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Nat Rev Neurosci. 2014 Apr;15(4):233-49. doi: 10.1038/nrn3689. Epub 2014 Mar 12.

Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases.

Author information

1
1] Biomedical Neuroscience Institute, Faculty of Medicine, University of Chile, Santiago, Chile. [2] Institute of Biomedical Sciences, Center for Molecular Studies of the Cell, Program of Cellular and Molecular Biology, University of Chile, Santiago, Chile. [3] Neurounion Biomedical Foundation, Santiago, Chile. [4] Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, Massachusetts 02115, USA.
2
Laboratory of Molecular Biology of the Cell, CNRS UMR5239, Ecole Normale Supérieure de Lyon, UMS3444 Biosciences Lyon Gerland, University of Lyon, Lyon 69364, France.

Abstract

The unfolded protein response (UPR) is a homeostatic mechanism by which cells regulate levels of misfolded proteins in the endoplasmic reticulum (ER). Although it is well characterized in non-neuronal cells, a proliferation of papers over the past few years has revealed a key role for the UPR in normal neuronal function and as an important driver of neurodegenerative diseases. A complex scenario is emerging in which distinct UPR signalling modules have specific and even opposite effects on neurodegeneration depending on the disease context. Here, we provide an overview of the most recent findings addressing the biological relevance of ER stress in the nervous system.

PMID:
24619348
DOI:
10.1038/nrn3689
[Indexed for MEDLINE]
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