Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
Open accessAbstract
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.
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Disturbance of endoplasmic reticulum function is emerging as a relevant factor driving neurodegeneration in Alzheimer's disease.
“Disturbance of endoplasmic reticulum (ER) function is emerging as a relevant factor driving neurodegeneration in Alzheimer’s disease77.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [77]
Aβ oligomers have also been proposed to cause ER dysfunction leading to UPR-mediated neurotoxicity and neuronal cell death.
“Conversely, Aβ oligomers have also been proposed to cause ER dysfunction leading to UPR mediated neurotoxicity and neuronal cell death77.”
From Chlamydia pneumoniae can infect the central nervous system via the olfactory and trigeminal nerves and contributes to Alzheimer’s disease risk (2022) · cites this paper as [77]
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- Authors
- Hetz, C., & Mollereau, B.
- Affiliations
- Neurounion Biomedical Foundation (CL)
- École Normale Supérieure de Lyon (FR)
- Corresponding author
- Hetz, Claudio
- Mollereau, Bertrand
- Venue
- Nature Reviews Neuroscience
- Published
- 2014-03-12
- Volume
- 15
- Issue
- 4
- Pages
- 233-249
- ISSN
- 1471-003X (ISSN-L)
- 1471-0048
- OpenAlex
- W2037950411
- Cited by
- 684
- References
- 11
- Citations by year
- 2026: 28 · 2025: 40 · 2024: 40 · 2023: 40 · 2022: 47 · 2021: 35 · 2020: 67 · 2019: 33 · 2018: 68 · 2017: 91 · 2016: 84 · 2015: 83 · 2014: 27
- FWCI
- 9.55
- Type
- journal article
- Language
- en
- Open access
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Nature reviews. Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (publishedVersion, other-oa)
- HAL (submittedVersion)
- Americanae (AECID Library) (submittedVersion, other-oa)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, other-oa)
- Universidad de Chile (submittedVersion, cc-by-nc-nd)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- unfolded protein response, endoplasmic reticulum stress, neurodegenerative diseases, ER proteostasis, misfolded proteins, neuronal function, nervous system
- MeSH terms
- Animals, Endoplasmic Reticulum, Homeostasis, Humans, Stress, Physiological, Neurodegenerative Diseases, Unfolded Protein Response
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