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XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
Open accessAbstract
Mutations in superoxide dismutase-1 (SOD1) cause familial amyotrophic lateral sclerosis (fALS). Recent evidence implicates adaptive responses to endoplasmic reticulum (ER) stress in the disease process via a pathway known as the unfolded protein response (UPR). Here, we investigated the contribution to fALS of X-box-binding protein-1 (XBP-1), a key UPR transcription factor that regulates genes involved in protein folding and quality control. Despite expectations that XBP-1 deficiency would enhance the pathogenesis of mutant SOD1, we observed a dramatic decrease in its toxicity due to an enhanced clearance of mutant SOD1 aggregates by macroautophagy, a cellular pathway involved in lysosome-mediated protein degradation. To validate these observations in vivo, we generated mutant SOD1 transgenic mice with specific deletion of XBP-1 in the nervous system. XBP-1-deficient mice were more resistant to developing disease, correlating with increased levels of autophagy in motoneurons and reduced accumulation of mutant SOD1 aggregates in the spinal cord. Post-mortem spinal cord samples from patients with sporadic ALS and fALS displayed a marked activation of both the UPR and autophagy. Our results reveal a new function of XBP-1 in the control of autophagy and indicate critical cross-talk between these two signaling pathways that can provide protection against neurodegeneration.
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“antagonizing the unfolded protein response (UPR) through deletion of XBP1 [335] triggers autophagy and the clearance of SOD1 inclusions, in the process delaying disease onset and improving survival.”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [335]
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“Conversely, genetic interventions that promote autophagy, such as the inactivation of the transcription factor XBP1 (X‐box binding protein 1) or restoration of HSPB8 expression in the nervous system, counteract ALS symptomatology by promoting the autophagy‐dependent disposal of SOD1G93A (Hetz et al, 2009; Crippa et al, 2010).”
From Autophagy in major human diseases (2021) · cites this paper as Hetz et al, 2009
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Metadata
- Authors
- Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A. M., Brown, R. H., & Glimcher, L. H.
- Affiliations
- Harvard University (US)
- University of Chile (CL)
- Pontificia Universidad Católica de Chile (CL)
- Albert Einstein College of Medicine (US)
- Massachusetts General Hospital (US)
- ORCID
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2009-09-17
- Volume
- 23
- Issue
- 19
- Pages
- 2294-2306
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC2758741
- OpenAlex
- W2149927906
- Cited by
- 530
- References
- 53
- Citations by year
- 2026: 8 · 2025: 17 · 2024: 17 · 2023: 15 · 2022: 25 · 2021: 32 · 2020: 28 · 2019: 28 · 2018: 35 · 2017: 43 · 2016: 46 · 2015: 48 · 2014: 35 · 2013: 44 · 2012: 44
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Americanae (AECID Library) (submittedVersion, other-oa)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, other-oa)
- HighWire Press Open Archive (submittedVersion)
- Universidad de Chile (submittedVersion, cc-by-nc-nd)
- Funders
- Michael J. Fox Foundation for Parkinson's Research
- ALS Association
- National Parkinson Foundation
- Muscular Dystrophy Association
- ALS Therapy Alliance
- Cure Huntington's Disease Initiative
- Broad Institute
- National Institutes of Health (AG031782)
- Parkinsonfonden
- Comisión Nacional de Investigación Científica y Tecnológica
- National Institute on Aging (P01AG031782, AG031782)
- National Institute of Allergy and Infectious Diseases (AI 32412, R01AI032412)
- Fondo de Financiamiento de Centros de Investigación en Áreas Prioritarias (15010006)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- XBP1, amyotrophic lateral sclerosis, SOD1, unfolded protein response, endoplasmic reticulum stress, autophagy, macroautophagy, protein aggregate clearance, motor neurons, neuroprotection, transgenic mice, sporadic ALS, neurodegeneration
- MeSH terms
- Regulatory Factor X Transcription Factors, X-Box Binding Protein 1, Superoxide Dismutase-1, Amyotrophic Lateral Sclerosis, Animals, Autophagy, DNA-Binding Proteins, Endoribonucleases, Female, Humans, Longevity, Male, Mice, Transgenic, Nervous System, Spinal Cord, Superoxide Dismutase, Transcription Factors, Up-Regulation, Protein Serine-Threonine Kinases, Mice, Gene Knockdown Techniques
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