Evidence map›Paper›PMID 37989995›Full record

ArticleNature communications2023

PTK2B promotes TBK1 and STING oligomerization and enhances the STING-TBK1 signaling.

Yongfang Lin, Jing Yang, Qili Yang, Sha Zeng, Jiayu Zhang, Yuanxiang Zhu, Yuxin Tong, Lin Li, Weiqi Tan, Dahua Chen and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 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
3.6field-weighted citation impact, top 7% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

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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

11 authors at 2 institutions in 2 countries.

Yongfang Lin *State Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.
Jing Yang *State Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.
Qili YangState Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.
Sha ZengInstitute of Biomedical Research, Yunnan University, 650500, Kunming, China.
Jiayu ZhangState Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.ORCID 0000-0003-3333-5889
Yuanxiang ZhuInstitute of Biomedical Research, Yunnan University, 650500, Kunming, China.ORCID 0000-0002-9140-5622
Yuxin TongInstitute of Biomedical Research, Yunnan University, 650500, Kunming, China.
Lin LiState Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.ORCID 0000-0002-7141-8645
Weiqi TanState Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China.
Dahua ChenInstitute of Biomedical Research, Yunnan University, 650500, Kunming, China. chendh@ynu.edu.cn.
Qinmiao SunState Key Laboratory of Membrane Biology, Institute of Zoology, Chinese Academy of Sciences, Jia #3 Datun Road, Chaoyang District, 100101, Beijing, China. qinmiaosun@ioz.ac.cn.ORCID 0000-0001-8091-1653
Yunnan University · CNChinese Academy of Sciences · CN

Funding

National Natural Science Foundation of China (National Science Foundation of China) 31970895National Natural Science Foundation of China (National Science Foundation of China) 32370928
6 · The paper itself

Abstract

TANK-binding kinase 1 (TBK1) is a key kinase in regulating antiviral innate immune responses. While the oligomerization of TBK1 is critical for its full activation, the molecular mechanism of how TBK1 forms oligomers remains unclear. Here, we show that protein tyrosine kinase 2 beta (PTK2B) acts as a TBK1-interacting protein and regulates TBK1 oligomerization. Functional assays reveal that PTK2B depletion reduces antiviral signaling in mouse embryonic fibroblasts, macrophages and dendritic cells, and genetic experiments show that Ptk2b-deficient mice are more susceptible to viral infection than control mice. Mechanistically, we demonstrate that PTK2B directly phosphorylates residue Tyr591 of TBK1, which increases TBK1 oligomerization and activation. In addition, we find that PTK2B also interacts with the stimulator of interferon genes (STING) and can promote its oligomerization in a kinase-independent manner. Collectively, PTK2B enhances the oligomerization of TBK1 and STING via different mechanisms, subsequently regulating STING-TBK1 activation to ensure efficient antiviral innate immune responses.

Indexed as

FibroblastsMembrane ProteinsAnimalsAntiviral AgentsFocal Adhesion Kinase 2Immunity, InnateMiceSignal TransductionAntiviral AgentsFocal Adhesion Kinase 2Membrane ProteinsPtk2b protein, mouse

Identifiers

PMID37989995
PMCPMC10663505
OpenAlexW4388845180

What OpenQuestion holds

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LicenceCC BY
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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.