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© Research
Publication : Traffic (Copenhagen, Denmark)

The fate of PrP GPI-anchor signal peptide is modulated by P238S pathogenic mutation

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Traffic (Copenhagen, Denmark) - 31 Oct 2013

Guizzunti G, Zurzolo C

Link to Pubmed [PMID] – 24112521

Traffic 2014 Jan;15(1):78-93

Glycosylphosphatidylinositol (GPI)-anchored proteins are localized to the plasma membrane via a C-terminally linked GPI anchor. The GPI anchor is added concomitantly to the cleavage of the carboxy-terminal GPI-anchor signal sequence, thereby causing the release of a C-terminal hydrophobic peptide, whose fate has not yet been investigated. Here we followed the fate of the GPI-attachment signal of the prion protein (PrP), a protein implicated in various types of transmissible neurodegenerative spongiform encephalopathies (TSE). The PrP GPI-anchor signal sequence shows a remarkable and unusual degree of conservation across the species and contains two point mutations (M232R/T and P238S) that are responsible for genetic forms of prion disorders. We show that the PrP GPI-anchor signal peptide (SP), but not the one from an unrelated GPI-anchored protein (folate receptor), undergoes degradation via the proteasome. Moreover, the P238S point mutation partially protects the PrP GPI-anchor SP from degradation. Our data provide the first attempt to address the fate of a GPI-anchor SP and identify a role for the P238S mutation, suggesting the possibility that the PrP GPI-anchor SP could play a role in neurodegenerative prion diseases.

http://www.ncbi.nlm.nih.gov/pubmed/24112521