Evidence map›Paper›PMID 25990736›Full record

ArticleNucleic acids research2015

SLX4 contributes to telomere preservation and regulated processing of telomeric joint molecule intermediates.

Jaya Sarkar, Bingbing Wan, Jinhu Yin, Haritha Vallabhaneni, Kent Horvath, Tomasz Kulikowicz, Vilhelm A Bohr, Yanbin Zhang, Ming Lei, Yie Liu

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
4.3field-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

41 citing papers in PubMed, 67 citations in OpenAlex.

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  17. Coordinated roles of SLX4 and MutSβ in DNA repair and the maintenance of genome stability.Critical reviews in biochemistry and molecular biology · 2021
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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

10 authors at 4 institutions in 2 countries.

Jaya SarkarLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Bingbing WanNational Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 333 Haike Road, Shanghai 200031, China Department of Biological Chemistry, University of Michigan Medical School, 1150 W. Medical Center Drive, Ann Arbor, MI 48109, USA.
Jinhu YinLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Haritha VallabhaneniLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Kent HorvathLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Tomasz KulikowiczLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Vilhelm A BohrLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA.
Yanbin ZhangDepartment of Biochemistry and Molecular Biology, University of Miami Miller School of Medicine, Miami, FL 33136, USA.
Ming LeiLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA National Center for Protein Science Shanghai, State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 333 Haike Road, Shanghai 200031, China.
Yie LiuLaboratory of Molecular Gerontology, National Institute on Aging/National Institute of Health, 251 Bayview Blvd, Baltimore, MD 21224, USA liuyie@mail.nih.gov.
National Institute on Aging · USAnn Arbor Center for Independent Living · USMRC Laboratory of Molecular Biology · GBUniversity of Miami · US

Funding

Function of RecQ helicases in genome stabilityZIAAG000726 · NIA · NATIONAL INSTITUTE ON AGING · PI BROSH, ROBERT · 2009 to 2025
$13.1M
Structure nucleases in telomere secondary structure resolutionZIAAG000754 · NIA · NATIONAL INSTITUTE ON AGING · PI LIU, YIE · 2013 to 2024
$8.4M
The role of DNA damage and repair at telomeresZIAAG000744 · NIA · NATIONAL INSTITUTE ON AGING · PI LIU, YIE · 2009 to 2016
$3.9M
6 · The paper itself

Abstract

SLX4 assembles a toolkit of endonucleases SLX1, MUS81 and XPF, which is recruited to telomeres via direct interaction of SLX4 with TRF2. Telomeres present an inherent obstacle for DNA replication and repair due to their high propensity to form branched DNA intermediates. Here we provide novel insight into the mechanism and regulation of the SLX4 complex in telomere preservation. SLX4 associates with telomeres throughout the cell cycle, peaking in late S phase and under genotoxic stress. Disruption of SLX4's interaction with TRF2 or SLX1 and SLX1's nuclease activity independently causes telomere fragility, suggesting a requirement of the SLX4 complex for nucleolytic resolution of branched intermediates during telomere replication. Indeed, the SLX1-SLX4 complex processes a variety of telomeric joint molecules in vitro. The nucleolytic activity of SLX1-SLX4 is negatively regulated by telomeric DNA-binding proteins TRF1 and TRF2 and is suppressed by the RecQ helicase BLM in vitro. In vivo, in the presence of functional BLM, telomeric circle formation and telomere sister chromatid exchange, both arising out of nucleolytic processing of telomeric homologous recombination intermediates, are suppressed. We propose that the SLX4-toolkit is a telomere accessory complex that, in conjunction with other telomere maintenance proteins, ensures unhindered, but regulated telomere maintenance.

Indexed as

Cell CycleDNAEndodeoxyribonucleasesEndonucleasesHeLa CellsHomologous RecombinationHumansRecombinasesRecQ HelicasesSister Chromatid ExchangeTelomereTelomere-Binding ProteinsBloom syndrome proteinDNAEndodeoxyribonucleasesEndonucleasesRecombinasesRecQ HelicasesSLX1 protein, humanSLX4 protein, humanTelomere-Binding Proteins

Identifiers

PMID25990736
PMCPMC4499145
OpenAlexW1795141977

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.