Pathogenic mutations located in the hydrophobic core of the prion protein interfere with folding and attachment of the glycosylphosphatidylinositol anchor.

Abstract excerpt

Abnormal folding of the cellular prion protein (PrPC) is a key feature in prion diseases. Here we show that two pathogenic mutations linked to inherited prion diseases in humans severely affect folding and maturation of PrPC in the secretory pathway of neuronal cells. PrP-T183A and PrP-F198S adopt a misfolded and partially protease-resistant conformation, lack the glycosylphosphatidylinositol anchor, and are not...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Cell Line, Tumor
• Share to Kinetics