Evidence map›Paper›PMID 21085490›Full record

ArticlePloS one2010

Protein kinase A binds and activates heat shock factor 1.

Ayesha Murshid, Shiuh-Dih Chou, Thomas Prince, Yue Zhang, Ajit Bharti, Stuart K Calderwood

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

52 citing papers in PubMed, 79 citations in OpenAlex.

  1. Adaptation to heat stress by diversification of the vertebrate heat shock transcription factor family.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026
    Review
  2. Article
  3. Divergent condensates tune transcriptional responses during stress.bioRxiv : the preprint server for biology · 2026
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Monitoring of the Heat Shock Response with a Real-Time Luciferase Reporter.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  9. Review
  10. Article
  11. Review
  12. Heat Shock Proteins and HSF1 in Cancer.Frontiers in oncology · 2022
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Ayesha MurshidMolecular and Cellular Radiation Oncology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, Massachusetts, United States of America.
Shiuh-Dih Chou
Thomas Prince
Yue Zhang
Ajit Bharti
Stuart K Calderwood
Beth Israel Deaconess Medical Center · USHarvard University · USBoston University · US

Funding

TRANSMEMBRANE SIGNAL MODULATION BY HYPERTHERMIAR01CA047407 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1988 to 2014
$4.3M
Gene repression by HSF1 during hyperthermia and other stresses.R01CA077465 · NCI · DANA-FARBER CANCER INSTITUTE · PI CALDERWOOD, STUART KEITH · 1998 to 2011
$1.5M
NCI NIH HHS 2R01CA047407NCI NIH HHS R01 CA047407NCI NIH HHS R01 CA077465NCI NIH HHS R01CA077465
6 · The paper itself

Abstract

backgroundMany inducible transcription factors are regulated through batteries of posttranslational modifications that couple their activity to inducing stimuli. We have studied such regulation of Heat Shock Factor 1 (HSF1), a key protein in control of the heat shock response, and a participant in carcinogenisis, neurological health and aging. As the mechanisms involved in the intracellular regulation of HSF1 in good health and its dysregulation in disease are still incomplete we are investigating the role of posttranslational modifications in such regulation. METHODOLOGY/PRINCIPAL

findingsIn a proteomic study of HSF1 binding partners, we have discovered its association with the pleiotropic protein kinase A (PKA). HSF1 binds avidly to the catalytic subunit of PKA, (PKAcα) and becomes phosphorylated on a novel serine phosphorylation site within its central regulatory domain (serine 320 or S320), both in vitro and in vivo. Intracellular PKAcα levels and phosphorylation of HSF1 at S320 were both required for HSF1 to be localized to the nucleus, bind to response elements in the promoter of an HSF1 target gene (hsp70.1) and activate hsp70.1 after stress. Reduction in PKAcα levels by small hairpin RNA led to HSF1 exclusion from the nucleus, its exodus from the hsp70.1 promoter and decreased hsp70.1 transcription. Likewise, null mutation of HSF1 at S320 by alanine substitution for serine led to an HSF1 species excluded from the nucleus and deficient in hsp70.1 activation.

conclusionsThese findings of PKA regulation of HSF1 through S320 phosphorylation add to our knowledge of the signaling networks converging on this factor and may contribute to elucidating its complex roles in the stress response and understanding HSF1 dysregulation in disease.

Indexed as

Amino Acid SubstitutionBinding SitesCatalytic DomainCell Line, TumorCell NucleusCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsGreen Fluorescent ProteinsHeat Shock Transcription FactorsHEK293 CellsHeLa CellsHSP70 Heat-Shock ProteinsHumansImmunoblottingImmunoprecipitationMicroscopy, ConfocalCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsGreen Fluorescent Proteinsheat-shock protein 70.1Heat Shock Transcription FactorsHSF1 protein, humanHSP70 Heat-Shock ProteinsSerineTranscription Factors

Identifiers

PMID21085490
PMCPMC2976705
OpenAlexW2156771687

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.