ArticleNature communications2020
Sis1 potentiates the stress response to protein aggregation and elevated temperature.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 46 citations in OpenAlex.
- FBXL21 regulates diurnal proteostasis in skeletal muscle by targeting DNAJB6 and client proteins.EMBO reports · 2026Article
- Mitochondrial respiration modulates Hsf1 activation and the heat shock response.bioRxiv : the preprint server for biology · 2026Article
- Identification of the Integration/Excision Module and Regulatory Elements Involved in the Mobility of IME8, an Integrative and Mobilizable Element From Mosquitocidal Lysinibacillus sphaericus.Microbial biotechnology · 2026Article
- Physiological architecture and evolutionary origins of cellular adaptability.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms and regulation of the Hsp70 chaperone network.Nature reviews. Molecular cell biology · 2026Review
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Hsp70 chaperones, Ssa1 and Ssa2, limit poly(A) binding protein aggregation.Molecular biology of the cell · 2025Article
- Specific branches of the proteostasis network regulate the toxicity associated with mistranslation.Nucleic acids research · 2025Article
- The formation of chaperone-rich GET bodies depends on the tetratricopeptide repeat region of Sgt2 and is reversed by NADH.Journal of cell science · 2025Article
- Engineering a membrane protein chaperone to ameliorate the proteotoxicity of mutant huntingtin.Nature communications · 2025Article
- Preserve or destroy: Orphan protein proteostasis and the heat shock response.The Journal of cell biology · 2024Review
- The Heat Shock Response as a Condensate Cascade.Journal of molecular biology · 2024Review
- Clearing the JUNQ: the molecular machinery for sequestration, localization, and degradation of the JUNQ compartment.Frontiers in molecular biosciences · 2024Article
- Adaptive preservation of orphan ribosomal proteins in chaperone-dispersed condensates.Nature cell biology · 2023Article
- Global quantitative understanding of non-equilibrium cell fate decision-making in response to pheromone.iScience · 2023Article
- Transcriptional regulation of Sis1 promotes fitness but not feedback in the heat shock response.eLife · 2023Article
- Identification of subfunctionalized aggregate-remodeling J-domain proteins in Arabidopsis thaliana.Journal of experimental botany · 2023Article
- Article
- Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells adapt to conditions that compromise protein conformational stability by activating various stress response pathways, but the mechanisms used in sensing misfolded proteins remain unclear. Moreover, aggregates of disease proteins often fail to induce a productive stress response. Here, using a yeast model of polyQ protein aggregation, we identified Sis1, an essential Hsp40 co-chaperone of Hsp70, as a critical sensor of proteotoxic stress. At elevated levels, Sis1 prevented the formation of dense polyQ inclusions and directed soluble polyQ oligomers towards the formation of permeable condensates. Hsp70 accumulated in a liquid-like state within this polyQ meshwork, resulting in a potent activation of the HSF1 dependent stress response. Sis1, and the homologous DnaJB6 in mammalian cells, also regulated the magnitude of the cellular heat stress response, suggesting a general role in sensing protein misfolding. Sis1/DnaJB6 functions as a limiting regulator to enable a dynamic stress response and avoid hypersensitivity to environmental changes.
Indexed as
Identifiers
What OpenQuestion holds
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.