Evidence map›Paper›PMID 30467221›Full record

ArticleThe EMBO journal2018

The IκB kinase complex is a regulator of mRNA stability.

Nadine Mikuda, Marina Kolesnichenko, Patrick Beaudette, Oliver Popp, Bora Uyar, Wei Sun, Ahmet Bugra Tufan, Björn Perder, Altuna Akalin, Wei Chen and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
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  5. Bioinformatic Analysis ofInternational journal of molecular sciences · 2024
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  11. Eukaryotic mRNA Decapping Activation.Frontiers in genetics · 2022
    Review
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  16. Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 1 institution in 1 country.

Nadine MikudaSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Marina KolesnichenkoSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Patrick BeaudetteMass Spectrometry Group, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Oliver PoppMass Spectrometry Group, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Bora UyarBioinformatics/Mathematical Modelling Platform, Max Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID 0000-0002-3170-4890
Wei SunLaboratory for Functional Genomics and Systems Biology, Max Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID 0000-0001-9607-1361
Ahmet Bugra TufanSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Björn PerderSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Altuna AkalinBioinformatics/Mathematical Modelling Platform, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Wei ChenLaboratory for Functional Genomics and Systems Biology, Max Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID 0000-0003-3263-1627
Philipp MertinsMass Spectrometry Group, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Gunnar DittmarMass Spectrometry Group, Max Delbrück Center for Molecular Medicine, Berlin, Germany.ORCID 0000-0003-3647-8623
Michael HinzSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany.
Claus ScheidereitSignal Transduction Laboratory, Max Delbrück Center for Molecular Medicine, Berlin, Germany scheidereit@mdc-berlin.de.ORCID 0000-0002-0446-6129
Max Delbrück Center · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The IκB kinase (IKK) is considered to control gene expression primarily through activation of the transcription factor NF-κB. However, we show here that IKK additionally regulates gene expression on post-transcriptional level. IKK interacted with several mRNA-binding proteins, including a Processing (P) body scaffold protein, termed enhancer of decapping 4 (EDC4). IKK bound to and phosphorylated EDC4 in a stimulus-sensitive manner, leading to co-recruitment of P body components, mRNA decapping proteins 1a and 2 (DCP1a and DCP2) and to an increase in P body numbers. Using RNA sequencing, we identified scores of transcripts whose stability was regulated via the IKK-EDC4 axis. Strikingly, in the absence of stimulus, IKK-EDC4 promoted destabilization of pro-inflammatory cytokines and regulators of apoptosis. Our findings expand the reach of IKK beyond its canonical role as a regulator of transcription.

Indexed as

RNA StabilityEndoribonucleasesHEK293 CellsHep G2 CellsHumansI-kappa B KinaseMultiprotein ComplexesProteinsRNA, MessengerTrans-ActivatorsDCP1A protein, humanDCP2 protein, humanEDC4 protein, humanEndoribonucleasesI-kappa B KinaseIKBKB protein, humanMultiprotein ComplexesProteinsRNA, MessengerTrans-ActivatorsEDC4IKKP bodiespost‐transcriptional regulationRNA stability

Identifiers

PMID30467221
PMCPMC6293339
OpenAlexW2800076422

What OpenQuestion holds

Textmetadata
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.