Evidence map›Paper›PMID 37408195›Full record

ArticleCells2023

Implication of the Transmembrane Domain in the Interleukin 10 Receptor Platform Oligomerisation.

Thomas Kuntzel, Caroline Spenlé, Lucas D Pham-Van, Dafni Birmpili, Aurélien Riou, Aurore Loeuillet, Imane Charmarke-Askar, Dominique Bagnard

Abstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
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.

Thomas KuntzelUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.ORCID 0000-0002-3239-5882
Caroline SpenléUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.ORCID 0000-0002-6353-3109
Lucas D Pham-VanUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.
Dafni BirmpiliUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.
Aurélien RiouUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.
Aurore LoeuilletUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.
Imane Charmarke-AskarUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.
Dominique BagnardUMR7242 Biotechnology and Cell Signalling, Centre National de la Recherche Scientifique, Strasbourg Drug Discovery and Development Institute (IMS), University of Strasbourg, 67400 Illkirch-Graffenstaden, France.ORCID 0000-0002-5261-902X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interleukin 10 (IL-10) exerts anti-inflammatory and immune regulatory roles through its fixation to the IL-10 receptor (IL-10R). The two subunits (IL-10Rα and IL-10Rβ) organise themselves to form a hetero-tetramer to induce the activation of the transcription factor STAT3. We analysed the activation patterns of the IL-10R, especially the contribution of the transmembrane (TM) domain of the IL-10Rα and IL-10Rβ subunits, as evidence accumulates that this short domain has tremendous implications in receptor oligomerisation and activation. We also addressed whether targeting the TM domain of IL-10R with peptides mimicking the TM sequences of the subunits translates into biological consequences. The results illustrate the involvement of the TM domains from both subunits in receptor activation and feature a distinctive amino acid crucial for the interaction. The TM peptide targeting approach also appears to be suitable for modulating the activation of the receptor through its action on the dimerization capabilities of the TM domains and thereby constitutes a potential new strategy for the modulation of the inflammation in pathologic contexts.

Indexed as

Gene Expression RegulationTranscription FactorsAmino AcidsReceptors, Interleukin-10Signal TransductionAmino AcidsReceptors, Interleukin-10Transcription Factorsinterleukin 10macrophagepeptidetransmembrane domain

Identifiers

PMID37408195
PMCPMC10216903

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.