Abstract |
Cellular defense mechanisms, including the unfolded protein response (UPR) and autophagy, attempt to resolve toxic protein aggregates, which are common denominators of neurodegenerative diseases. In this issue of Genes & Development, Hetz and colleagues (pp. 2294-2306) surprisingly show that inhibition of the UPR by knockout of XBP-1 causes a massive increase in autophagy, enhances clearance of superoxide dismutase 1 (SOD1) aggregates, and delays the development of amyotrophic lateral sclerosis. These findings suggest the existence of a homeostatic-if not hormetic-balance between distinct cellular defense mechanisms.
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Authors | Frank Madeo, Tobias Eisenberg, Guido Kroemer |
Journal | Genes & development
(Genes Dev)
Vol. 23
Issue 19
Pg. 2253-9
(Oct 01 2009)
ISSN: 1549-5477 [Electronic] United States |
PMID | 19797764
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Comment)
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Chemical References |
- DNA-Binding Proteins
- Regulatory Factor X Transcription Factors
- SOD1 protein, human
- Transcription Factors
- X-Box Binding Protein 1
- XBP1 protein, human
- Superoxide Dismutase
- Superoxide Dismutase-1
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Topics |
- Aging
(physiology)
- Amyotrophic Lateral Sclerosis
(physiopathology)
- Animals
- Autophagy
(genetics, physiology)
- DNA-Binding Proteins
(genetics, metabolism)
- Gene Knockout Techniques
- Homeostasis
(physiology)
- Humans
- Neurons
(pathology, physiology)
- Regulatory Factor X Transcription Factors
- Superoxide Dismutase
(metabolism)
- Superoxide Dismutase-1
- Transcription Factors
(genetics, metabolism)
- X-Box Binding Protein 1
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