Evidence map›Paper›PMID 38632359›Full record

ArticleNature structural & molecular biology2024

DNA double-strand break-capturing nuclear envelope tubules drive DNA repair.

Mitra Shokrollahi, Mia Stanic, Anisha Hundal, Janet N Y Chan, Defne Urman, Chris A Jordan, Anne Hakem, Roderic Espin, Jun Hao, Rehna Krishnan and 6 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
11.9field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 54 citations in OpenAlex.

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  20. Recent advances in nuclear actin research.Nucleus (Austin, Tex.) · 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

16 authors at 5 institutions in 3 countries.

Mitra Shokrollahi *Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-9024-6666
Mia Stanic *Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0003-2149-2916
Anisha Hundal *Department of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0003-2018-8111
Janet N Y ChanDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0001-5644-985X
Defne UrmanDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0000-8598-0287
Chris A JordanDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0006-5392-3468
Anne HakemPrincess Margaret Cancer Research Centre, University Health Network, Toronto, Ontario, Canada.ORCID http://orcid.org/0009-0009-6432-0525
Roderic EspinProCURE, Catalan Institute of Oncology, Oncobell, Bellvitge Institute for Biomedical Research (IDIBELL), L'Hospitalet del Llobregat, Barcelona, Spain.ORCID http://orcid.org/0000-0003-2494-0964
Jun HaoPrincess Margaret Cancer Research Centre, University Health Network, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-8989-8771
Rehna KrishnanPrincess Margaret Cancer Research Centre, University Health Network, Toronto, Ontario, Canada.
Philipp G MaassDepartment of Molecular Genetics, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0002-2742-8301
Brendan C DicksonDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada.ORCID http://orcid.org/0000-0003-2269-6216
Manoor P HandeDepartment of Physiology, Yong Loo Lin School of Medicine, National University of Singapore, Singapore, Singapore.ORCID http://orcid.org/0000-0002-4511-6256
Miquel A PujanaProCURE, Catalan Institute of Oncology, Oncobell, Bellvitge Institute for Biomedical Research (IDIBELL), L'Hospitalet del Llobregat, Barcelona, Spain.ORCID http://orcid.org/0000-0003-3222-4044
Razqallah HakemDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada. razq.hakem@uhnresearch.ca.ORCID http://orcid.org/0000-0001-5948-7931
Karim MekhailDepartment of Laboratory Medicine and Pathobiology, Temerty Faculty of Medicine, University of Toronto, Toronto, Ontario, Canada. karim.mekhail@utoronto.ca.ORCID http://orcid.org/0000-0002-6084-020X
University of Toronto · CAUniversity Health Network · CAInstituto de Salud Carlos III · ESMount Sinai Hospital · CANational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Current models suggest that DNA double-strand breaks (DSBs) can move to the nuclear periphery for repair. It is unclear to what extent human DSBs display such repositioning. Here we show that the human nuclear envelope localizes to DSBs in a manner depending on DNA damage response (DDR) kinases and cytoplasmic microtubules acetylated by α-tubulin acetyltransferase-1 (ATAT1). These factors collaborate with the linker of nucleoskeleton and cytoskeleton complex (LINC), nuclear pore complex (NPC) protein NUP153, nuclear lamina and kinesins KIF5B and KIF13B to generate DSB-capturing nuclear envelope tubules (dsbNETs). dsbNETs are partly supported by nuclear actin filaments and the circadian factor PER1 and reversed by kinesin KIFC3. Although dsbNETs promote repair and survival, they are also co-opted during poly(ADP-ribose) polymerase (PARP) inhibition to restrain BRCA1-deficient breast cancer cells and are hyper-induced in cells expressing the aging-linked lamin A mutant progerin. In summary, our results advance understanding of nuclear structure-function relationships, uncover a nuclear-cytoplasmic DDR and identify dsbNETs as critical factors in genome organization and stability.

Indexed as

DNA Breaks, Double-StrandedDNA RepairNuclear EnvelopeAcetyltransferasesBRCA1 ProteinHeLa CellsHumansKinesinsLamin Type AMicrotubulesNuclear Pore Complex ProteinsAcetyltransferasesBRCA1 ProteinKinesinsLamin Type ANuclear Pore Complex ProteinsNUP153 protein, human

Identifiers

PMID38632359
OpenAlexW4394881884

What OpenQuestion holds

Textmetadata
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.