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Cytoplasmic DAXX drives SQSTM1/p62 phase condensation to activate Nrf2-mediated stress response

Yi Yang1, Thea L Willis1, Robert W Button1

  • 1Peninsula Medical School, Faculty of Medicine and Dentistry, Institute of Translational and Stratified Medicine, University of Plymouth, Research Way, Plymouth, PL6 8BU, UK.

Nature Communications
|August 23, 2019
PubMed

Insights

DAXX protein interaction promotes p62 liquid condensation, enhancing cellular protein quality control and stress response. This discovery reveals a novel mechanism for regulating autophagy and maintaining redox homeostasis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy is crucial for intracellular protein quality control.
  • SQSTM1/p62 acts as a cargo receptor, forming liquid compartments for selective autophagic degradation.
  • Regulation of p62 phase separation is poorly understood.

Purpose of the Study:

  • To investigate the regulation of p62 phase separation.
  • To identify proteins interacting with p62.
  • To elucidate the functional consequences of p62 condensation.

Main Methods:

  • Unbiased yeast two-hybrid screening.
  • Complementary biochemical and cellular approaches.
  • Analysis of protein-protein interactions and phase separation.

Main Results:

  • DAXX physically interacts with p62.
  • Cytoplasmic DAXX promotes p62 puncta formation and liquid phase condensation by inducing p62 oligomerization.
  • This process enhances p62 recruitment of Keap1, activating the Nrf2-mediated stress response.

Conclusions:

  • DAXX regulates p62 phase condensation through protein interaction.
  • DAXX plays a role in maintaining redox homeostasis.
  • This study provides mechanistic insight into the prosurvival function of DAXX.

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