Prion protein post-translational modifications modulate heparan sulfate binding and limit aggregate size in prion disease

• Published in: Neurobiology of disease Vol. 142; p. 104955
• Main Authors: Callender, Julia A., Sevillano, Alejandro M., Soldau, Katrin, Kurt, Timothy D., Schumann, Taylor, Pizzo, Donald P., Altmeppen, Hermann, Glatzel, Markus, Esko, Jeffrey D., Sigurdson, Christina J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2020; Elsevier
• Subjects: ADAM10 cleavage; Amyloid; Animals; Brain - metabolism; Cell Membrane - metabolism; Female; Glycans; Glycosaminoglycans; Glycosylation; Heparitin Sulfate - metabolism; Male; Mice; Mice, Transgenic; Neurodegeneration; Prion Diseases - genetics; Prion Diseases - metabolism; Prion Proteins - genetics; Prion Proteins - metabolism; Prion strains; Protein Aggregates - genetics; Protein Binding - genetics; Protein misfolding; Protein Processing, Post-Translational - genetics; Glycosaminoglycans; Protein misfolding; Neurodegeneration; Prion strains; ADAM10 cleavage; Amyloid; Glycans; Glycosylation

Many aggregation-prone proteins linked to neurodegenerative disease are post-translationally modified during their biogenesis. In vivo pathogenesis studies have suggested that the presence of post-translational modifications can shift the aggregate assembly pathway and profoundly alter the disease p...