Prion topology and toxicity

Adriano Aguzzi; Andrew D Steele

doi:10.1016/j.cell.2009.05.041

Prion topology and toxicity

Cell. 2009 Jun 12;137(6):994-6. doi: 10.1016/j.cell.2009.05.041.

Authors

Adriano Aguzzi¹, Andrew D Steele

Affiliation

¹ Institute of Neuropathology, University Hospital Zurich, Zurich, Switzerland. [email protected]

PMID: 19524502
DOI: 10.1016/j.cell.2009.05.041

Abstract

Inactivation of mahogunin, an E3 ubiquitin ligase, causes a spongiform encephalopathy resembling prion disease. Chakrabarti and Hegde (2009) now report that prion proteins with aberrant topologies inactivate mahogunin, providing a plausible explanation for certain aspects of prion pathology.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Animals
Humans
Mice
PrPC Proteins / chemistry
PrPC Proteins / metabolism*
Prion Diseases / metabolism*
Ubiquitin-Protein Ligases / chemistry
Ubiquitin-Protein Ligases / metabolism

Substances

PrPC Proteins
MGRN1 protein, human
Mgrn1 protein, mouse
Ubiquitin-Protein Ligases