ArticleMolecular and cellular biology2015
Uncoupling Stress-Inducible Phosphorylation of Heat Shock Factor 1 from Its Activation.
Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 104 citations in OpenAlex.
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- The intracellular domain of the epilepsy protein PCDH19 regulates spine density in cortical neurons in vivo viaThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2026Article
- Systematic Optimization of Fragment TLX Ligands toward Agonism and Inverse Agonism.Journal of medicinal chemistry · 2026Article
- The metabolic dysfunction-associated steatohepatitis (MASH) drug resmetirom exhibits broad nuclear receptor activity with minimal functional impact.Scientific reports · 2026Article
- Scaffold Fusion and SAR Transfer with a Chemical Language Model Generates Novel Liver X Receptor Modulators.Journal of medicinal chemistry · 2025Article
- Comparative Profiling and Chemogenomics Application of Chemical Tools for NR4A Nuclear Receptors.Journal of medicinal chemistry · 2025Article
- A guide to heat shock factors as multifunctional transcriptional regulators.The FEBS journal · 2025Review
- Role of HSF1 in cell division, tumorigenesis and therapy: a literature review.Cell division · 2025Review
- Fragment-Based Discovery of Drug-like LRH-1 Agonists.ACS medicinal chemistry letters · 2025Article
- Fatty Acid Mimetic Fragments as Liver Receptor Homologue-1 Modulators.ACS pharmacology & translational science · 2025Article
- Chemogenomics for steroid hormone receptors (NR3).Communications chemistry · 2025Article
- HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025Review
- Structural basis of the human transcriptional Mediator regulated by its dissociable kinase module.Molecular cell · 2024Article
- Human coronaviruses activate and hijack the host transcription factor HSF1 to enhance viral replication.Cellular and molecular life sciences : CMLS · 2024Article
- The Heat Shock Response as a Condensate Cascade.Journal of molecular biology · 2024Review
- Chemogenomics for NR1 nuclear hormone receptors.Nature communications · 2024Article
- The dance of proteostasis and metabolism: Unveiling the caloristatic controlling switch.Cell stress & chaperones · 2024Review
- Article
- Development of a Potent Nurr1 Agonist Tool for In Vivo Applications.Journal of medicinal chemistry · 2023Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In mammals the stress-inducible expression of genes encoding heat shock proteins is under the control of the heat shock transcription factor 1 (HSF1). Activation of HSF1 is a multistep process, involving trimerization, acquisition of DNA-binding and transcriptional activities, which coincide with several posttranslational modifications. Stress-inducible phosphorylation of HSF1, or hyperphosphorylation, which occurs mainly within the regulatory domain (RD), has been proposed as a requirement for HSF-driven transcription and is widely used for assessing HSF1 activation. Nonetheless, the contribution of hyperphosphorylation to the activity of HSF1 remains unknown. In this study, we generated a phosphorylation-deficient HSF1 mutant (HSF1Δ∼PRD), where the 15 known phosphorylation sites within the RD were disrupted. Our results show that the phosphorylation status of the RD does not affect the subcellular localization and DNA-binding activity of HSF1. Surprisingly, under stress conditions, HSF1Δ∼PRD is a potent transactivator of both endogenous targets and a reporter gene, and HSF1Δ∼PRD has a reduced activation threshold. Our results provide the first direct evidence for uncoupling stress-inducible phosphorylation of HSF1 from its activation, and we propose that the phosphorylation signature alone is not an appropriate marker for HSF1 activity.
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