ArticleScientific reports2017
Recurrent background mutations in WHI2 impair proteostasis and degradation of misfolded cytosolic proteins in Saccharomyces cerevisiae.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The Whi2-Psr1-Psr2 complex selectively regulates TORC1 and autophagy under low leucine conditions but not nitrogen depletion.Autophagy · 2025Article
- The Effect of Calorie Restriction on Protein Quality Control in Yeast.Biomolecules · 2023Review
- Article
- Genetic interaction network has a very limited impact on the evolutionary trajectories in continuous culture-grown populations of yeast.BMC ecology and evolution · 2021Article
- Suppressors of mRNA Decapping Defects Restore Growth Without Major Effects on mRNA Decay Rates or Abundance.Genetics · 2020Article
- The Whi2p-Psr1p/Psr2p complex regulates interference competition and expansion of cells with competitive advantage in yeast colonies.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Unique genetic basis of the distinct antibiotic potency of high acetic acid production in the probiotic yeastGenome research · 2019Article
- Whi2: a new player in amino acid sensing.Current genetics · 2019Review
- WHI-2 Regulates Intercellular Communication via a MAP Kinase Signaling Complex.Frontiers in microbiology · 2019Article
- Whi2 signals low leucine availability to halt yeast growth and cell death.FEMS yeast research · 2018Review
- Whi2 is a conserved negative regulator of TORC1 in response to low amino acids.PLoS genetics · 2018Article
- Article
- Unintended Side Effects of Transformation Are Very Rare inG3 (Bethesda, Md.) · 2018Article
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3 authors.
Funding
Abstract
Proteostasis promotes viability at both the cellular and organism levels by maintaining a functional proteome. This requires an intricate protein quality control (PQC) network that mediates protein folding by molecular chaperones and removes terminally misfolded proteins via the ubiquitin proteasome system and autophagy. How changes within the PQC network can perturb proteostasis and shift the balance between protein folding and proteolysis remain poorly understood. However, given that proteostasis is altered in a number of conditions such as cancer and ageing, it is critical that we identify the factors that mediate PQC and understand the interplay between members of the proteostatic network. In this study, we investigated the degradation of a thermally unstable cytosolic model substrate and identified a surprisingly high number of strains in the yeast knockout collection that displayed impaired turnover of the misfolded substrate. We found that this phenotype was caused by frequent background mutations in the general stress response gene WHI2. We linked this proteostatic defect to the lack of activity of the stress response transcription factor Msn2, potentially under conditions where the TOR pathway is active. Our results underscore how changes to the elaborate PQC network can perturb proteostasis and impair degradation of misfolded cytosolic proteins.
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