ArticleAging cell2013
Caenorhabditis elegans HSF-1 is an essential nuclear protein that forms stress granule-like structures following heat shock.
Article in Aging cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed.
- Turnera diffusa polysaccharides promote healthy aging through conserved stress response regulation and metabolic remodeling across multiple aging models.Biogerontology · 2026Article
- SVHRSP Attenuates PTZ-Induced Seizure-Like Behavior in C. elegans: Involvement of HSF-1 and Associated Changes in GABAergic Markers and Mitochondrial Homeostasis.Neurochemical research · 2026Article
- Gene- and Isoform-Level Responses to Extreme Acidic pH Stress in an Emerging Marine Invertebrate Model OrganismAntioxidants (Basel, Switzerland) · 2026Article
- Proteostasis Rebalancing by LET-607 Deficiency Promotes Longevity.Aging cell · 2026Article
- Reduced Proteasome Degradation of HSF-1 Shifts Protein Stress Management With Age in Caenorhabditis elegans.Aging cell · 2026Article
- The heat shock factor Cbr-HSF-1 is necessary for lifespan maintenance inmicroPublication biology · 2026Article
- Herbal Cuscutae Semen Contributes to Oxidative Stress Tolerance and Extends Lifespan via Sirtuin1 inAntioxidants (Basel, Switzerland) · 2025Article
- Heat tolerance and genetic adaptations in Caenorhabditis briggsae: insights from comparative studies with Caenorhabditis elegans.Genetics · 2025Article
- Transposable Elements Drive Regulatory and Functional Innovation of F-box Genes.Molecular biology and evolution · 2025Article
- The neurohormone tyramine stimulates the secretion of an insulin-like peptide from the Caenorhabditis elegans intestine to modulate the systemic stress response.PLoS biology · 2025Article
- Article
- Regulatory mechanism of cold-inducible diapause in Caenorhabditis elegans.Nature communications · 2024Article
- Lysosome-related organelles promote stress and immune responses in C. elegans.Communications biology · 2023Article
- Amphid sensory neurons ofLife science alliance · 2023Article
- Article
- Organismal Roles of Hsp90.Biomolecules · 2023Review
- Lack of peroxisomal catalase affects heat shock response inLife science alliance · 2023Article
- The Thermal Stress Coping Network of the NematodeInternational journal of molecular sciences · 2022Review
- Cabin1 domain-containing gene picd-1 interacts with pry-1/Axin to regulate multiple processes in Caenorhabditis elegans.Scientific reports · 2022Article
- Auxin-Inducible Degron System Reveals Temporal-Spatial Roles of HSF-1 and Its Transcriptional Program in Lifespan Assurance.Frontiers in aging · 2022Article
10 more citing papers are in PubMed but not listed here.
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2 authors.
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Abstract
The heat shock transcription factor (HSF) is a conserved regulator of heat shock-inducible gene expression. Organismal roles for HSF in physiological processes such as development, aging, and immunity have been defined largely through studies of the single Caenorhabditis elegans HSF homolog, hsf-1. However, the molecular and cell biological properties of hsf-1 in C. elegans are incompletely understood. We generated animals expressing physiological levels of an HSF-1::GFP fusion protein and examined its function, localization, and regulation in vivo. HSF-1::GFP was functional, as measured by its ability to rescue phenotypes associated with two hsf-1 mutant alleles. Rescue of hsf-1 development phenotypes was abolished in a DNA-binding-deficient mutant, demonstrating that the transcriptional targets of hsf-1 are critical to its function even in the absence of stress. Under nonstress conditions, HSF-1::GFP was found primarily in the nucleus. Following heat shock, HSF-1::GFP rapidly and reversibly redistributed into dynamic, subnuclear structures that share many properties with human nuclear stress granules, including colocalization with markers of active transcription. Rapid formation of HSF-1 stress granules required HSF-1 DNA-binding activity, and the threshold for stress granule formation was altered by growth temperature. HSF-1 stress granule formation was not induced by inhibition of IGF signaling, a pathway previously suggested to function upstream of hsf-1. Our findings suggest that development, stress, and aging pathways may regulate HSF-1 function in distinct ways, and that HSF-1 nuclear stress granule formation is an evolutionarily conserved aspect of HSF-1 regulation in vivo.
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