Evidence map›Paper›PMID 39095374›Full record

ArticleNature communications2024

Prion-like domain mediated phase separation of ARID1A promotes oncogenic potential of Ewing's sarcoma.

Yong Ryoul Kim, Jaegeon Joo, Hee Jung Lee, Chaelim Kim, Ju-Chan Park, Young Suk Yu, Chang Rok Kim, Do Hui Lee, Joowon Cha, Hyemin Kwon and 8 more

Abstract read
In one paragraph

Article in Nature communications, 2024. 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
–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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. [Mechanisms of RNA-binding protein phase separation in steroid-associated necrosis of the femoral head].Zhong nan da xue xue bao. Yi xue ban = Journal of Central South University. Medical sciences · 2026
    Review
  4. Review
  5. Article
  6. Article
  7. Molecular basis of EWS interdomain self-association and its role in condensate formation.Protein science : a publication of the Protein Society · 2025
    Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Yeast Prions: Discovery, Nature, Cellular Manipulation and Implication.Journal of microbiology and biotechnology · 2025
    Review
  13. Article
  14. Phase Separation in Chromatin Organization and Human Diseases.International journal of molecular sciences · 2025
    Review
  15. Review
  16. Article
  17. Liquid condensates: a new barrier to loop extrusion?Cellular and molecular life sciences : CMLS · 2025
    Review
  18. Article
  19. Article
  20. 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

18 authors.

Yong Ryoul Kim *Creative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.
Jaegeon Joo *Department of Biological Sciences, Korea Advanced Institute of Science & Technology, Daejeon, South Korea.
Hee Jung LeeInterdisciplinary Program in Bioengineering, Seoul National University, Seoul, South Korea.
Chaelim KimInterdisciplinary Program in Bioengineering, Seoul National University, Seoul, South Korea.
Ju-Chan ParkResearch Center of Genomic Medicine Institute, Seoul National University College of Medicine, Seoul, South Korea.ORCID 0000-0001-5938-7420
Young Suk YuCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.
Chang Rok KimCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.ORCID 0000-0002-6578-880X
Do Hui LeeCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.
Joowon ChaCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.
Hyemin KwonCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea.
Kimberley M HanssenHopp-Children's Cancer Center (KiTZ), Heidelberg, Germany.ORCID 0000-0002-2919-3104
Thomas G P GrünewaldHopp-Children's Cancer Center (KiTZ), Heidelberg, Germany.ORCID 0000-0003-0920-7377
Murim ChoiDepartment of Biomedical Sciences, Seoul National University College of Medicine, Seoul, South Korea.ORCID 0000-0002-9195-1455
Ilkyu HanDepartment of Orthopaedic Surgery, Seoul National University College of Medicine, Seoul, South Korea.
Sangsu BaeResearch Center of Genomic Medicine Institute, Seoul National University College of Medicine, Seoul, South Korea.ORCID 0000-0003-3615-8566
Inkyung JungDepartment of Biological Sciences, Korea Advanced Institute of Science & Technology, Daejeon, South Korea. ijung@kaist.ac.kr.ORCID 0000-0002-5885-2754
Yongdae ShinInterdisciplinary Program in Bioengineering, Seoul National University, Seoul, South Korea. ydshin@snu.ac.kr.ORCID 0000-0003-3441-1986
Sung Hee BaekCreative Research Initiatives Center for Epigenetic Code and Diseases, School of Biological Sciences, Seoul National University, Seoul, South Korea. sbaek@snu.ac.kr.ORCID 0000-0002-0588-8243

Funding

National Research Foundation of Korea (NRF) 2017R1A3B1023387National Research Foundation of Korea (NRF) NRF-2023R1A2C3002773National Research Foundation of Korea (NRF) RS-2023-00211612Seoul National University 2019
6 · The paper itself

Abstract

Liquid-liquid phase separation (LLPS) facilitates the formation of membraneless organelles within cells, with implications in various biological processes and disease states. AT-rich interactive domain-containing protein 1A (ARID1A) is a chromatin remodeling factor frequently associated with cancer mutations, yet its functional mechanism remains largely unknown. Here, we find that ARID1A harbors a prion-like domain (PrLD), which facilitates the formation of liquid condensates through PrLD-mediated LLPS. The nuclear condensates formed by ARID1A LLPS are significantly elevated in Ewing's sarcoma patient specimen. Disruption of ARID1A LLPS results in diminished proliferative and invasive abilities in Ewing's sarcoma cells. Through genome-wide chromatin structure and transcription profiling, we identify that the ARID1A condensate localizes to EWS/FLI1 target enhancers and induces long-range chromatin architectural changes by forming functional chromatin remodeling hubs at oncogenic target genes. Collectively, our findings demonstrate that ARID1A promotes oncogenic potential through PrLD-mediated LLPS, offering a potential therapeutic approach for treating Ewing's sarcoma.

Indexed as

Chromatin Assembly and DisassemblyDNA-Binding ProteinsRNA-Binding Protein EWSSarcoma, EwingTranscription FactorsAnimalsBone NeoplasmsCarcinogenesisCell Line, TumorCell ProliferationChromatinGene Expression Regulation, NeoplasticHumansMiceOncogene Proteins, FusionPhase SeparationARID1A protein, humanChromatinDNA-Binding ProteinsEWS-FLI fusion proteinOncogene Proteins, FusionProto-Oncogene Protein c-fli-1RNA-Binding Protein EWSTranscription Factors

Identifiers

PMID39095374
PMCPMC11297139

What OpenQuestion holds

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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.