Evidence map›Paper›PMID 28100697›Full record

ArticleNucleic acids research2017

The histone demethylase PHF8 is a molecular safeguard of the IFNγ response.

Elena Asensio-Juan, Raquel Fueyo, Stella Pappa, Simona Iacobucci, Carmen Badosa, Sergi Lois, Miriam Balada, Laia Bosch-Presegué, Alex Vaquero, Sara Gutiérrez and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.8field-weighted citation impact, top 31% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Targeting the PHF8/YY1 axis suppresses cancer cell growth through modulation of ROS.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. Risk factors for inhibitors in hemophilia A based on RNA-seq and DNA methylation.Research and practice in thrombosis and haemostasis · 2022
    Article
  10. Article
  11. Article
  12. PHF2 histone demethylase prevents DNA damage and genome instability by controlling cell cycle progression of neural progenitors.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  13. Review
  14. Review
  15. 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

14 authors at 6 institutions in 1 country.

Elena Asensio-JuanDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Raquel FueyoDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Stella PappaDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Simona IacobucciDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Carmen BadosaDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Sergi LoisVall d'Hebron Institute of Research (VHIR), Passeig de la Vall d'Hebron, 119, E-08035 Barcelona, Spain.
Miriam BaladaDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Laia Bosch-PreseguéChromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Institut d?Investigació Biomèdica de Bellvitge (IDIBELL), 08907- L'Hospitalet de Llobregat, Barcelona, Spain.
Alex VaqueroChromatin Biology Laboratory, Cancer Epigenetics and Biology Program (PEBC), Institut d?Investigació Biomèdica de Bellvitge (IDIBELL), 08907- L'Hospitalet de Llobregat, Barcelona, Spain.
Sara GutiérrezDepartment of Cell Biology, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Carme CaellesDepartment of Biochemistry and Molecular Biology, School of Pharmacy, University of Barcelona, Barcelona 08028, Spain.
Carme GallegoDepartment of Cell Biology, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Xavier de la CruzVall d'Hebron Institute of Research (VHIR), Passeig de la Vall d'Hebron, 119, E-08035 Barcelona, Spain.
Marian A Martínez-BalbásDepartment of Molecular Genomics, Instituto de Biología Molecular de Barcelona (IBMB), Consejo Superior de Investigaciones Científicas (CSIC), Barcelona 08028, Spain.
Consejo Superior de Investigaciones Científicas · ESInstitut de Biologia Molecular de Barcelona · ESInstitut d'Investigació Biomédica de Bellvitge · ESInstitució Catalana de Recerca i Estudis Avançats · ESUniversitat de Barcelona · ESVall d'Hebron Institut de Recerca · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A precise immune response is essential for cellular homeostasis and animal survival. The paramount importance of its control is reflected by the fact that its non-specific activation leads to inflammatory events that ultimately contribute to the appearance of many chronic diseases. However, the molecular mechanisms preventing non-specific activation and allowing a quick response upon signal activation are not yet fully understood. In this paper we uncover a new function of PHF8 blocking signal independent activation of immune gene promoters. Affinity purifications coupled with mass spectrometry analysis identified SIN3A and HDAC1 corepressors as new PHF8 interacting partners. Further molecular analysis demonstrated that prior to interferon gamma (IFNγ) stimulation, PHF8 is bound to a subset of IFNγ-responsive promoters. Through the association with HDAC1 and SIN3A, PHF8 keeps the promoters in a silent state, maintaining low levels of H4K20me1. Upon IFNγ treatment, PHF8 is phosphorylated by ERK2 and evicted from the promoters, correlating with an increase in H4K20me1 and transcriptional activation. Our data strongly indicate that in addition to its well-characterized function as a coactivator, PHF8 safeguards transcription to allow an accurate immune response.

Indexed as

Transcriptional ActivationCell LineChromatinGene SilencingHistone Deacetylase 1Histone DemethylasesHumansInterferon-gammaMitogen-Activated Protein Kinase 1Promoter Regions, GeneticRepressor ProteinsSin3 Histone Deacetylase and Corepressor ComplexTranscription FactorsChromatinHDAC1 protein, humanHistone Deacetylase 1Histone DemethylasesInterferon-gammaMitogen-Activated Protein Kinase 1PHF8 protein, humanRepressor ProteinsSIN3A transcription factorSin3 Histone Deacetylase and Corepressor ComplexTranscription Factors

Identifiers

PMID28100697
PMCPMC5397186
OpenAlexW2574126393

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.