ArticlePLoS biology2022
Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.
Article in PLoS biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- Endogenous Expression of HSP70 and Thioredoxin-1 During Methamphetamine-Induced Degeneration.Biomedicines · 2026Article
- Novel Insights into the Human Hsc70 Structure by Cross-Linking Mass Spectrometry and Molecular Modeling.Journal of proteome research · 2026Article
- Stabilization of HSP70 by deubiquitinase OTUB1 attenuates sleep deprivation-induced cognitive impairment in mice.Journal of physiology and biochemistry · 2026Article
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- DnaJB1 chaperone inhibits tau aggregation by recognizing its N-terminus.bioRxiv : the preprint server for biology · 2025Article
- PTMs as molecular encoders: reprogramming chaperones into epichaperomes for network control in disease.Trends in biochemical sciences · 2025Review
- Hsp70: A Multifunctional Chaperone in Maintaining Proteostasis and Its Implications in Human Disease.Cells · 2025Review
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.PLoS genetics · 2024Article
- Oxidative stress in poultry production.Poultry science · 2024Review
- Article
- Acetylation of the yeast Hsp40 chaperone protein Ydj1 fine-tunes proteostasis and translational fidelity.bioRxiv : the preprint server for biology · 2024Article
- Second international symposium on the chaperone code, 2023.Cell stress & chaperones · 2024Article
- Elucidation of Site-Specific Ubiquitination on Chaperones in Response to Mutant Huntingtin.Cellular and molecular neurobiology · 2023Article
- Understanding chaperone specificity: evidence for a 'client code'.Trends in biochemical sciences · 2023Article
- Second Virtual International Symposium on Cellular and Organismal Stress Responses, September 8-9, 2022.Cell stress & chaperones · 2023Article
- Editorial: Guardians of protein homeostasis (proteostasis) in health, disease and aging.Frontiers in molecular biosciences · 2023Article
- Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones.Frontiers in molecular biosciences · 2023Review
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Authors and funding
19 authors at 9 institutions in 4 countries.
Funding
Abstract
Hsp70 interactions are critical for cellular viability and the response to stress. Previous attempts to characterize Hsp70 interactions have been limited by their transient nature and the inability of current technologies to distinguish direct versus bridged interactions. We report the novel use of cross-linking mass spectrometry (XL-MS) to comprehensively characterize the Saccharomyces cerevisiae (budding yeast) Hsp70 protein interactome. Using this approach, we have gained fundamental new insights into Hsp70 function, including definitive evidence of Hsp70 self-association as well as multipoint interaction with its client proteins. In addition to identifying a novel set of direct Hsp70 interactors that can be used to probe chaperone function in cells, we have also identified a suite of posttranslational modification (PTM)-associated Hsp70 interactions. The majority of these PTMs have not been previously reported and appear to be critical in the regulation of client protein function. These data indicate that one of the mechanisms by which PTMs contribute to protein function is by facilitating interaction with chaperones. Taken together, we propose that XL-MS analysis of chaperone complexes may be used as a unique way to identify biologically important PTMs on client proteins.
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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.