ArticleProceedings of the National Academy of Sciences of the United States of America2009
Trithorax requires Hsp90 for maintenance of active chromatin at sites of gene expression.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 122 citations in OpenAlex.
- Proteostasis of organelles in aging and disease.The FEBS journal · 2026Review
- Heat shock proteins at the crossroads of endosomal trafficking pathways.Cell biology and toxicology · 2025Review
- HSP90 as an evolutionary capacitor drives adaptive eye size reduction via atonal.Nature communications · 2025Article
- Potential therapeutic effects of shrimp protein hydrolysates on NAFLD-induced infertility disorders: Insights into redox balance, heat shock protein expression, and chromatin compaction in male rats.Iranian journal of basic medical sciences · 2025Article
- The Hsp90 Molecular Chaperone as a Global Modifier of the Genotype-Phenotype-Fitness Map: An Evolutionary Perspective.Journal of molecular biology · 2024Review
- Organ transformation by environmental disruption of protein integrity and epigenetic memory in Drosophila.PLoS biology · 2024Article
- Potential Role of DNA Methylation as a Driver of Plastic Responses to the Environment Across Cells, Organisms, and Populations.Genome biology and evolution · 2024Article
- Hsp70 and Hsp90 Elaborately Regulate RNAi Efficiency inInternational journal of molecular sciences · 2023Article
- Impact of Heat Stress on Transposable Element Expression and Derived Small RNAs in Drosophila subobscura.Genome biology and evolution · 2023Article
- Chromatin Immunoprecipitation (ChIP) of Heat Shock Protein 90 (Hsp90).Methods in molecular biology (Clifton, N.J.) · 2023Article
- Quantitative analysis of redox proteome reveals oxidation-sensitive protein thiols acting in fundamental processes of developmental hematopoiesis.Redox biology · 2022Article
- Is there a role for HSF1 in viral infections?FEBS open bio · 2022Review
- Direct targeted therapy for MLL-fusion-driven high-risk acute leukaemias.Clinical and translational medicine · 2022Article
- Heat Shock Proteins and Ferroptosis.Frontiers in cell and developmental biology · 2022Review
- The Role of HSP90 in Preserving the Integrity of Genomes Against Transposons Is Evolutionarily Conserved.Cells · 2021Review
- Polycomb RequiresFrontiers in cell and developmental biology · 2021Article
- The Nutrient-Responsive Molecular Chaperone Hsp90 Supports Growth and Development inFrontiers in physiology · 2021Article
- Kinome-Wide RNAi Screen Uncovers Role of Ballchen in Maintenance of Gene Activation by Trithorax Group inFrontiers in cell and developmental biology · 2021Article
- Article
- The Hsp90 Molecular Chaperone Regulates the Transcription Factor Network Controlling Chromatin Accessibility.Journal of molecular biology · 2019Article
4 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Molecular chaperone heat-shock protein 90 kDa (Hsp90) is known to facilitate the conformational maturation of a diverse range of proteins involved in different signal transduction pathways during development. Recent studies have implicated Hsp90 in transcriptional regulation and an important role for Hsp90 in epigenetic processes has been proposed. Importantly, genetic and pharmacological perturbation of Hsp90 was shown to reveal heritable phenotypic variation and Hsp90 was found to play an important role in buffering genetic and epigenetic variation whose expression led to altered phenotypes. The underlying molecular mechanism remains elusive, however. Here, we show a direct molecular interaction between Hsp90 and Trithorax (Trx). Trx is a member of the TrxG chromatin proteins controlling, together with the members of the Polycomb group, the developmental fate of cells by modulating epigenetic signals. Hsp90 cooperates with Trx at chromatin for maintaining the active expression state of targets like the Hox genes. Pharmacological inhibition of Hsp90 results in degradation of Trx and a concomitant down-regulation of homeotic gene expression. A similar effect is observed with the human orthologue mixed-lineage leukemia. Connecting an epigenetic network controlling major developmental and cellular pathways with a system sensing external cues may explain the rapid fixation and epigenetic inheritance of phenotypic variation as a result of impaired Hsp90.
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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.