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- W2014043099 abstract "Prion diseases involve the conversion of the endogenous prion protein, PrP(C), into a disease-associated form PrP(Sc). Reports show that a subset of PrP(C) is subject to degradation in the cytosol by the ubiquitin-proteasome system. Some studies show that cytosolic PrP(C) is neuroprotective, while others show that it is neurotoxic. Here, we report that cytosolic PrP(C) constructs interact with a pro-apoptotic protein, NRAGE (neurotrophin receptor interacting MAGE homolog). This novel interaction was identified in a yeast two-hybrid screen using PrP(C) as bait and confirmed by an in vitro binding assay and co-immunoprecipitations. Endogenous NRAGE accumulated in perinuclear aggregates following proteasome inhibition, and recombinant NRAGE and PrP(C)-EGFP co-localized in aggresomes after proteasome inhibition. Finally, co-expression of NRAGE and cytosolic PrP(C) affected mitochondrial membrane potential in neuroblastoma cells. Our results suggest that interaction of cytosolic PrP and NRAGE could affect neuronal viability." @default.
- W2014043099 created "2016-06-24" @default.
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- W2014043099 date "2005-06-01" @default.
- W2014043099 modified "2023-09-26" @default.
- W2014043099 title "Interaction of PrP with NRAGE, a protein involved in neuronal apoptosis" @default.
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- W2014043099 doi "https://doi.org/10.1016/j.mcn.2005.02.013" @default.
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