Evidence map›Paper›PMID 24943839›Full record

ArticleMolecular biology of the cell2014

A role for nuclear envelope-bridging complexes in homology-directed repair.

Rebecca K Swartz, Elisa C Rodriguez, Megan C King

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
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  15. Fission yeast Ase1Molecular biology research communications · 2021
    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

3 authors at 1 institution in 1 country.

Rebecca K SwartzDepartment of Cell Biology, Yale School of Medicine, New Haven, CT -06520.
Elisa C RodriguezDepartment of Cell Biology, Yale School of Medicine, New Haven, CT -06520.
Megan C KingDepartment of Cell Biology, Yale School of Medicine, New Haven, CT -06520 megan.king@yale.edu.
Yale University · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007499 · NIGMS · YALE UNIVERSITY · PI CARLSON, JOHN R, REINKE, VALERIE J · 1985 to 2022
$13.9M
INSTITUTIONAL NATIONAL RESEARCH SERVICE AWARDT32GM007324 · NIGMS · YALE UNIVERSITY · PI BENNETT, ANTON M · 1987 to 2022
$6.2M
The role of nuclear architecture in adaptationDP2OD008429 · OD · YALE UNIVERSITY · PI KING, MEGAN C · 2011 to 2011
$2.5M
NIGMS NIH HHS 2T32GM007324-36A1NIGMS NIH HHS T32 GM007324NIGMS NIH HHS T32 GM007499NIGMS NIH HHS T32GM007499NIH HHS DP2 OD008429NIH HHS DP2OD008429-01
6 · The paper itself

Abstract

Unless efficiently and faithfully repaired, DNA double-strand breaks (DSBs) cause genome instability. We implicate a Schizosaccharomyces pombe nuclear envelope-spanning linker of nucleoskeleton and cytoskeleton (LINC) complex, composed of the Sad1/Unc84 protein Sad1 and Klarsicht/Anc1/SYNE1 homology protein Kms1, in the repair of DSBs. An induced DSB associates with Sad1 and Kms1 in S/G2 phases of the cell cycle, connecting the DSB to cytoplasmic microtubules. DSB resection to generate single-stranded DNA and the ATR kinase drive the formation of Sad1 foci in response to DNA damage. Depolymerization of microtubules or loss of Kms1 leads to an increase in the number and size of DSB-induced Sad1 foci. Further, Kms1 and the cytoplasmic microtubule regulator Mto1 promote the repair of an induced DSB by gene conversion, a type of homology-directed repair. kms1 genetically interacts with a number of genes involved in homology-directed repair; these same gene products appear to attenuate the formation or promote resolution of DSB-induced Sad1 foci. We suggest that the connection of DSBs with the cytoskeleton through the LINC complex may serve as an input to repair mechanism choice and efficiency.

Indexed as

DNA RepairCell CycleDNA Breaks, Double-StrandedDNA, FungalDNA, Single-StrandedGenomic InstabilityMicrotubulesNuclear EnvelopeSchizosaccharomycesSchizosaccharomyces pombe ProteinsDNA, FungalDNA, Single-StrandedKMS1 protein, S pombeSAD1 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID24943839
PMCPMC4142617
OpenAlexW2140826954

What OpenQuestion holds

Textmetadata
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.