ArticleMolecular and cellular biology2003
Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 149 papers.
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Who cites it
149 citing papers in PubMed, 310 citations in OpenAlex.
- Emergent 3D genome reorganization and graded gene control from the stepwise assembly of transcriptional condensates.Cell reports · 2026Article
- MPC-mediated lactate production drives histone lactylation in dendritic cells to affect tumor progression and immunotherapy.Cellular and molecular life sciences : CMLS · 2025Article
- SUMOylation is not a prerequisite for HSF1's role in stress protection and transactivation.Scientific reports · 2025Article
- HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025Review
- Exploring mitochondrial dynamics and localization under cellular stress: A comprehensive insight.Journal of biosciences · 2025Review
- Review
- Mitochondrial Thermogenesis Can Trigger Heat Shock Response in the Nucleus.ACS central science · 2024Article
- Disrupted HSF1 regulation in normal and exceptional brain aging.Biogerontology · 2024Article
- HSF1 at the crossroads of chemoresistance: from current insights to future horizons in cell death mechanisms.Frontiers in cell and developmental biology · 2024Review
- Kainic Acid-Induced Excitotoxicity Leads to the Activation of Heat Shock Response.Molecular neurobiology · 2023Article
- Thermosensitive SUMOylation of TaHsfA1 defines a dynamic ON/OFF molecular switch for the heat stress response in wheat.The Plant cell · 2023Article
- Article
- HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023Review
- Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022Review
- Protein Kinase CK2 and Its Potential Role as a Therapeutic Target in Huntington's Disease.Biomedicines · 2022Review
- Binding of the HSF-1 DNA-binding domain to multimeric C. elegans consensus HSEs is guided by cooperative interactions.Scientific reports · 2022Article
- Network Theoretical Approach to Explore Factors Affecting Signal Propagation and Stability in Dementia's Protein-Protein Interaction Network.Biomolecules · 2022Article
- Reversible phase separation of HSF1 is required for an acute transcriptional response during heat shock.Nature cell biology · 2022Article
- SUMOylation inhibition enhances dexamethasone sensitivity in multiple myeloma.Journal of experimental & clinical cancer research : CR · 2022Article
- HSF-1: Guardian of the Proteome Through Integration of Longevity Signals to the Proteostatic Network.Frontiers in aging · 2022Review
89 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heat shock response, which is accompanied by a rapid and robust upregulation of heat shock proteins (Hsps), is a highly conserved protection mechanism against protein-damaging stress. Hsp induction is mainly regulated at transcriptional level by stress-inducible heat shock factor 1 (HSF1). Upon activation, HSF1 trimerizes, binds to DNA, concentrates in the nuclear stress granules, and undergoes a marked multisite phosphorylation, which correlates with its transcriptional activity. In this study, we show that HSF1 is modified by SUMO-1 and SUMO-2 in a stress-inducible manner. Sumoylation is rapidly and transiently enhanced on lysine 298, located in the regulatory domain of HSF1, adjacent to several critical phosphorylation sites. Sumoylation analyses of HSF1 phosphorylation site mutants reveal that specifically the phosphorylation-deficient S303 mutant remains devoid of SUMO modification in vivo and the mutant mimicking phosphorylation of S303 promotes HSF1 sumoylation in vitro, indicating that S303 phosphorylation is required for K298 sumoylation. This finding is further supported by phosphopeptide mapping and analysis with S303/7 phosphospecific antibodies, which demonstrate that serine 303 is a target for strong heat-inducible phosphorylation, corresponding to the inducible HSF1 sumoylation. A transient phosphorylation-dependent colocalization of HSF1 and SUMO-1 in nuclear stress granules provides evidence for a strictly regulated subnuclear interplay between HSF1 and SUMO.
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