ArticleCell stress & chaperones2000
RSK2 represses HSF1 activation during heat shock.
Article in Cell stress & chaperones, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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.
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Who cites it
7 citing papers in PubMed, 27 citations in OpenAlex.
- Role of Heat Shock Factors in Stress-Induced Transcription: An Update.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Role of Heat Shock Factors in Stress-Induced Transcription.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Transformation of eEF1Bδ into heat-shock response transcription factor by alternative splicing.EMBO reports · 2011Article
- The role of heat shock factors in stress-induced transcription.Methods in molecular biology (Clifton, N.J.) · 2011Article
- Signal Transduction Pathways Leading to Heat Shock Transcription.Signal transduction insights · 2010Article
- A transcription cofactor required for the heat-shock response.EMBO reports · 2008Article
- Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1.Molecular and cellular biology · 2003Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Heat shock transcription factor 1(HSF1) activation is a multistep process. The conversion of a latent cytoplasmic form to a nuclear, DNA binding state appears to be activated by nonsteroidal anti-inflammatory drugs. In previous studies, we showed that HSF 1 is phosphorylated by the protein kinase RSK2 in vitro and that this effect is inhibited by nonsteroidal anti-inflammatory drugs at the concentration that leads to the activation of HSF1 in vivo (Stevenson et al 1999). In the present study, using cells from a patient with Coffin-Lowry syndrome (deficient in RSK2), we demonstrate that RSK2 slightly represses activation of HSF1 in vivo at 37 degrees C. In Coffin-Lowry syndrome cells, HSF1-HSE DNA binding activity after treatment with sodium salicylate was slightly higher than that in untreated cells, indicating that although RSK2 is involved in HSF1 regulation, it is not the unique protein kinase that suppresses HSF1-HSE binding activity at 37 degrees C. However, heat shock treatment resulted in significantly higher HSF1-HSE binding activity in Coffin-Lowry syndrome cells as compared with normal controls, suggesting that RSK2 represses HSF1-HSE binding activity during heat shock.
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