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Copper drives prion protein phase separation and modulates aggregation.

Mariana Juliani do Amaral1,2, Satabdee Mohapatra2, Aline Ribeiro Passos3

  • 1Faculdade de Farmácia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.

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|November 3, 2023
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Summary
This summary is machine-generated.

Copper (Cu2+) promotes prion protein (PrP) condensation, acting as a cellular buffer. However, prolonged oxidative stress can cause these condensates to transition into toxic PrP aggregates, contributing to prion diseases.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Prion diseases involve prion protein (PrP) aggregation and neurodegeneration, linked to oxidative stress.
  • Prion protein's function may involve sequestering copper (Cu2+), with Cu2+ dyshomeostasis observed in prion disease brains.

Purpose of the Study:

  • To investigate the role of Cu2+ in PrP aggregation, specifically its influence on PrP condensation.
  • To elucidate the molecular mechanisms by which Cu2+ affects PrP structure and aggregation.

Main Methods:

  • Studied Cu2+-induced PrP condensation in live cells and in vitro using copartitioning assays.
  • Analyzed molecular changes in PrP structure (β-structure, hydrophobic exposure) upon Cu2+ binding.
  • Investigated the effect of oxidation (H2O2) on PrP:Cu2+ condensates and PrP aggregation.
  • Examined the impact of PrPC overexpression on cellular Cu2+ cytotoxicity and aggregation.

Main Results:

  • Cu2+ promotes PrP condensation in cells and in vitro, inhibiting PrP β-structure and hydrophobic residue exposure.
  • Oxidation triggers a liquid-to-solid transition of PrP:Cu2+ condensates, promoting amyloid-like PrP aggregation.
  • Overexpressed PrPC initially protects against Cu2+ toxicity but leads to PrPC aggregation with prolonged copper exposure.

Conclusions:

  • PrP condensates act as a copper buffer, preventing cellular toxicity.
  • Prolonged oxidative stress can shift PrP condensates towards aggregation, potentially contributing to prion disease pathogenesis.