The DOI matches its Crossref record; 115 of the 143 references it cites were found in a registry or an index, and 28 are not checked yet.
The unfolded protein response and cellular senescence. A Review in the Theme: Cellular Mechanisms of Endoplasmic Reticulum Stress Signaling in Health and Disease
Abstract
The endoplasmic reticulum (ER) is a multifunctional organelle critical for the proper folding and assembly of secreted and transmembrane proteins. Perturbations of ER functions cause ER stress, which activates a coordinated system of transcriptional and translational controls called the unfolded protein response (UPR), to cope with accumulation of misfolded proteins and proteotoxicity. It results in ER homeostasis restoration or in cell death. Senescence is a complex cell phenotype induced by several stresses such as telomere attrition, DNA damage, oxidative stress, and activation of some oncogenes. It is mainly characterized by a cell enlargement, a permanent cell-cycle arrest, and the production of a secretome enriched in proinflammatory cytokines and components of the extracellular matrix. Senescent cells accumulate with age in tissues and are suspected to play a role in age-associated diseases. Since senescence is a stress response, the question arises of whether an ER stress could occur concomitantly with senescence and participate in the onset or maintenance of the senescent features. Here, we described the interconnections between the UPR signaling and the different aspects of the cellular senescence programs and discuss the implication of UPR modulations in this context.
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Metadata
- Authors
- Pluquet, O., Pourtier, A., & Abbadie, C.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Corresponding author
- Pluquet, Olivier
- Venue
- American Journal of Physiology-Cell Physiology
- Publisher
- American Physiological Society
- Published
- 2015-03-15
- Volume
- 308
- Issue
- 6
- Pages
- C415-C425
- ISSN
- 0363-6143 (ISSN-L)
- 1522-1563
- OpenAlex
- W2093398011
- Semantic Scholar
- 28aee3c356339845b8920cf8fc965b9d001ce341
- Cited by
- 305
- References
- 143
- Citations by year
- 2026: 21 · 2025: 24 · 2024: 25 · 2023: 29 · 2022: 28 · 2021: 45 · 2020: 38 · 2019: 33 · 2018: 26 · 2017: 21 · 2016: 13 · 2015: 2
- FWCI
- 1.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- American Journal of Physiology-Cell Physiology (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Funders
- Association pour la recherche contre le cancer
- Ligue Contre le Cancer
- Centre national de la recherche scientifique
- Chaire d'excellence Lille2/CNRS
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Aging › Genetics, Aging, and Longevity in Model Organisms
- Keywords
- unfolded protein response, cellular senescence, endoplasmic reticulum stress, ER stress signaling, protein misfolding, proteotoxicity, senescence-associated secretome, age-related diseases, cell cycle arrest, extracellular matrix
- MeSH terms
- Aging, Animals, Endoplasmic Reticulum, Humans, Phenotype, Signal Transduction, Cellular Senescence, Unfolded Protein Response, Endoplasmic Reticulum Stress
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