IndraLab

Statements

USP14 activates prion protein. 5 / 5
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"Although pharmacological inhibitors of USP14's ubiquitin-hydrolase activity reduced microtubule associate protein tau, tar DNA binding protein, and prion protein in culture, the effect was similar in wild type and USP14-deficient neurons, thus impacting their use for specifically evaluating USP14 in a therapeutic manner."
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"USP14 negatively regulates prion protein degradation."
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"Results demonstrated that an inhibitor of USP14 reduced PrP C in mouse neuroblastoma cells, as well as PrP Sc, indicating that USP14 negatively regulates degradation of prion protein."
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"Based on our results, we propose a model that shows that USP14 rescues prion protein from proteasomal degradation."
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"In summary, our findings demonstrated a novel mechanism by which USP14 negatively regulated prion protein degradation via the proteasome, although the detailed mechanism remains unclear."
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