Evidence map›Paper›PMID 41203642›Full record

ArticleNature communications2025

Deciphering the molecular mechanisms of FET fusion oncoprotein-DNA hollow co-condensates.

Linyu Zuo, Qirui Guo, Cheng Li, Kecheng Zhang, Yancao Chen, Baiyi Jiang, Zhixing Chen, Yufei Xia, Long Qian, Lei Zhang and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Article
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.

Linyu Zuo *Center for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Qirui Guo *Center for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Cheng Li *Center for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Kecheng ZhangPeking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Yancao ChenCenter for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Baiyi JiangCenter for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.
Zhixing ChenPeking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China.ORCID http://orcid.org/0000-0001-5962-7359
Yufei XiaKey Laboratory of Biopharmaceutical Preparation and Delivery, Chinese Academy of Sciences, Beijing, China. yfxia@ipe.ac.cn.ORCID http://orcid.org/0000-0003-1215-6128
Long QianCenter for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China. long.qian@pku.edu.cn.ORCID http://orcid.org/0000-0003-3728-7917
Lei ZhangCenter for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China. zhangl@math.pku.edu.cn.ORCID http://orcid.org/0000-0001-9972-2051
Zhi QiCenter for Quantitative Biology, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing, China. zhiqi7@pku.edu.cn.ORCID http://orcid.org/0000-0002-1572-9721

Funding

National Natural Science Foundation of China (National Science Foundation of China) T2222022National Natural Science Foundation of China (National Science Foundation of China) T2225009
6 · The paper itself

Abstract

Biomolecules such as nucleic acids and proteins can undergo phase separation to form biomolecular condensates with diverse architectures. Here, we report that the FUS/EWS/TAF15 family fusion oncoprotein FUS-ERG forms hollow co-condensates with double-stranded DNA containing GGAA microsatellites. Through a combination of biochemical assays, super-resolution imaging, and mathematical modeling, we reveal that the interior surface of hollow co-condensates exhibits properties distinct from those of the external surface, a phenomenon we term nested asymmetric phase separation. Furthermore, we harness FUS-ERG for DNA-based information manipulation and demonstrated the hollow condensate morphology uniquely enhances data sorting specificity, enabling targeted DNA deletion within dsDNA libraries and facilitating dynamic, hierarchical data selection. These findings provide critical insights into the biophysical mechanisms underlying multicomponent phase-separated cellular bodies and establish a foundation for leveraging condensate morphology in biotechnology.

Indexed as

Biomolecular CondensatesDNAOncogene Proteins, FusionRNA-Binding Protein FUSHumansDNAOncogene Proteins, FusionRNA-Binding Protein FUS

Identifiers

PMID41203642
PMCPMC12594852

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

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.