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Deubiquitinase USP13 dictates MCL1 stability and sensitivity to BH3 mimetic inhibitors

Shengzhe Zhang1,2, Meiying Zhang3, Ying Jing1

  • 1State Key Laboratory of Oncogenes and Related Genes, Department of Obstetrics and Gynecology, Ren Ji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai, 200127, China.

Nature Communications
|January 17, 2018
PubMed

Insights

The deubiquitinase USP13 stabilizes MCL1, a protein promoting cancer cell survival. Inhibiting USP13 reduces MCL1, hindering tumor growth and increasing sensitivity to cancer therapies.

Area of Science:

  • Molecular Biology
  • Cancer Research
  • Biochemistry

Background:

  • MCL1 is a key anti-apoptotic protein in the BCL-2 family.
  • MCL1 expression is regulated by ubiquitination and deubiquitination.
  • USP9X is known to stabilize MCL1 by removing polyubiquitin chains.

Purpose of the Study:

  • To identify novel deubiquitinases regulating MCL1 stability.
  • To investigate the role of USP13 in cancer cell survival and tumor growth.
  • To evaluate USP13 as a potential therapeutic target.

Main Methods:

  • Unbiased siRNA screening to identify regulators of MCL1.
  • CRISPR/Cas9 gene editing for USP13 depletion.
  • Xenograft mouse models to assess tumor growth inhibition.
  • Western blotting to analyze protein levels and ubiquitination status.

Main Results:

  • USP13 was identified as a novel deubiquitinase that stabilizes MCL1.
  • USP13 interacts with and deubiquitinates MCL1, preserving its expression.
  • USP13 depletion inhibited tumor growth in vivo.
  • Inhibition of USP13 reduced MCL1 protein levels and sensitized cancer cells to BH3 mimetics.

Conclusions:

  • USP13 is a novel regulator of MCL1 turnover in solid tumors.
  • USP13 inhibition represents a potential therapeutic strategy for various malignancies.
  • Targeting USP13 may enhance the efficacy of existing cancer treatments.

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