Open Access
Article
Understanding the neurospecificity of Prion protein signaling
Benoit Schneider1,Mathea Pietri1,Elodie Pradines1,Damien Loubet1,Jean-Marie Launay1,Odile Kellermann1,Sophie Mouillet-Richard1
1
INSERM U747, Paris Descartes University, 75006 Paris, France
DOI: 10.2741/3682 Volume 16 Issue 1, pp.169-186
Published: 01 January 2011
(This article belongs to the Special Issue Cellular prion protein partners and signaling)
Abstract

The cellular prion protein PrP(C) is the normal counterpart of the scrapie prion protein PrP(Sc), the main component of the infectious agent of transmissible spongiform encephalopathies (TSEs). It is a ubiquitous cell-surface glycoprotein, abundantly expressed in neurons, which constitute the targets of TSE pathogenesis. The presence of PrP(C) at the surface of neurons is an absolute requirement for the development of prion diseases and corruption of PrP(C) function(s) within an infectious context emerges as a proximal cause for PrP(Sc)-induced neurodegeneration. Experimental evidence gained over the past decade indicates that PrP(C) has the capacity to mobilize promiscuous signal transduction cascades that, notably, contribute to cell homeostasis. Beyond ubiquitous effectors, much data converge onto a neurospecificity of PrP(C) signaling, which may be the clue to neuronal cell demise in prion disorders. In this article, we highlight the requirement of PrP(C) for TSEs-associated neurodegeneration and review the current knowledge of PrP(C)-dependent signal transduction in neuronal cells and its implications for PrP(Sc)-mediated neurotoxicity.

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Benoit Schneider, Mathea Pietri, Elodie Pradines, Damien Loubet, Jean-Marie Launay, Odile Kellermann, Sophie Mouillet-Richard. Understanding the neurospecificity of Prion protein signaling. Frontiers in Bioscience-Landmark. 2011. 16(1); 169-186.