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Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
Published on: May 10, 2015
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Deubiquitinating enzyme USP37 regulating oncogenic function of 14-3-3γ
Jin-Ock Kim1, So-Ra Kim1, Key-Hwan Lim1
1Department of Biomedical Science, CHA University, Bundang CHA Hospital, Gyeonggi-Do 463-400, Republic of Korea.
Oncotarget
|October 3, 2015
Summary
High expression of 14-3-3γ protein promotes cancer cell invasion and proliferation. The deubiquitinating enzyme USP37 stabilizes 14-3-3γ, potentially offering a new cancer therapeutic target.
Area of Science:
- Molecular Biology
- Cancer Biology
- Biochemistry
Background:
- 14-3-3 proteins are highly conserved and involved in numerous cellular processes.
- Previous studies indicated 14-3-3γ inhibits apoptosis and promotes immune cell proliferation.
- The deubiquitinating enzyme USP37 was identified as a binding partner for 14-3-3γ.
Purpose of the Study:
- To investigate the role of 14-3-3γ in cancer cell proliferation and invasion.
- To determine if USP37 mediates cancer cell proliferation through its interaction with 14-3-3γ.
- To elucidate the regulatory mechanism between USP37 and 14-3-3γ stability.
Main Methods:
- Analysis of 14-3-3γ expression in cancer cell lines.
- Overexpression studies of 14-3-3γ in cancer cells.
- In vivo tumor formation assays in SCID-NOD mice.
- Investigation of USP37's interaction with ubiquitin-conjugated 14-3-3γ.
- Assessment of USP37's catalytic activity on 14-3-3γ stability.
Main Results:
- High expression of 14-3-3γ correlates with increased cancer cell invasiveness and migration.
- Overexpression of 14-3-3γ promotes cell transformation, foci, and tumor formation in vivo.
- USP37 stabilizes ubiquitin-conjugated 14-3-3γ through its catalytic activity.
- USP37 prevents 14-3-3γ degradation, suggesting a role in regulating its stability.
Conclusions:
- USP37 acts as a specific deubiquitinating enzyme that stabilizes 14-3-3γ.
- The USP37-14-3-3γ interaction may contribute to malignant transformation via the MAPK signaling pathway.
- This interaction presents a potential new therapeutic target for cancer treatment.
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