Evidence map›Paper›PMID 36864667›Full record

ArticleNucleic acids research2023

Filament assembly underpins the double-stranded DNA specificity of AIM2-like receptors.

Archit Garg, Christina M Stallings, Jungsan Sohn

Abstract read
In one paragraph

Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Design Considerations for Potent DNA-Platform-Based Cancer Vaccines.Current opinion in biomedical engineering · 2026
    Article
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  6. Review
  7. Article
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  13. The Role of the AIM2 Gene in Obesity-Related Glucose and Lipid Metabolic Disorders: A Recent Update.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024
    Review
  14. 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

3 authors.

Archit GargDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.ORCID 0000-0002-5931-2522
Christina M StallingsDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Jungsan SohnDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.ORCID 0000-0002-9570-2544

Funding

Biochemistry, Cellular and Molecular Biology Program: JHU BioGREAT (Biomedical Graduate REsiliency & Adaptability Training)T32GM144272 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Takanari Inoue · 2022 to 2026
$5.4M
Mechanistic Studies of cytosolic double-stranded DNA sensing pathways.R35GM145363 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JUNGSAN SOHN · 2022 to 2026
$2.3M
Mechanistic Studies of Cytoplasmic dsDNA-Sensing PathwaysR01GM129342 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SOHN, JUNGSAN · 2018 to 2021
$1.6M
NIGMS NIH HHS R01 GM129342NIGMS NIH HHS R35 GM145363NIGMS NIH HHS T32 GM144272
6 · The paper itself

Abstract

Upon sensing cytosolic- and/or viral double-stranded (ds)DNA, absent-in-melanoma-2 (AIM2)-like-receptors (ALRs) assemble into filamentous signaling platforms to initiate inflammatory responses. The versatile yet critical roles of ALRs in host innate defense are increasingly appreciated; however, the mechanisms by which AIM2 and its related IFI16 specifically recognize dsDNA over other nucleic acids remain poorly understood (i.e. single-stranded (ss)DNA, dsRNA, ssRNA and DNA:RNA hybrid). Here, we find that although AIM2 can interact with various nucleic acids, it preferentially binds to and assembles filaments faster on dsDNA in a duplex length-dependent manner. Moreover, AIM2 oligomers assembled on nucleic acids other than dsDNA not only display less ordered filamentous structures, but also fail to induce the polymerization of downstream ASC. Likewise, although showing broader nucleic acid selectivity than AIM2, IFI16 binds to and oligomerizes most readily on dsDNA in a duplex length-dependent manner. Nevertheless, IFI16 fails to form filaments on single-stranded nucleic acids and does not accelerate the polymerization of ASC regardless of bound nucleic acids. Together, we reveal that filament assembly is integral to nucleic acid distinction by ALRs.

Indexed as

DNA-Binding ProteinsNuclear ProteinsPhosphoproteinsCarrier ProteinsHumansInflammasomesAIM2 protein, humanCarrier ProteinsDNA-Binding ProteinsIFI16 protein, humanInflammasomesNuclear ProteinsPhosphoproteins

Identifiers

PMID36864667
PMCPMC10085679

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Registered trials

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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.