Partial Deletion of the Carboxyl-Terminal Signal Sequence of the Cellular Prion Protein Alters Protein Expression via Endoplasmic Reticulum-Associated Degradation.

ABSTRACT: Cellular prion protein (PrP^C) is a glycoprotein tethered to the plasma membrane via a GPI-anchor, and it plays a crucial role in prion diseases by undergoing conformational change to PrP^Sc. To generate a knock-in (KI) mouse model expressing bank vole PrP^C (BVPrP^C), a KI targeting construct was designed. However, a Prnp gene sequence that encodes PrP^C lacking seven C-terminal amino acid residues of the GPI-anchoring signal sequence (GPI-SS) was unintentionally introduced into the construct. The resulting KIBVPrP248 mice exhibited very low PrP^C expression and resistance to prion infection. To investigate the underlying mechanism of reduced PrP^C expression, RK13 cells expressing either full-length GPI-SS (BVPrP255) o

SUBMITTER: Yoo M 

PROVIDER: S-EPMC12410294 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature