Evidence map›Paper›PMID 40750945›Full record

ArticleNature structural & molecular biology2025

The molecular basis of lamin-specific chromatin interactions.

Baihui Wang, Rafael Kronenberg-Tenga, Valentina Rosti, Emanuele Di Patrizio Soldateschi, Qiang Luo, Ugo Maria Iannacchero, Louise Pinet, Matthias Eibauer, Rajaa Boujemaa-Paterski, Benjamin Schuler and 2 more

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing 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

23 citing papers in PubMed.

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  17. bioRxiv : the preprint server for biology · 2026
    Article
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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

12 authors.

Baihui Wang *Department of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4313-4335
Rafael Kronenberg-Tenga *Department of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-4774-7462
Valentina Rosti *Istituto Nazionale Genetica Molecolare 'Romeo ed Enrica Invernizzi', Milan, Italy.
Emanuele Di Patrizio SoldateschiIstituto Nazionale Genetica Molecolare 'Romeo ed Enrica Invernizzi', Milan, Italy.ORCID http://orcid.org/0000-0002-3091-4386
Qiang LuoDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-8839-2739
Ugo Maria IannaccheroInstitute of Biomedical Technologies, National Research Council, Milan, Italy.ORCID http://orcid.org/0009-0000-5041-922X
Louise PinetDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-5629-6187
Matthias EibauerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0003-0638-9347
Rajaa Boujemaa-PaterskiDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0001-9645-387X
Benjamin SchulerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-5970-4251
Chiara LanzuoloIstituto Nazionale Genetica Molecolare 'Romeo ed Enrica Invernizzi', Milan, Italy. chiara.lanzuolo@cnr.it.ORCID http://orcid.org/0000-0003-2649-6334
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland. omedalia@bioc.uzh.ch.ORCID http://orcid.org/0000-0003-0994-2937

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the cell nucleus, chromatin is anchored to the nuclear lamina, a network of lamin filaments and binding proteins that underly the inner nuclear membrane. The nuclear lamina is involved in chromatin organization through the interaction of lamina-associated domains within the densely packed heterochromatin regions. Using cryo-focused ion beam milling in conjunction with cryo-electron tomography, we analyzed the distribution of nucleosomes at the lamin-chromatin interface at the nanometer scale. Depletion of lamins A and C reduced nucleosome concentration at the nuclear periphery, while B-type lamin depletion contributed to nucleosome density in proximity to the lamina but not further away. We then investigated whether specific lamins can mediate direct interactions with chromatin. Using cryo-electron microscopy, we identified a specific binding motif of the lamin A tail domain that interacts with nucleosomes, distinguishing it from the other lamin isoforms. Furthermore, we examined chromatin structure dynamics using a genome-wide analysis that revealed lamin-dependent macroscopic-scale alterations in gene expression and chromatin remodeling. Our findings provide detailed insights into the dynamic and structural interplay between lamin isoforms and chromatin, molecular interactions that shape chromatin architecture and epigenetic regulation.

Indexed as

ChromatinLaminsLamin Type ALamin Type BChromatin Assembly and DisassemblyCryoelectron MicroscopyHumansNuclear LaminaNucleosomesProtein BindingChromatinLaminsLamin Type ALamin Type BNucleosomes

Identifiers

PMID40750945
PMCPMC12527912

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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.