ArticleMolecular biology of the cell2016
Cytosolic splice isoform of Hsp70 nucleotide exchange factor Fes1 is required for the degradation of misfolded proteins in yeast.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 43 citations in OpenAlex.
- Co-chaperones fine-tune the function of heat shock protein 70 (Hsp70), whether to fold, hold, or degrade substrates in ensuring cellular protein homeostasis.Journal of biosciences · 2025Review
- Feedback control of the heat shock response by spatiotemporal regulation of Hsp70.The Journal of cell biology · 2024Article
- Chp1 is a dedicated chaperone at the ribosome that safeguards eEF1A biogenesis.Nature communications · 2024Article
- Article
- Feedback control of the heat shock response by spatiotemporal regulation of Hsp70.bioRxiv : the preprint server for biology · 2024Article
- Contribution of the yeast bi-chaperone system in the restoration of the RNA helicase Ded1 and translational activity under severe ethanol stress.The Journal of biological chemistry · 2023Article
- Genetic inactivation of essentialMolecular biology of the cell · 2023Article
- Distribution, expression of hexaploid wheatFrontiers in plant science · 2022Article
- Regulation of alternative splicing in response to temperature variation in plants.Journal of experimental botany · 2021Review
- OsFes1C, a potential nucleotide exchange factor for OsBiP1, is involved in the ER and salt stress responses.Plant physiology · 2021Article
- Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.Experimental biology and medicine (Maywood, N.J.) · 2021Review
- SCRaMbLE: A Study of Its Robustness and Challenges through Enhancement of Hygromycin B Resistance in a Semi-Synthetic Yeast.Bioengineering (Basel, Switzerland) · 2021Article
- Acquired Resistance to Severe Ethanol Stress in Saccharomyces cerevisiae Protein Quality Control.Applied and environmental microbiology · 2021Article
- Cloning and activity analysis of the promoter of nucleotide exchange factor gene ZjFes1 from the seagrasses Zostera japonica.Scientific reports · 2020Article
- Origin, conservation, and loss of alternative splicing events that diversify the proteome in Saccharomycotina budding yeasts.RNA (New York, N.Y.) · 2020Article
- Heat-stress induced expression of stress-inducible nucleotide exchange factor Fes1 in seagrass Zostera japonica.Ecotoxicology (London, England) · 2020Article
- Genetic Selection Based on a Ste6G3 (Bethesda, Md.) · 2020Article
- BRF Negatively Regulates Thermotolerance Defect ofFrontiers in plant science · 2020Article
- Cellular sequestrases maintain basal Hsp70 capacity ensuring balanced proteostasis.Nature communications · 2019Article
- Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.Current genetics · 2019Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells maintain proteostasis by selectively recognizing and targeting misfolded proteins for degradation. InSaccharomyces cerevisiae, the Hsp70 nucleotide exchange factor Fes1 is essential for the degradation of chaperone-associated misfolded proteins by the ubiquitin-proteasome system. Here we show that theFES1transcript undergoes unique 3' alternative splicing that results in two equally active isoforms with alternative C-termini, Fes1L and Fes1S. Fes1L is actively targeted to the nucleus and represents the first identified nuclear Hsp70 nucleotide exchange factor. In contrast, Fes1S localizes to the cytosol and is essential to maintain proteostasis. In the absence of Fes1S, the heat-shock response is constitutively induced at normally nonstressful conditions. Moreover, cells display severe growth defects when elevated temperatures, amino acid analogues, or the ectopic expression of misfolded proteins, induce protein misfolding. Importantly, misfolded proteins are not targeted for degradation by the ubiquitin-proteasome system. These observations support the notion that cytosolic Fes1S maintains proteostasis by supporting the removal of toxic misfolded proteins by proteasomal degradation. This study provides key findings for the understanding of the organization of protein quality control mechanisms in the cytosol and nucleus.
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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.