All quiet on the neuronal front: NMDA receptor inhibition by prion protein

The normal function of the prion protein (PrP)—the causative agent of mad cow or prion disease—has long remained out of reach. Deciphering PrP's function may help to unravel the complex chain of events triggered by PrP misfolding during prion disease. In this issue of the JCB, an exciting paper...

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Detalles Bibliográficos
Autor principal: Steele, Andrew D.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2008
Materias:
Reviews
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2364702/
https://www.ncbi.nlm.nih.gov/pubmed/18443224
http://dx.doi.org/10.1083/jcb.200803152
Descripción
Sumario:The normal function of the prion protein (PrP)—the causative agent of mad cow or prion disease—has long remained out of reach. Deciphering PrP's function may help to unravel the complex chain of events triggered by PrP misfolding during prion disease. In this issue of the JCB, an exciting paper (Khosravani, H., Y. Zhang, S. Tsutsui, S. Hameed, C. Altier, J. Hamid, L. Chen, M. Villemaire, Z. Ali, F.R. Jirik, and G.W. Zamponi. 2008. J. Cell Biol. 181:551–565) connects diverse observations regarding PrP into a coherent framework whereby PrP dampens the activity of an N-methyl-d-aspartate (NMDA) receptor (NMDAR) subtype and reduces excitotoxic lesions. The findings of this study suggest that understanding the normal function of proteins associated with neurodegenerative disease may elucidate the molecular pathogenesis.

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