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USP30 deubiquitylates mitochondrial Parkin substrates and restricts apoptotic cell death

Jin-Rui Liang1, Aitor Martinez2, Jon D Lane3

  • 1Cellular and Molecular Physiology, Institute of Translational Medicine, University of Liverpool, Liverpool, UK.

EMBO Reports
|March 6, 2015
PubMed

Insights

The deubiquitylase USP30 controls mitochondrial cell death. USP30 depletion enhances apoptosis and sensitizes cancer cells, suggesting it as an anti-cancer therapy target.

Area of Science:

  • Mitochondrial biology
  • Cell death pathways
  • Ubiquitin regulation

Background:

  • Mitochondria are central to apoptosis.
  • Ubiquitin dynamics regulate cell death.
  • USP30 is a unique mitochondrial deubiquitylase.

Purpose of the Study:

  • Investigate USP30's role in mitochondrial cell death.
  • Determine USP30's impact on apoptosis regulation.
  • Explore USP30 as a potential cancer therapeutic target.

Main Methods:

  • Studied USP30's opposition to Parkin-dependent TOM20 ubiquitylation.
  • Assessed cell death in Parkin-overexpressing cells with USP30 depletion.
  • Examined USP30's regulation of BAX/BAK-dependent apoptosis.

Main Results:

  • USP30 depletion enhances depolarization-induced cell death in Parkin-overexpressing cells.
  • USP30 regulates BAX/BAK-dependent apoptosis.
  • USP30 depletion sensitizes cancer cells to BH3-mimetics.

Conclusions:

  • USP30 is crucial for setting the threshold of mitochondrial cell death.
  • USP30 represents a potential target for combinatorial anti-cancer therapies.
Keywords:
ParkinTOM20USP30apoptosismitophagy

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