ArticleCurrent genetics2020
A functional unfolded protein response is required for chronological aging in Saccharomyces cerevisiae.
Article in Current genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Black Tea Aqueous Extract Extends Yeast Longevity via Antioxidant Gene Activation: Transcriptomic Analysis of Anti-Aging Mechanisms.Food science & nutrition · 2025Article
- Metformin modulates the unfolded protein responses, altering lifespan and health-promoting effects in UPR-activated worms.PloS one · 2025Article
- Longevity control by supersulfide-mediated mitochondrial respiration and regulation of protein quality.Redox biology · 2024Article
- Article
- Fundamental and Applicative Aspects of the Unfolded Protein Response in Yeasts.Journal of fungi (Basel, Switzerland) · 2023Review
- The Effect of Calorie Restriction on Protein Quality Control in Yeast.Biomolecules · 2023Review
- EIF5A2 specifically regulates the transcription of aging-related genes in human neuroblastoma cells.BMC geriatrics · 2023Article
- Tra1 controls the transcriptional landscape of the aging cell.G3 (Bethesda, Md.) · 2023Article
- Translational control in cell ageing: an update.Biochemical Society transactions · 2021Review
- Review
- Does Inter-Organellar Proteostasis Impact Yeast Quality and Performance During Beer Fermentation?Frontiers in genetics · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Progressive impairment of proteostasis and accumulation of toxic misfolded proteins are associated with the cellular aging process. Here, we employed chronologically aged yeast cells to investigate how activation of the unfolded protein response (UPR) upon accumulation of misfolded proteins in the endoplasmic reticulum (ER) affects lifespan. We found that cells lacking a functional UPR display a significantly reduced chronological lifespan, which contrasts previous findings in models of replicative aging. We find exacerbated UPR activation in aged cells, indicating an increase in misfolded protein burden in the ER during the course of aging. We also observed that caloric restriction, which promotes longevity in various model organisms, extends lifespan of UPR-deficient strains. Similarly, aging in pH-buffered media extends lifespan, albeit independently of the UPR. Thus, our data support a role for caloric restriction and reduced acid stress in improving ER homeostasis during aging. Finally, we show that UPR-mediated upregulation of the ER chaperone Kar2 and functional ER-associated degradation (ERAD) are essential for proper aging. Our work documents the central role of secretory protein homeostasis in chronological aging in yeast and highlights that the requirement for a functional UPR can differ between post-mitotic and actively dividing eukaryotic cells.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.