Evidence map›Paper›PMID 29139553›Full record

ArticleFEBS letters2017

Distinct B subunits of PP2A regulate the NF-κB signalling pathway through dephosphorylation of IKKβ, IκBα and RelA.

Yoshihiro Tsuchiya, Keiko Osaki, Mayu Kanamoto, Yuki Nakao, Ena Takahashi, Toru Higuchi, Hideaki Kamata

Open access · hybridAbstract readLetter
In one paragraph

Article in FEBS letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

30 citing papers in PubMed, 38 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

7 authors at 1 institution in 1 country.

Yoshihiro TsuchiyaLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Keiko OsakiLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Mayu KanamotoLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Yuki NakaoLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Ena TakahashiLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Toru HiguchiLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Hideaki KamataLaboratory of Biomedical Chemistry, Department of Molecular Medical Science, Graduate School of Biomedical Science, Hiroshima University, Japan.
Hiroshima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PP2A is composed of a scaffolding subunit (A), a catalytic subunit (C) and a regulatory subunit (B) that is classified into four families including B, B', B'' and B'''/striatin. Here, we found that a distinct PP2A complex regulates NF-κB signalling by dephosphorylation of IKKβ, IκBα and RelA/p65. The PP2A core enzyme AC dimer and the holoenzyme AB'''C trimer dephosphorylate IKKβ, IκBα and RelA, whereas the ABC trimer dephosphorylates IκBα but not IKKβ and RelA in cells. In contrast, AB'C and AB''C trimers have little effect on dephosphorylation of these signalling proteins. These results suggest that different forms of PP2A regulate NF-κB pathway signalling through multiple steps each in a different manner, thereby finely tuning NF-κB- and IKKβ-mediated cellular responses.

Indexed as

Cells, CulturedHumansI-kappa B KinaseNF-kappa BNF-KappaB Inhibitor alphaPhosphorylationProtein Phosphatase 2Protein SubunitsSignal TransductionTranscription Factor RelAI-kappa B KinaseNF-kappa BNF-KappaB Inhibitor alphaProtein Phosphatase 2Protein SubunitsRELA protein, humanTranscription Factor RelANF-kappa Bprotein phosphataseprotein phosphatase 2 A (PP2A)

Identifiers

PMID29139553
PMCPMC5767752
OpenAlexW2769765923

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.