ArticleScientific reports2019
Rapid deacetylation of yeast Hsp70 mediates the cellular response to heat stress.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- Dynamic global acetylation remodeling during the yeast heat shock response.Genome biology · 2026Article
- Deacetylation of HSC70 by SIRT2 promotes chaperone mediated autophagy.Autophagy reports · 2025Article
- Exogenous Trehalose AssistsJournal of fungi (Basel, Switzerland) · 2024Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.PLoS genetics · 2024Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.bioRxiv : the preprint server for biology · 2024Article
- High Glucose Is a Stimulation Signal of the Salt-Tolerant YeastJournal of fungi (Basel, Switzerland) · 2024Article
- Rewiring regulation on respiro-fermentative metabolism relieved Crabtree effects inSynthetic and systems biotechnology · 2022Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
- MicroRNA-570 targets the HSP chaperone network, increases proteotoxic stress and inhibits mammary tumor cell migration.Scientific reports · 2022Article
- Quantitative Proteomic Analysis Reveals Important Roles of the Acetylation of ER-Resident Molecular Chaperones for Conidiation in Fusarium oxysporum.Molecular & cellular proteomics : MCP · 2022Article
- Regulation of heat shock proteins 70 and their role in plant immunity.Journal of experimental botany · 2022Review
- Bioactivity Profiles of Cytoprotective Short-Chain Quinones.Molecules (Basel, Switzerland) · 2021Article
- Molecular Chaperones: Molecular Assembly Line Brings Metabolism and Immunity in Shape.Metabolites · 2020Review
- Post-translational modifications of Hsp70 family proteins: Expanding the chaperone code.The Journal of biological chemistry · 2020Review
- Host expression system modulates recombinant Hsp70 activity through post-translational modifications.The FEBS journal · 2020Article
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Authors and funding
10 authors at 5 institutions in 4 countries.
Funding
Abstract
Hsp70 is a highly conserved molecular chaperone critical for the folding of new and denatured proteins. While traditional models state that cells respond to stress by upregulating inducible HSPs, this response is relatively slow and is limited by transcriptional and translational machinery. Recent studies have identified a number of post-translational modifications (PTMs) on Hsp70 that act to fine-tune its function. We utilized mass spectrometry to determine whether yeast Hsp70 (Ssa1) is differentially modified upon heat shock. We uncovered four lysine residues on Ssa1, K86, K185, K354 and K562 that are deacetylated in response to heat shock. Mutation of these sites cause a substantial remodeling of the Hsp70 interaction network of co-chaperone partners and client proteins while preserving essential chaperone function. Acetylation/deacetylation at these residues alter expression of other heat-shock induced chaperones as well as directly influencing Hsf1 activity. Taken together our data suggest that cells may have the ability to respond to heat stress quickly though Hsp70 deacetylation, followed by a slower, more traditional transcriptional response.
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Registered trials
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