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Usp7 protects genomic stability by regulating Bub3

Serena Giovinazzi1, Pietro Sirleto, Vasilisa Aksenova

  • 1Department of Anatomy and Cell Biology, University of Florida College of Medicine, Gainesville, FL; University of Florida Health Cancer Center, Gainesville, FL.

Oncotarget
|July 9, 2014
PubMed

Insights

Ubiquitin Specific Processing Protease-7 (USP7) regulates genomic stability by controlling the spindle assembly checkpoint component Bub3. USP7 inhibition causes mitotic abnormalities, highlighting its potential in cancer therapy.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Ubiquitin Specific Processing Protease-7 (USP7) is a deubiquitinase regulating cellular processes.
  • USP7 deregulation is linked to cancer, making USP7 inhibition a potential anti-cancer strategy.

Purpose of the Study:

  • To investigate the novel function of USP7 in maintaining genomic stability.
  • To identify USP7 substrates and related cellular activities for potential clinical applications.

Main Methods:

  • USP7 depletion and inhibition using small molecule inhibitors.
  • Analysis of mitotic progression, chromosomal abnormalities, and protein levels (e.g., cyclin B, Bub3).
  • In silico analysis of USP7 levels and genomic instability across NCI-60 cell lines.

Main Results:

  • USP7 depletion leads to prolonged mitosis, micronuclei accumulation, lagging chromosomes, and karyotype instability.
  • USP7 inhibition stabilizes cyclin B and induces mitotic abnormalities.
  • USP7 interacts with and deubiquitinates Bub3, a spindle assembly checkpoint component, leading to decreased Bub3 levels.
  • Lower USP7 levels correlate with genomic instability in NCI-60 cell lines.

Conclusions:

  • USP7 plays a novel and critical role in regulating the spindle assembly checkpoint (SAC) component Bub3.
  • USP7 is essential for maintaining genomic stability.
  • USP7 inhibition presents a promising avenue for anti-cancer therapeutic strategies.

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