Wild-Type PrP and a Mutant Associated with Prion Disease are Subject to Retrograde Transport and Proteasome Degradation

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 98; no. 26; pp. 14955 - 14960
• Main Authors: Ma, Jiyan, Lindquist, Susan
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 18.12.2001; National Acad Sciences; The National Academy of Sciences
• Subjects: Antibodies; Base Sequence; Biological Sciences; Cell aggregates; Cell Line; COS cells; Cultured cells; Cysteine Endopeptidases - metabolism; Cysteine Proteinase Inhibitors - pharmacology; Cytoplasm; Disease; DNA Primers; Fluorescent Antibody Technique; Hydrolysis; Multienzyme Complexes - metabolism; Mutagenesis, Site-Directed; Neurons; Prion diseases; Prion Diseases - genetics; Prion Diseases - metabolism; Prions; Proteasome Endopeptidase Complex; Protein Transport; Proteins; PrPSc Proteins - genetics; PrPSc Proteins - metabolism; Transfection

The cytoplasm seems to provide an environment that favors conversion of the prion protein (PrP) to a form with the physical characteristics of the PrPScconformation, which is associated with transmissible spongiform encephalopathies. However, it is not clear whether PrP would ever exist in the cytop...