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Updated: Jul 18, 2025

Techniques to Induce and Quantify Cellular Senescence
Published on: May 1, 2017
USP13 regulates cell senescence through mediating MDM2 stability
Jinshan He1, Boina Baoyinna2, Sarah J Taleb2
1Department of Physiology and Cell Biology, the Ohio State University Wexner Medical Center, Columbus, OH 43210, USA; Department of Microbial Infection and Immunity, the Ohio State University Wexner Medical Center, Columbus, OH 43210, USA.
Ubiquitin-Specific Protease 13 (USP13) promotes lung cell senescence and aging by reducing MDM2 levels. This deubiquitinating enzyme plays a key role in lung aging mechanisms.
Area of Science:
- Gerontology
- Molecular Biology
- Cellular Biology
Background:
- Lung aging impairs function, remodeling, and regeneration, increasing disease susceptibility.
- Deubiquitinating enzymes (DUBs) are implicated in aging and disease via cellular signaling.
- The specific role of Ubiquitin-Specific Protease 13 (USP13) in lung aging is not well understood.
Purpose of the Study:
- To investigate the function of USP13 in cellular senescence and lung aging.
- To elucidate the molecular mechanisms by which USP13 influences lung aging.
Main Methods:
- Compared USP13 and MDM2 protein levels in aged and young mouse lung tissues.
- Utilized gene silencing and overexpression of USP13 in human cell lines.
- Assessed MDM2 levels via qPCR and Western blotting; measured senescence using β-galactosidase staining.
Main Results:
- Aged mouse lungs exhibited higher USP13 levels, negatively correlating with MDM2.
- USP13 deficiency increased MDM2 levels; USP13 overexpression promoted senescence and reduced MDM2.
- USP13 targets MDM2 for degradation, reducing its K63-linked polyubiquitination.
Conclusions:
- USP13 is upregulated in aged lungs and promotes cellular senescence.
- USP13 regulates lung aging pathways by controlling MDM2 protein stability.
- USP13 represents a potential therapeutic target for age-related lung diseases.
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