Evidence map›Paper›PMID 36301259›Full record

ArticleThe Journal of cell biology2022

Nucleoplasmic lamin C rapidly accumulates at sites of nuclear envelope rupture with BAF and cGAS.

Yohei Kono, Stephen A Adam, Yuko Sato, Karen L Reddy, Yixian Zheng, Ohad Medalia, Robert D Goldman, Hiroshi Kimura, Takeshi Shimi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.6field-weighted citation impact, top 6% of its field
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

36 citing papers in PubMed, 45 citations in OpenAlex.

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  18. The molecular basis of lamin-specific chromatin interactions.Nature structural & molecular biology · 2025
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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

9 authors at 5 institutions in 3 countries.

Yohei KonoCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0001-8264-9417
Stephen A AdamDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.ORCID 0000-0003-3444-7655
Yuko SatoCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0002-7805-9171
Karen L ReddyDepartment of Biological Chemistry, Johns Hopkins University, Baltimore, MD.ORCID 0000-0003-4548-5999
Yixian ZhengDepartment of Embryology, Carnegie Institution for Science, Baltimore, MD.ORCID 0000-0002-1992-4014
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID 0000-0003-0994-2937
Robert D GoldmanDepartment of Cell and Developmental Biology, Feinberg School of Medicine, Northwestern University, Chicago, IL.ORCID 0000-0003-0383-1435
Hiroshi KimuraCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0003-0854-083X
Takeshi ShimiCell Biology Center, Institute of Innovative Research, Tokyo Institute of Technology, Yokohama, Japan.ORCID 0000-0002-9864-1820
Tokyo Institute of Technology · JPNorthwestern University · USCarnegie Institution for Science · USJohns Hopkins University · USUniversity of Zurich · CH

Funding

Differential Regulation and Roles of A-type Lamins in Early G1R01GM132427 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI REDDY, KAREN LYNN, WILSON, KATHERINE L · 2020 to 2023
$2.4M
NIGMS NIH HHS R01 GM132427
6 · The paper itself

Abstract

In mammalian cell nuclei, the nuclear lamina (NL) underlies the nuclear envelope (NE) to maintain nuclear structure. The nuclear lamins, the major structural components of the NL, are involved in the protection against NE rupture induced by mechanical stress. However, the specific role of the lamins in repair of NE ruptures has not been fully determined. Our analyses using immunofluorescence and live-cell imaging revealed that the nucleoplasmic pool of lamin C rapidly accumulated at sites of NE rupture induced by laser microirradiation in mouse embryonic fibroblasts. The accumulation of lamin C at the rupture sites required both the immunoglobulin-like fold domain that binds to barrier-to-autointegration factor (BAF) and a nuclear localization signal. The accumulation of nuclear BAF and cytoplasmic cyclic GMP-AMP synthase (cGAS) at the rupture sites was in part dependent on lamin A/C. These results suggest that nucleoplasmic lamin C, BAF, and cGAS concertedly accumulate at sites of NE rupture for rapid repair.

Indexed as

Lamin Type ANuclear EnvelopeAnimalsCell NucleusCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseDNA-Binding ProteinsFibroblastsMembrane ProteinsMiceNucleotidyltransferasescGAS protein, mouseCyclic Guanosine Monophosphate-Adenosine Monophosphate SynthaseDNA-Binding Proteinslamin CLamin Type AMembrane ProteinsNucleotidyltransferases

Identifiers

PMID36301259
PMCPMC9617480
OpenAlexW4307643636

What OpenQuestion holds

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LicenceCC BY
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.