Cellular and Molecular Life Sciences

, Volume 69, Issue 7, pp 1105–1124 | Cite as

Allosteric function and dysfunction of the prion protein

  • Rafael Linden
  • Yraima Cordeiro
  • Luis Mauricio T. R. Lima
Review

Abstract

Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases associated with progressive oligo- and multimerization of the prion protein (PrPC), its conformational conversion, aggregation and precipitation. We recently proposed that PrPC serves as a cell surface scaffold protein for a variety of signaling modules, the effects of which translate into wide-range functional consequences. Here we review evidence for allosteric functions of PrPC, which constitute a common property of scaffold proteins. The available data suggest that allosteric effects among PrPC and its partners are involved in the assembly of multi-component signaling modules at the cell surface, impose upon both physiological and pathological conformational responses of PrPC, and that allosteric dysfunction of PrPC has the potential to entail progressive signal corruption. These properties may be germane both to physiological roles of PrPC, as well as to the pathogenesis of the TSEs and other degenerative/non-communicable diseases.

Keywords

Prion Scaffold proteins Signal transduction Neurodegeneration Cell surface Oligomerization Signaling modules 

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Copyright information

© Springer Basel AG 2011

Authors and Affiliations

  • Rafael Linden
    • 1
  • Yraima Cordeiro
    • 2
  • Luis Mauricio T. R. Lima
    • 2
  1. 1.Instituto de Biofísica Carlos Chagas FilhoUFRJ, CCS, bloco G, Cidade UniversitáriaRio de JaneiroBrazil
  2. 2.Faculdade de FarmáciaUFRJRio de JaneiroBrazil

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