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First published online January 27, 2006

Journal of Cell Science 119, 304e (2006)
© The Company of Biologists Limited
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In this issue

Rafts to escape prion disease


Figure 1

Despite intensive research, the cell biology of prion diseases - neurodegenerative diseases associated with the conformational conversion of the cell-surface glycoprotein PrPC into its pathogenic PrPSc form - remains controversial. On p. 433, Chiara Zurzolo and co-workers provide new evidence to support the hypothesis that detergent-resistant microdomains (DRMs, sometimes called lipid rafts) in the endoplasmic reticulum (ER) are important for the correct folding of PrP. They have investigated the intracellular synthesis, degradation and localization of PrPT182A, a PrP mutant associated with Creutzfeldt-Jakob disease, an inherited human prion disease. They show that PrPT182A is retained in the ER, where it is mainly associated with DRMs. Moreover, they demonstrate that misfolded PrPT182A is not degraded by the proteosome, arguing against the hypothesis that impaired proteosomal degradation causes cytosolic accumulation of neurotoxic PrP molecules in prion diseases. Finally, they show that cholesterol depletion impairs the association of PrPT182A with DRMs and increases its misfolding. Thus, the authors conclude, DRMs may protect cells against the pathological misfolding of PrP mutants.


Related articles in JCS:

Detergent-resistant membrane domains but not the proteasome are involved in the misfolding of a PrP mutant retained in the endoplasmic reticulum
Vincenza Campana, Daniela Sarnataro, Carlo Fasano, Philippe Casanova, Simona Paladino, and Chiara Zurzolo
JCS 2006 119: 433-442. [Abstract] [Full Text]  




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