Evidence map›Paper›PMID 10022868›Full record

ArticleMolecular and cellular biology1999

The histone acetylase PCAF is a phorbol-ester-inducible coactivator of the IRF family that confers enhanced interferon responsiveness.

A Masumi, I M Wang, B Lefebvre, X J Yang, Y Nakatani, K Ozato

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

39 citing papers in PubMed, 137 citations in OpenAlex.

  1. Review
  2. Article
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  4. Loss of Long Noncoding RNACancer research · 2022
    Article
  5. Complex functions of Gcn5 and Pcaf in development and disease.Biochimica et biophysica acta. Gene regulatory mechanisms · 2021
    Review
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  8. Review
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  12. Review
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  18. Review
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  20. Altered memory capacities and response to stress in p300/CBP-associated factor (PCAF) histone acetylase knockout mice.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2008
    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 1 institution in 4 countries.

A MasumiLaboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2753, USA.
I M Wang
B Lefebvre
X J Yang
Y Nakatani
K Ozato
National Institutes of Health · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcription factors of the interferon regulatory factor (IRF) family bind to the type I interferon (IFN)-responsive element (ISRE) and activate transcription from IFN-inducible genes. To identify cofactors that associate with IRF proteins, DNA affinity binding assays were performed with nuclear extracts prepared from tissue culture cells. The results demonstrated that the endogenous IRFs bound to the ISRE are complexed with the histone acetylases, PCAF, GCN5, and p300/CREB binding protein and that histone acetylase activities are accumulated on the IRF-ISRE complexes. By testing recombinant proteins, we show that PCAF directly binds to some but not all members of the IRF family through distinct domains of the two proteins. This interaction was functionally significant, since transfection of PCAF strongly enhanced IRF-1- and IRF-2-dependent promoter activities. Further studies showed that expression of PCAF and other histone acetylases was markedly induced in U937 cells upon phorbol ester treatment, which led to increased recruitment of PCAF to the IRF-ISRE complexes. Coinciding with the induction of histone acetylases, phorbol ester markedly enhanced IFN-alpha-stimulated gene expression in U937 cells. Supporting the role for PCAF in conferring IFN responsiveness, transfection of PCAF into U937 cells led to a large increase in IFN-alpha-inducible promoter activity. These results demonstrate that PCAF is a phorbol ester-inducible coactivator of the IRF proteins which contributes to the establishment of type I IFN responsiveness.

Indexed as

Saccharomyces cerevisiae ProteinsTranscription FactorsAcetyltransferasesAnimalsBinding, CompetitiveBinding SitesCell Cycle ProteinsCell LineCREB-Binding ProteinDNA-Binding ProteinsE1A-Associated p300 ProteinGene ExpressionHistone AcetyltransferasesHumansInterferon-alphaInterferon Regulatory Factor-1AcetyltransferasesCell Cycle ProteinsCREB-Binding ProteinCREBBP protein, humanCrebbp protein, mouseDNA-Binding ProteinsE1A-Associated p300 ProteinEp300 protein, mouseGcn5l2 protein, mouseHistone AcetyltransferasesInterferon-alphaInterferon Regulatory Factor-1Interferon Regulatory Factor-2Interferon Regulatory Factor-4Interferon Regulatory Factor-8Interferon Regulatory FactorsIRF1 protein, humanIrf1 protein, mouseIRF2 protein, humanIrf2 protein, mouseKAT2A protein, humanNuclear Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsPhosphoproteinsRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsTetradecanoylphorbol AcetateTrans-ActivatorsTranscription Factors

Identifiers

PMID10022868
PMCPMC83974
OpenAlexW2147410548

What OpenQuestion holds

Texttitle and abstract
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.