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Updated: Aug 24, 2025

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy
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The Dep1 protein: A new regulator of mitophagy in yeast

Nadine Camougrand1, Pierre Vigié2, Jim Dompierre1

  • 1CNRS, UMR5095, 1 rue Camille Saint-Saëns, 33077, Bordeaux cedex, France; Université de Bordeaux, UMR5095, 1 rue Camille Saint-Saëns, 33077, Bordeaux cedex, France.

Biochemical and Biophysical Research Communications
|October 25, 2022
PubMed

Insights

Dep1, a novel regulator of mitophagy, controls mitochondrial quality by modulating Atg32 expression. Its absence impairs mitophagy during starvation and stationary growth phases.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Mitochondria are vital organelles in eukaryotic cells, requiring quality control through mitophagy.
  • Mitophagy, the selective removal of damaged mitochondria, is mediated by receptors like Atg32.
  • Atg32 interacts with Atg11 and Atg8 to initiate and execute mitophagy, respectively.

Purpose of the Study:

  • To identify novel regulators of mitophagy.
  • To investigate the role of the Dep1 protein in the mitophagy pathway.
  • To elucidate the mechanism by which Dep1 influences Atg32 expression and mitophagy.

Main Methods:

  • Identification of Dep1 as part of the Rpd3L histone deacetylase complex.
  • Subcellular localization studies of Dep1 (nucleus and mitochondria).
  • Analysis of mitophagy induction under starvation and stationary phase conditions in wild-type and Dep1-deficient cells.

Main Results:

  • Dep1 is a novel regulator essential for mitophagy.
  • Dep1 associates with mitochondria and regulates the transcription and expression of the Atg32 protein.
  • Depletion of Dep1 significantly impairs mitophagy induced by nitrogen starvation or during the stationary phase.

Conclusions:

  • Dep1 plays a critical role in regulating mitophagy, likely through its influence on Atg32.
  • Dep1's dual localization and association with a histone deacetylase complex suggest complex regulatory mechanisms.
  • Further research into Dep1's function can uncover new therapeutic targets for mitochondrial dysfunction.

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