Evidence map›Paper›PMID 26008745›Full record

ArticleThe Journal of cell biology2015

Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling.

Stephan Wilmes, Oliver Beutel, Zhi Li, Véronique Francois-Newton, Christian P Richter, Dennis Janning, Cindy Kroll, Patrizia Hanhart, Katharina Hötte, Changjiang You and 3 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.1field-weighted citation impact, top 4% 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

80 citing papers in PubMed, 131 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Single-Molecule FRET-Tracking of InlB-Activated MET Receptors in Living Cells.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  5. Tuning of G-CSFR signaling by de novo-designed agonists.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  6. Article
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  9. Article
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Structure-function of type I and III interferons.Current opinion in immunology · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. Review

20 more citing papers are in PubMed but not listed here.

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

13 authors at 3 institutions in 2 countries.

Stephan WilmesDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Oliver BeutelDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Zhi LiInstitut Pasteur, Cytokine Signaling Unit, Centre National de la Recherche Scientifique URA1961, 75724 Paris, France.
Véronique Francois-NewtonInstitut Pasteur, Cytokine Signaling Unit, Centre National de la Recherche Scientifique URA1961, 75724 Paris, France.
Christian P RichterDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Dennis JanningDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Cindy KrollDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Patrizia HanhartDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Katharina HötteDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Changjiang YouDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany.
Gilles UzéCentre National de la Recherche Scientifique Montpellier, 34095 Montpellier, France.
Sandra PellegriniInstitut Pasteur, Cytokine Signaling Unit, Centre National de la Recherche Scientifique URA1961, 75724 Paris, France.
Jacob PiehlerDepartment of Biology, Division of Biophysics, University of Osnabrück, 49074 Osnabrück, Germany piehler@uos.de.
Osnabrück University · DEInstitut Pasteur · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type I interferons (IFNs) activate differential cellular responses through a shared cell surface receptor composed of the two subunits, IFNAR1 and IFNAR2. We propose here a mechanistic model for how IFN receptor plasticity is regulated on the level of receptor dimerization. Quantitative single-molecule imaging of receptor assembly in the plasma membrane of living cells clearly identified IFN-induced dimerization of IFNAR1 and IFNAR2. The negative feedback regulator ubiquitin-specific protease 18 (USP18) potently interferes with the recruitment of IFNAR1 into the ternary complex, probably by impeding complex stabilization related to the associated Janus kinases. Thus, the responsiveness to IFNα2 is potently down-regulated after the first wave of gene induction, while IFNβ, due to its ∼100-fold higher binding affinity, is still able to efficiently recruit IFNAR1. Consistent with functional data, this novel regulatory mechanism at the level of receptor assembly explains how signaling by IFNβ is maintained over longer times compared with IFNα2 as a temporally encoded cause of functional receptor plasticity.

Indexed as

EndopeptidasesHeLa CellsHumansInterferon Type IJanus Kinase 1Protein BindingProtein MultimerizationProtein StabilityReceptor, Interferon alpha-betaSignal TransductionUbiquitin ThiolesteraseEndopeptidasesIFNAR1 protein, humanIFNAR2 protein, humanInterferon Type IJAK1 protein, humanJanus Kinase 1Receptor, Interferon alpha-betaUbiquitin ThiolesteraseUSP18 protein, human

Identifiers

PMID26008745
PMCPMC4442803
OpenAlexW2111218879

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.