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Abstract
The cellular prion protein (PrPC) is an N-glycosylated GPI-anchored protein usually present in lipid rafts with numerous putative functions. When it changes its conformation to a pathological isoform (then referred to as PrPSc), it is an essential part of the prion, the agent causing fatal and transmissible neurodegenerative prion diseases. There is growing evidence that toxicity and neuronal damage on the one hand and propagation/infectivity on the other hand are two distinct processes of the disease and that the GPI-anchor attachment of PrPC and PrPSc plays an important role in protein localization and in neurotoxicity. Here we review how the signal sequence of the GPI-anchor matters in PrPC localization, how an altered cellular localization of PrPC or differences in GPI-anchor composition can affect prion infection, and we discuss through which mechanisms changes on the anchorage of PrPC can modify the disease process.
Disclosure of Potential Conflicts of Interest
No potential conflicts of interest were disclosed.
Acknowledgments
This work is supported by grants of the Werner-Otto-Stiftung (to H.A.) and the Deutsche Forschungsgemeinschaft (DFG, GRK1459 and FOR885).
