Evidence map›Paper›PMID 28165510›Full record

ArticleNature structural & molecular biology2017

STAT2 is an essential adaptor in USP18-mediated suppression of type I interferon signaling.

Kei-Ichiro Arimoto, Sara Löchte, Samuel A Stoner, Christoph Burkart, Yue Zhang, Sayuri Miyauchi, Stephan Wilmes, Jun-Bao Fan, Jürgen J Heinisch, Zhi Li and 5 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 132 papers.

0numbers the graph read from it
0cells of the map it votes in
132citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

132 citing papers in PubMed, 198 citations in OpenAlex.

  1. Review
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  14. TRIM21 is a molecular rheostat for influenza A virus replication.bioRxiv : the preprint server for biology · 2026
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72 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

15 authors at 5 institutions in 3 countries.

Kei-Ichiro ArimotoMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Sara LöchteDepartment of Biology, University of Osnabrück, Osnabrück, Germany.
Samuel A StonerMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Christoph BurkartMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Yue ZhangDivision of Biological Sciences, University of California San Diego, La Jolla, California, USA.
Sayuri MiyauchiMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Stephan WilmesDepartment of Biology, University of Osnabrück, Osnabrück, Germany.
Jun-Bao FanMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Jürgen J HeinischDepartment of Biology, University of Osnabrück, Osnabrück, Germany.
Zhi LiInstitut Pasteur, Cytokine Signaling Unit, Inserm, Paris, France.
Ming YanMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
Sandra PellegriniInstitut Pasteur, Cytokine Signaling Unit, Inserm, Paris, France.
Frédéric CollandHybrigenics, impasse Reille, Paris, France.
Jacob PiehlerDepartment of Biology, University of Osnabrück, Osnabrück, Germany.
Dong-Er ZhangMoores UCSD Cancer Center, University of California San Diego, La Jolla, California, USA.
University of California, San Diego · USOsnabrück University · DEHybrigenics (France) · FRInserm · FRInstitut Pasteur · FR

Funding

Training Program in Basic Clinical GeneticsT32GM008666 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMILTON, BRUCE A · 1998 to 2021
$8.6M
ISG15 and Protein ISGylation in CancerR01CA177305 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHANG, DONG-ER · 2013 to 2023
$3.7M
UBP43 in HematopoiesisR01HL091549 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI ZHANG, DONG-ER · 2008 to 2012
$1.9M
NCI NIH HHS R01 CA177305NHLBI NIH HHS R01 HL091549NIGMS NIH HHS T32 GM008666
6 · The paper itself

Abstract

Type I interferons (IFNs) are multifunctional cytokines that regulate immune responses and cellular functions but also can have detrimental effects on human health. A tight regulatory network therefore controls IFN signaling, which in turn may interfere with medical interventions. The JAK-STAT signaling pathway transmits the IFN extracellular signal to the nucleus, thus resulting in alterations in gene expression. STAT2 is a well-known essential and specific positive effector of type I IFN signaling. Here, we report that STAT2 is also a previously unrecognized, crucial component of the USP18-mediated negative-feedback control in both human and mouse cells. We found that STAT2 recruits USP18 to the type I IFN receptor subunit IFNAR2 via its constitutive membrane-distal STAT2-binding site. This mechanistic coupling of effector and negative-feedback functions of STAT2 may provide novel strategies for treatment of IFN-signaling-related human diseases.

Indexed as

Signal TransductionAnimalsCell Line, TumorEndopeptidasesFeedback, PhysiologicalHumansImmunoblottingInterferon Type IMiceMutant ProteinsProtein BindingProtein DomainsReceptor, Interferon alpha-betaSTAT2 Transcription FactorTwo-Hybrid System TechniquesUbiquitin ThiolesteraseEndopeptidasesIFNAR2 protein, humanInterferon Type IMutant ProteinsReceptor, Interferon alpha-betaSTAT2 Transcription FactorUbiquitin ThiolesteraseUSP18 protein, human

Identifiers

PMID28165510
PMCPMC5365074
OpenAlexW2586938873

What OpenQuestion holds

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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.