Evidence map›Paper›PMID 30526044›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2019

NF-κB p65 dimerization and DNA-binding is important for inflammatory gene expression.

Tabea Riedlinger, Robert Liefke, Johanna Meier-Soelch, Liane Jurida, Andrea Nist, Thorsten Stiewe, Michael Kracht, M Lienhard Schmitz

Open access · hybridAbstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

33 citing papers in PubMed, 46 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Tabea RiedlingerInstitute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.
Robert LiefkeInstitute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.
Johanna Meier-SoelchRudolf-Buchheim-Institute of Pharmacology, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany; and.
Liane JuridaRudolf-Buchheim-Institute of Pharmacology, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany; and.
Andrea NistGenomics Core Facility-Institute of Molecular Oncology, Philipps University Marburg, Marburg, Germany.
Thorsten StieweGenomics Core Facility-Institute of Molecular Oncology, Philipps University Marburg, Marburg, Germany.
Michael KrachtRudolf-Buchheim-Institute of Pharmacology, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany; and.
M Lienhard SchmitzInstitute of Biochemistry, Member of the German Center for Lung Research, Justus-Liebig-University, Giessen, Germany.
Justus-Liebig-Universität Gießen · DEPhilipps University of Marburg · DECardio-Pulmonary Institute · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Increasing evidence shows that many transcription factors execute important biologic functions independent from their DNA-binding capacity. The NF-κB p65 (RELA) subunit is a central regulator of innate immunity. Here, we investigated the relative functional contribution of p65 DNA-binding and dimerization in p65-deficient human and murine cells reconstituted with single amino acid mutants preventing either DNA-binding (p65 E/I) or dimerization (p65 FL/DD). DNA-binding of p65 was required for RelB-dependent stabilization of the NF-κB p100 protein. The antiapoptotic function of p65 and expression of the majority of TNF-α-induced genes were dependent on p65's ability to bind DNA and to dimerize. Chromatin immunoprecipitation with massively parallel DNA sequencing experiments revealed that impaired DNA-binding and dimerization strongly diminish the chromatin association of p65. However, there were also p65-independent TNF-α-inducible genes and a subgroup of p65 binding sites still allowed some residual chromatin association of the mutants. These sites were enriched in activator protein 1 (AP-1) binding motifs and showed increased chromatin accessibility and basal transcription. This suggests a mechanism of assisted p65 chromatin association that can be in part facilitated by chromatin priming and cooperativity with other transcription factors such as AP-1.-Riedlinger, T., Liefke, R., Meier-Soelch, J., Jurida, L., Nist, A., Stiewe, T., Kracht, M., Schmitz, M. L. NF-κB p65 dimerization and DNA-binding is important for inflammatory gene expression.

Indexed as

AnimalsBinding SitesCell Line, TumorChromatinChromatin Assembly and DisassemblyDimerizationDNADNA-Binding ProteinsGene ExpressionHeLa CellsHumansInflammationMiceProtein BindingTranscription Factor AP-1Transcription Factor RelAChromatinDNADNA-Binding ProteinsTranscription Factor AP-1Transcription Factor RelATranscription Factor RelBchromatininflammationtranscription

Identifiers

PMID30526044
PMCPMC6404571
OpenAlexW2904754040

What OpenQuestion holds

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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.