Evidence map›Paper›PMID 37870259›Full record

ArticleEMBO reports2023

SIRT2 negatively regulates the cGAS-STING pathway by deacetylating G3BP1.

Yutong Li, Juntao Bie, Chen Song, Yunfei Li, Tianzhuo Zhang, Haishuang Li, Long Zhao, Fuping You, Jianyuan Luo

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
4.9field-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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Physiological Significance and Functions of AA.Reviews of physiology, biochemistry and pharmacology · 2027
    Review
  2. Article
  3. NADThe Journal of general virology · 2026
    Review
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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

9 authors at 1 institution in 1 country.

Yutong LiDepartment of Medical Genetics, Center for Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Juntao BieDepartment of Medical Genetics, Center for Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Chen SongDepartment of Medical Genetics, Center for Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Yunfei LiDepartment of Immunology, School of Basic Medical Sciences, Beijing Key Laboratory of Tumor Systems Biology, Institute of Systems Biomedicine, Peking University Health Science Center, Beijing, China.
Tianzhuo ZhangDepartment of Medical Genetics, Center for Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.
Haishuang LiDepartment of Pathology, School of Basic Medical Sciences, Peking University Third Hospital, Peking University Health Science Center, Beijing, China.
Long ZhaoDepartment of Gastroenterological Surgery, Peking University People's Hospital, Beijing, China.ORCID 0000-0002-9014-8345
Fuping YouDepartment of Immunology, School of Basic Medical Sciences, Beijing Key Laboratory of Tumor Systems Biology, Institute of Systems Biomedicine, Peking University Health Science Center, Beijing, China.ORCID 0000-0002-7444-729X
Jianyuan LuoDepartment of Medical Genetics, Center for Medical Genetics, School of Basic Medical Sciences, Peking University Health Science Center, Beijing, China.ORCID 0000-0001-6057-2914
Peking University · CN

Funding

MOST | National Natural Science Foundation of China (NSFC) 81671389MOST | National Natural Science Foundation of China (NSFC) 81874147MOST | National Natural Science Foundation of China (NSFC) 82172959
6 · The paper itself

Abstract

SIRT2, a cytoplasmic member of the Sirtuin family, has important roles in immunity and inflammation. However, its function in regulating the response to DNA virus infection remains elusive. Here, we find that SIRT2 is a unique regulator among the Sirtuin family that negatively modulates the cGAS-STING-signaling pathway. SIRT2 is down-regulated after Herpes simplex virus-1 (HSV-1) infection, and SIRT2 deficiency markedly elevates the expression levels of type I interferon (IFN). SIRT2 inhibits the DNA binding ability and droplet formation of cGAS by interacting with and deacetylating G3BP1 at K257, K276, and K376, leading to the disassembly of the cGAS-G3BP1 complex, which is critical for cGAS activation. Administration of AGK2, a selective SIRT2 inhibitor, protects mice from HSV-1 infection and increases the expression of IFN and IFN-stimulated genes. Our study shows that SIRT2 negatively regulates cGAS activation through G3BP1 deacetylation, suggesting a potential antiviral strategy by modulating SIRT2 activity.

Indexed as

DNA HelicasesImmunity, InnateAnimalsMiceNucleotidyltransferasesPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsSignal TransductionSirtuin 2DNA HelicasesG3bp1 protein, mouseNucleotidyltransferasesPoly-ADP-Ribose Binding ProteinsRNA HelicasesRNA Recognition Motif ProteinsSirt2 protein, mouseSirtuin 2acetylationcGASG3BP1innate immunitySIRT2

Identifiers

PMID37870259
PMCPMC10702829
OpenAlexW4387865958

What OpenQuestion holds

Textmetadata
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.