AUTHOR=Hernandez-Rapp Julia , Martin-Lannerée Séverine , Hirsch Théo Z., Launay Jean-Marie , Mouillet-Richard Sophie 

TITLE=Hijacking PrPc-dependent signal transduction: when prions impair Aβ clearance

JOURNAL=Frontiers in Aging Neuroscience

VOLUME=6

YEAR=2014

URL=https://www.frontiersin.org/journals/aging-neuroscience/articles/10.3389/fnagi.2014.00025

DOI=10.3389/fnagi.2014.00025

ISSN=1663-4365

ABSTRACT=<p>The cellular prion protein PrP<sup>c</sup> is the normal counterpart of the scrapie prion protein PrP<sup> Sc</sup>, the main component of the infectious agent of transmissible spongiform encephalopathies. The recent discovery that PrP<sup> c</sup> can serve as a receptor for the amyloid beta (Aβ) peptide and relay its neurotoxicity is sparking renewed interest on this protein and its involvement in signal transduction processes. Disease-associated PrP<sup> Sc</sup> shares with Aβ the ability to hijack PrP<sup> c</sup>-dependent signaling cascades, and thereby instigate pathogenic events. Among these is an impairment of Aβ clearance, uncovered in prion-infected neuronal cells. These findings add another facet to the intricate interplay between PrP<sup> c</sup> and Aβ. Here, we summarize the connection between PrP-mediated signaling and Aβ clearance and discuss its pathological implications.</p>