Evidence map›Paper›PMID 38587486›Full record

ArticleThe Journal of cell biology2024

LLPS of FXR proteins drives replication organelle clustering for β-coronaviral proliferation.

Meng Li, Yali Hou, Yuzheng Zhou, Zhenni Yang, Hongyu Zhao, Tao Jian, Qianxi Yu, Fuxing Zeng, Xiaotian Liu, Zheng Zhang and 1 more

Abstract read
In one paragraph

Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Pull-Down Techniques for Determining Virus-Host Protein Interactions.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  10. Review
  11. Article
  12. Review
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.

Meng Li *Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0000-0002-3728-1817
Yali Hou *Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0009-0007-5491-1829
Yuzheng Zhou *Institute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0009-0000-2206-0782
Zhenni Yang *Shenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0000-0003-0150-3980
Hongyu ZhaoNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, P.R. China.ORCID 0009-0003-7675-7800
Tao JianDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Kowloon, P.R. China.ORCID 0000-0002-9754-1051
Qianxi YuDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, P.R. China.ORCID 0009-0007-9972-9860
Fuxing ZengDepartment of Systems Biology, School of Life Sciences, Southern University of Science and Technology, Shenzhen, P.R. China.ORCID 0000-0003-0790-0151
Xiaotian LiuShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0000-0001-5009-1287
Zheng ZhangInstitute for Hepatology, National Clinical Research Center for Infectious Disease, Shenzhen Third People's Hospital, The Second Affiliated Hospital, School of Medicine, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0000-0002-3544-1389
Yan G ZhaoShenzhen Key Laboratory of Biomolecular Assembling and Regulation, School of Life Sciences, Southern University of Science and Technology , Shenzhen, P.R. China.ORCID 0000-0002-4588-6752

Funding

Guangdong Innovative and Entrepreneurial Research Team Program 2021ZT09Y104Guangdong Program 2019CX01Y222Guangdong Science and Technology Plan Project, Construction of high-level biosafety laboratories 2021B1212030010National Key Research and Development Program 2021YFA1300800National Natural Science Foundation of China 32222021R&D Program of Guangzhou Laboratory GZNL2024A01008Shenzhen Fundamental Research InstitutionsShenzhen-Hong Kong Institute of Brain Science 2023SHIBS0002Shenzhen Science and Technology Program ZDSYS20220402111000001Shenzhen Talent Program KQTD20210811090115021
6 · The paper itself

Abstract

β-Coronaviruses remodel host endomembranes to form double-membrane vesicles (DMVs) as replication organelles (ROs) that provide a shielded microenvironment for viral RNA synthesis in infected cells. DMVs are clustered, but the molecular underpinnings and pathophysiological functions remain unknown. Here, we reveal that host fragile X-related (FXR) family proteins (FXR1/FXR2/FMR1) are required for DMV clustering induced by expression of viral non-structural proteins (Nsps) Nsp3 and Nsp4. Depleting FXRs results in DMV dispersion in the cytoplasm. FXR1/2 and FMR1 are recruited to DMV sites via specific interaction with Nsp3. FXRs form condensates driven by liquid-liquid phase separation, which is required for DMV clustering. FXR1 liquid droplets concentrate Nsp3 and Nsp3-decorated liposomes in vitro. FXR droplets facilitate recruitment of translation machinery for efficient translation surrounding DMVs. In cells depleted of FXRs, SARS-CoV-2 replication is significantly attenuated. Thus, SARS-CoV-2 exploits host FXR proteins to cluster viral DMVs via phase separation for efficient viral replication.

Indexed as

COVID-19Fragile X Messenger Ribonucleoprotein 1LiposomesRNA-Binding ProteinsSARS-CoV-2Cell ProliferationCluster AnalysisCytoplasmHeLa CellsHumansOrganellesViral Nonstructural ProteinsFMR1 protein, humanFragile X Messenger Ribonucleoprotein 1FXR1 protein, humanFXR2 protein, humanLiposomesRNA-Binding ProteinsViral Nonstructural Proteins

Identifiers

PMID38587486
PMCPMC11001562

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.