Evidence map›Paper›PMID 20547488›Full record

ArticleThe Journal of biological chemistry2010

Cross-talk between the p38alpha and JNK MAPK pathways mediated by MAP kinase phosphatase-1 determines cellular sensitivity to UV radiation.

Christopher J Staples, David M Owens, Jana V Maier, Andrew C B Cato, Stephen M Keyse

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 79 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Article
  5. Article
  6. Surprising regulatory plasticity for the conserved HOG pathway in diversebioRxiv : the preprint server for biology · 2025
    Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
  16. Mapping p38α mitogen-activated protein kinase signaling by proximity-dependent labeling.Protein science : a publication of the Protein Society · 2020
    Article
  17. Article
  18. Understanding MAPK Signaling Pathways in Apoptosis.International journal of molecular sciences · 2020
    Review
  19. Review
  20. Dual-Specificity Phosphatase Regulation in Neurons and Glial Cells.International journal of molecular sciences · 2019
    Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Christopher J StaplesCR-UK Stress Response Laboratory, Biomedical Research Institute, Ninewells Hospital and Medical School, University of Dundee, Dundee, Scotland, UK.
David M Owens
Jana V Maier
Andrew C B Cato
Stephen M Keyse
Karlsruhe Institute of Technology · DEUniversity of Dundee · GBNinewells Hospital · GB

Funding

Cancer Research UK 12053Medical Research Council
6 · The paper itself

Abstract

MAPK phosphatase-1 (DUSP1/MKP-1) is a mitogen and stress-inducible dual specificity protein phosphatase, which can inactivate all three major classes of MAPK in mammalian cells. DUSP1/MKP-1 is implicated in cellular protection against a variety of genotoxic insults including hydrogen peroxide, ionizing radiation, and cisplatin, but its role in the interplay between different MAPK pathways in determining cell death and survival is not fully understood. We have used pharmacological and genetic tools to demonstrate that DUSP1/MKP-1 is an essential non-redundant regulator of UV-induced cell death in mouse embryo fibroblasts (MEFs). The induction of DUSP1/MKP-1 mRNA and protein in response to UV radiation is mediated by activation of the p38alpha but not the JNK1 or JNK2 MAPK pathways. Furthermore, we identify MSK1 and -2 and their downstream effectors cAMP-response element-binding protein/ATF1 as mediators of UV-induced p38alpha-dependent DUSP1/MKP-1 transcription. Dusp1/Mkp-1 null MEFs display increased signaling through both the p38alpha and JNK MAPK pathways and are acutely sensitive to UV-induced apoptosis. This lethality is rescued by the reintroduction of wild-type DUSP1/MKP-1 and by a mutant of DUSP1/MKP-1, which is unable to bind to either p38alpha or ERK1/2, but retains full activity toward JNK. Importantly, whereas small interfering RNA-mediated knockdown of DUSP1/MKP-1 sensitizes wild-type MEFs to UV radiation, DUSP1/MKP-1 knockdown in MEFS lacking JNK1 and -2 does not result in increased cell death. Our results demonstrate that cross-talk between the p38alpha and JNK pathways mediated by induction of DUSP1/MKP-1 regulates the cellular response to UV radiation.

Indexed as

Radiation ToleranceAnimalsCell DeathCells, CulturedDual Specificity Phosphatase 1FibroblastsJNK Mitogen-Activated Protein KinasesMiceMitogen-Activated Protein Kinase 14Receptor Cross-TalkRNA, MessengerSignal TransductionTranscriptional ActivationUltraviolet RaysDual Specificity Phosphatase 1JNK Mitogen-Activated Protein KinasesMitogen-Activated Protein Kinase 14RNA, Messenger

Identifiers

PMID20547488
PMCPMC2923983
OpenAlexW2047152276

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.