Article
A pathogenic PrP mutation and doppel interfere with polarized sorting of the prion protein.
The Journal of biological chemistry - 18 Feb 2005
Uelhoff Armgard, Tatzelt Jörg, Aguzzi Adriano, Winklhofer Konstanze F, Haass Christian
Abstract excerpt
Several proteins linked to neurodegenerative diseases, such as the beta-amyloid precursor protein, amyloid beta-peptide, beta-secretase, and tau, undergo selective polarized sorting. We investigated polarized sorting of the mammalian prion protein (PrP(C)) and its homologue doppel (Dpl). In contrast to Dpl, which accumulates on the apical surface, PrP(C) is targeted selectively to the basolateral side in...
Topics
- Animals
- Cell Line
- Cell Polarity
- Dogs
- GPI-Linked Proteins
- Hydrophobic and Hydrophilic Interactions
- Mice
- Mutation
- Prion Diseases
- Prions
- Protein Sorting Signals