Evidence map›Paper›PMID 22579474›Full record

ArticleImmunity2012

Structural analysis of the STING adaptor protein reveals a hydrophobic dimer interface and mode of cyclic di-GMP binding.

Songying Ouyang, Xianqiang Song, Yaya Wang, Heng Ru, Neil Shaw, Yan Jiang, Fengfeng Niu, Yanping Zhu, Weicheng Qiu, Kislay Parvatiyar and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 201 papers.

0numbers the graph read from it
0cells of the map it votes in
201citing papers in PubMed
10.8field-weighted citation impact, top 1% 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

201 citing papers in PubMed, 329 citations in OpenAlex.

  1. Trial
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  13. Conjugated STING agonists.Molecular therapy. Nucleic acids · 2025
    Review
  14. Review
  15. Article
  16. Review
  17. cGAS-STING: mechanisms and therapeutic opportunities.Science China. Life sciences · 2025
    Review
  18. Article
  19. Review
  20. Review

141 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

14 authors at 2 institutions in 2 countries.

Songying OuyangNational Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.
Xianqiang Song
Yaya Wang
Heng Ru
Neil Shaw
Yan Jiang
Fengfeng Niu
Yanping Zhu
Weicheng Qiu
Kislay Parvatiyar
Yang Li
Rongguang Zhang
Genhong Cheng
Zhi-Jie Liu
Chinese Academy of Sciences · CNUniversity of California, Los Angeles · US

Funding

Viral Mediated Type I Interferon InductionR01AI069120 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2006 to 2021
$6.0M
Mechanisms of Biodefense By Toll-Like ReceptorsR01AI056154 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2004 to 2014
$3.7M
ROLE OF TOLL-LIKE RECEPTORS IN SKINR37AI047868 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MODLIN, ROBERT L · 2000 to 2009
$2.9M
Divergence of Phagocytic and Antimicrobial Programs in LeprosyR01AI047868 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MODLIN, ROBERT L · 2010 to 2014
$2.4M
Role of IRF3 and RXRa Crosstalk in Host Response to Viral InfectionsR01AI078389 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHENG, GENHONG · 2009 to 2013
$1.8M
NIAID NIH HHS AI047868NIAID NIH HHS AI056154NIAID NIH HHS AI069120NIAID NIH HHS R01 AI047868NIAID NIH HHS R01 AI056154NIAID NIH HHS R01 AI069120NIAID NIH HHS R01 AI078389NIAID NIH HHS R37 AI047868
6 · The paper itself

Abstract

STING is an essential signaling molecule for DNA and cyclic di-GMP (c-di-GMP)-mediated type I interferon (IFN) production via TANK-binding kinase 1 (TBK1) and interferon regulatory factor 3 (IRF3) pathway. It contains an N-terminal transmembrane region and a cytosolic C-terminal domain (CTD). Here, we describe crystal structures of STING CTD alone and complexed with c-di-GMP in a unique binding mode. The strictly conserved aa 153-173 region was shown to be cytosolic and participated in dimerization via hydrophobic interactions. The STING CTD functions as a dimer and the dimerization was independent of posttranslational modifications. Binding of c-di-GMP enhanced interaction of a shorter construct of STING CTD (residues 139-344) with TBK1. This suggests an extra TBK1 binding site, other than serine 358. This study provides a glimpse into the unique architecture of STING and sheds light on the mechanism of c-di-GMP-mediated TBK1 signaling.

Indexed as

Amino Acid SequenceConserved SequenceCrystallography, X-RayCyclic GMPDimerizationHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsMembrane ProteinsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein BindingProtein ConformationProtein Interaction MappingProtein Serine-Threonine Kinasesbis(3',5')-cyclic diguanylic acidCyclic GMPMembrane ProteinsPeptide FragmentsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSTING1 protein, humanSTING ProteinTBK1 protein, human

Identifiers

PMID22579474
PMCPMC3654694
OpenAlexW2093268266

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.