacts with Cyclin E and enhances its stability by inhibiting ubiquitination.
- USP27 suppression significantly inhibited HCC cell growth, migration, and invasion.
- A positive correlation was observed between USP27 and Cyclin E expression in HCC tissues.
- USP27 expression is downregulated by 5-FU, and its depletion sensitizes HCC cells to 5-FU-induced apoptosis.
Conclusions:
- USP27 stabilizes Cyclin E, contributing to HCC tumorigenesis.
- Targeting USP27 represents a promising therapeutic strategy for Cyclin E-driven cancers.
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