Functional genomics screen identifies proteostasis targets that modulate prion protein (PrP) stability.

ABSTRACT: Prion protein (PrP) adopts either a helical conformation (PrP^C) or an alternative, beta sheet-rich, misfolded conformation (PrP^Sc). The PrP^Sc form has the ability to "infect" PrP^C and force it into the misfolded state. Accumulation of PrP^Sc is associated with a number of lethal neurodegenerative disorders, including Creutzfeldt-Jacob disease (CJD). Knockout of PrP^C protects cells and animals from PrP^Sc infection; thus, there is interest in identifying factors that regulate PrP^C stability, with the therapeutic goal of reducing PrP^C levels and limiting infection by PrP^Sc. Here, we assembled a short-hairpin RNA (shRNA) library composed of 25+ shRNA sequences for each of 133 protein ho

SUBMITTER: Abrams J 

PROVIDER: S-EPMC7925731 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature