Evidence map›Paper›PMID 33268814›Full record

ArticleCell death and differentiation2021

The stress-responsive kinase DYRK2 activates heat shock factor 1 promoting resistance to proteotoxic stress.

Rita Moreno, Sourav Banerjee, Angus W Jackson, Jean Quinn, Gregg Baillie, Jack E Dixon, Albena T Dinkova-Kostova, Joanne Edwards, Laureano de la Vega

Open access · hybridAbstract read
In one paragraph

Article in Cell death and differentiation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Functional Roles of DYRK2 as a Tumor Regulator.Current issues in molecular biology · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  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

9 authors at 3 institutions in 2 countries.

Rita MorenoDivision of Cellular Medicine, School of Medicine, University of Dundee, Dundee, Scotland, UK.
Sourav BanerjeeDivision of Cellular Medicine, School of Medicine, University of Dundee, Dundee, Scotland, UK.
Angus W JacksonDivision of Cellular Medicine, School of Medicine, University of Dundee, Dundee, Scotland, UK.
Jean QuinnUnit of Gastrointestinal Oncology and Molecular Pathology, Institute of Cancer Sciences, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow, UK.
Gregg BaillieUnit of Gastrointestinal Oncology and Molecular Pathology, Institute of Cancer Sciences, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow, UK.
Jack E DixonDepartment of Pharmacology, University of California San Diego, La Jolla, CA, 92093-0721, USA.
Albena T Dinkova-KostovaDivision of Cellular Medicine, School of Medicine, University of Dundee, Dundee, Scotland, UK.ORCID http://orcid.org/0000-0003-0316-9859
Joanne EdwardsUnit of Gastrointestinal Oncology and Molecular Pathology, Institute of Cancer Sciences, College of Medical, Veterinary, and Life Sciences, University of Glasgow, Glasgow, UK.ORCID http://orcid.org/0000-0002-7192-6906
Laureano de la VegaDivision of Cellular Medicine, School of Medicine, University of Dundee, Dundee, Scotland, UK. l.delavega@dundee.ac.uk.ORCID http://orcid.org/0000-0003-2707-7414
University of Dundee · GBUniversity of Glasgow · GBUniversity of California San Diego · US

Funding

Cancer Research UK 18644Cancer Research UK 22869
6 · The paper itself

Abstract

To survive proteotoxic stress, cancer cells activate the proteotoxic-stress response pathway, which is controlled by the transcription factor heat shock factor 1 (HSF1). This pathway supports cancer initiation, cancer progression and chemoresistance and thus is an attractive therapeutic target. As developing inhibitors against transcriptional regulators, such as HSF1 is challenging, the identification and targeting of upstream regulators of HSF1 present a tractable alternative strategy. Here we demonstrate that in triple-negative breast cancer (TNBC) cells, the dual specificity tyrosine-regulated kinase 2 (DYRK2) phosphorylates HSF1, promoting its nuclear stability and transcriptional activity. DYRK2 depletion reduces HSF1 activity and sensitises TNBC cells to proteotoxic stress. Importantly, in tumours from TNBC patients, DYRK2 levels positively correlate with active HSF1 and associates with poor prognosis, suggesting that DYRK2 could be promoting TNBC. These findings identify DYRK2 as a key modulator of the HSF1 transcriptional programme and a potential therapeutic target.

Indexed as

Dyrk KinasesHeat Shock Transcription FactorsHumansPrognosisProtein Serine-Threonine KinasesProtein-Tyrosine KinasesTranscription FactorsTransfectionDyrk KinasesHeat Shock Transcription FactorsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesTranscription Factors

Identifiers

PMID33268814
PMCPMC8166837
OpenAlexW3110055410

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.