Evidence map›Paper›PMID 40037706›Full record

ArticleNucleic acids research2025

Conformational reorganization and phase separation drive hyper-editing of ADR-2-ADBP-1 complex.

Jianqiang Mu, Cang Wu, Kaiming Xu, Xingang Liu, Yajuan Fu, Zhen Zhang, Jingwei Yu, Chenyang Xue, Zi Wang, Xinmeng Chen and 3 more

Abstract read
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In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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3 · Its place in the literature

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0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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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

13 authors.

Jianqiang MuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Cang WuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Kaiming XuTsinghua-Peking Center for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, China.
Xingang LiuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Yajuan FuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Zhen ZhangShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Jingwei YuDepartment of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055 Guangdong, China.ORCID 0000-0003-4268-436X
Chenyang XueShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.ORCID 0000-0002-9603-3426
Zi WangTsinghua-Peking Center for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, China.
Xinmeng ChenShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.
Yanhong ChenDepartment of Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen 518055 Guangdong, China.
Guangshuo OuTsinghua-Peking Center for Life Sciences, Beijing Frontier Research Center for Biological Structure, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing 100084, China.
Zhongmin LiuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology Shenzhen, 518055 Guangdong, China.ORCID 0000-0002-3280-3890

Funding

Guangdong Basic and Applied Basic Research Foundation 2024A1515011538Guangdong Innovative and Entrepreneurial Research Team Program 2021ZT09Y104National Science Foundation of China 32371275Pearl River Talent Recruitment Program 2021QN02Y449Shenzhen Municipal Basic Research projects JCYJ20210324105007020Shenzhen Science and Technology Program ZDSYS20220402111000001Southern University of Science and Technology
6 · The paper itself

Abstract

Adenosine deaminase acting on RNA (ADAR) proteins, which mediate adenosine-to-inosine editing of double-stranded ribonucleic acid (dsRNA) substrates, play essential roles in balancing innate immunity. Using cryogenic electron microscopy, we solved the structure of the Caenorhabditis elegans ADR-2-ADBP-1 complex (stoichiometric ratio, 2:2), which is an asymmetric ADR-2 dimer with one editing site blocked by the other ADR-2. Unexpectedly, dsRNA recruitment triggered dissociation of the ADR-2 dimer, exposing more competent dsRNA editing sites. Furthermore, high dsRNA and protein concentrations caused the formation of liquid-liquid phase-separated puncta, in which significantly greater editing activity was observed, indicating that organizational transitions enable the ADR-2-ADBP-1 complex to perform dsRNA hyper-editing. Our findings suggest that the ADAR editing mechanism adapts to different conditions via conformational reorganization.

Indexed as

Adenosine DeaminaseCaenorhabditis elegans ProteinsRNA-Binding ProteinsRNA EditingAnimalsCaenorhabditis elegansCryoelectron MicroscopyModels, MolecularPhase SeparationProtein BindingProtein ConformationProtein MultimerizationRNA, Double-StrandedAdenosine DeaminaseCaenorhabditis elegans ProteinsRNA-Binding ProteinsRNA, Double-Stranded

Identifiers

PMID40037706
PMCPMC11879458

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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.