Global analysis of protein degradation in prion infected cells.

ABSTRACT: Prion diseases are rare, neurological disorders caused by the misfolding of the cellular prion protein (PrP^C) into cytotoxic fibrils (PrP^Sc). Intracellular PrP^Sc aggregates primarily accumulate within late endosomes and lysosomes, organelles that participate in the degradation and turnover of a large subset of the proteome. Thus, intracellular accumulation of PrP^Sc aggregates has the potential to globally influence protein degradation kinetics within an infected cell. We analyzed the proteome-wide effect of prion infection on protein degradation rates in N2a neuroblastoma cells by dynamic stable isotopic labeling with amino acids in cell culture (dSILAC) and bottom-up proteomics. The analysis quantified the degradation rates of more than 4,700 pr

SUBMITTER: Hutti CR 

PROVIDER: S-EPMC7329860 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature