Evidence map›Paper›PMID 40069174›Full record

ArticleNature communications2025

The DEAD-box helicase eIF4A1/2 acts as RNA chaperone during mitotic exit enabling chromatin decondensation.

Ramona Jühlen, Sabine C Wiesmann, Anja Scheufen, Thilo Stausberg, Isabel Braun, Chantal Strobel, Carmen Llera-Brandt, Sabrina Rappold, Rabia Suluyayla, Marianna Tatarek-Nossol and 6 more

Abstract read
PubMed Full text at PMC Publisher
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

16 authors.

Ramona Jühlen *Institute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany. rjuehlen@ukaachen.de.ORCID http://orcid.org/0000-0002-5689-9030
Sabine C Wiesmann *Institute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.ORCID http://orcid.org/0009-0007-6753-8840
Anja ScheufenInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Thilo StausbergInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.ORCID http://orcid.org/0009-0006-9827-0106
Isabel BraunInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.ORCID http://orcid.org/0009-0000-4829-8529
Chantal StrobelInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Carmen Llera-BrandtInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Sabrina RappoldInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Rabia SuluyaylaInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Marianna Tatarek-NossolInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Birgitt LennartzInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Hongqi LueInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Maximilian W G SchneiderInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.
Juan-Felipe Perez-CorreaInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany.ORCID http://orcid.org/0009-0005-3861-2146
Daniel Moreno-AndrésInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany. dmoreno@ukaachen.de.ORCID http://orcid.org/0000-0003-2160-448X
Wolfram AntoninInstitute of Biochemistry and Molecular Cell Biology, Medical School, RWTH Aachen University, Aachen, Germany. wantonin@ukaachen.de.ORCID http://orcid.org/0000-0003-4669-379X

Funding

Deutsche Forschungsgemeinschaft (German Research Foundation) 107479298
6 · The paper itself

Abstract

During mitosis, chromosomes condense and decondense to segregate faithfully and undamaged. The exact molecular mechanisms are not well understood. We identify the DEAD-box helicase eIF4A1/2 as a critical factor in this process. In a cell-free condensation assay eIF4A1/2 is crucial for this process, relying on its RNA-binding ability but not its ATPase activity. Reducing eIF4A1/2 levels in cells consistently slows down chromatin decondensation during nuclear reformation. Conversely, increasing eIF4A1/2 concentration on mitotic chromosomes accelerates their decondensation. The absence of eIF4A1/2 affects the perichromatin layer, which surrounds the chromosomes during mitosis and consists of RNA and mainly nucleolar proteins. In vitro, eIF4A1/2 acts as an RNA chaperone, dissociating biomolecular condensates of RNA and perichromatin proteins. During mitosis, the chaperone activity of eIF4A1/2 is required to regulate the composition and fluidity of the perichromatin layer, which is crucial for the dynamic reorganization of chromatin as cells exit mitosis.

Indexed as

ChromatinDEAD-box RNA HelicasesEukaryotic Initiation Factor-4AMitosisMolecular ChaperonesRNAHeLa CellsHumansChromatinDEAD-box RNA HelicasesEIF4A1 protein, humanEukaryotic Initiation Factor-4AMolecular ChaperonesRNA

Identifiers

PMID40069174
PMCPMC11897408

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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.