Cytoskeleton-dependent clustering of membrane-bound prion protein on the cell surface.

ABSTRACT: Prion diseases are a group of neurodegenerative disorders that infect animals and humans with proteinaceous particles called prions. Prions consist of scrapie prion protein (PrP^Sc), a misfolded version of the cellular prion protein (PrP^C). During disease progression, PrP^Sc replicates by interacting with PrP^C and inducing its conversion to PrP^Sc. Attachment of PrP^C to cellular membranes via a glycosylphosphatidylinositol (GPI) anchor is critical for the conversion of PrP^C into PrP^Sc. However, the mechanisms governing PrP^C conversion and replication on the membrane remain largely unclear. Here, a site-selectively modified PrP variant equipped with a fluorescent GPI anchor mimic (PrP-GPI) was em

SUBMITTER: Hackl S 

PROVIDER: S-EPMC7988330 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature