Evidence map›Paper›PMID 28716910›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Methylcytosine dioxygenase TET3 interacts with thyroid hormone nuclear receptors and stabilizes their association to chromatin.

Wenyue Guan, Romain Guyot, Jacques Samarut, Frédéric Flamant, Jiemin Wong, Karine Cécile Gauthier

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Selective Estrogen Receptor Modulators' (SERMs) Influence onInternational journal of molecular sciences · 2024
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  9. Mechanisms that regulate the activities of TET proteins.Cellular and molecular life sciences : CMLS · 2022
    Review
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  11. Article
  12. Review
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  14. TET3 regulates DNA hydroxymethylation of neuroprotective genes following focal ischemia.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2021
    Article
  15. Review
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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

6 authors at 4 institutions in 2 countries.

Wenyue GuanShanghai Key Laboratory of Regulatory Biology, The Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China.
Romain GuyotInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, CNRS, Ecole Normale Supérieure de Lyon, 69364 Lyon cedex 07, France.
Jacques SamarutInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, CNRS, Ecole Normale Supérieure de Lyon, 69364 Lyon cedex 07, France.
Frédéric FlamantInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, CNRS, Ecole Normale Supérieure de Lyon, 69364 Lyon cedex 07, France.
Jiemin WongShanghai Key Laboratory of Regulatory Biology, The Institute of Biomedical Sciences and School of Life Sciences, East China Normal University, Shanghai 200241, China; karine.gauthier@ens-lyon.fr jmweng@bio.ecnu.edu.cn.
Karine Cécile GauthierInstitut de Génomique Fonctionnelle de Lyon, Université de Lyon, CNRS, Ecole Normale Supérieure de Lyon, 69364 Lyon cedex 07, France karine.gauthier@ens-lyon.fr jmweng@bio.ecnu.edu.cn.
Institut de Génomique Fonctionnelle de Lyon · FRUniversité Claude Bernard Lyon 1 · FRCentre National de la Recherche Scientifique · FREast China Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thyroid hormone receptors (TRs) are members of the nuclear hormone receptor superfamily that act as ligand-dependent transcription factors. Here we identified the ten-eleven translocation protein 3 (TET3) as a TR interacting protein increasing cell sensitivity to T3. The interaction between TET3 and TRs is independent of TET3 catalytic activity and specifically allows the stabilization of TRs on chromatin. We provide evidence that TET3 is required for TR stability, efficient binding of target genes, and transcriptional activation. Interestingly, the differential ability of different TRα1 mutants to interact with TET3 might explain their differential dominant activity in patients carrying TR germline mutations. So this study evidences a mode of action for TET3 as a nonclassical coregulator of TRs, modulating its stability and access to chromatin, rather than its intrinsic transcriptional activity. This regulatory function might be more general toward nuclear receptors. Indeed, TET3 interacts with different members of the superfamily and also enhances their association to chromatin.

Indexed as

Catalytic DomainChromatinDioxygenasesGene Expression RegulationHEK293 CellsHumansImmunoprecipitationMutationNitrilesProtein Interaction Domains and MotifsReceptors, AndrogenThiazolesThyroid Hormone Receptors alphaThyroid Hormone Receptors betaTranscription, GeneticUbiquitinationAR protein, humanChromatinDioxygenasesNitrilesReceptors, AndrogenTET3 protein, humanThiazolesthyroid hormone receptor alpha, humanThyroid Hormone Receptors alphaThyroid Hormone Receptors betaXCT790chromatin recruitmentmethylcytosine dioxygenase TET3protein stabilityRTH syndromethyroid hormone receptor

Identifiers

PMID28716910
PMCPMC5547603
OpenAlexW2735951677

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.