Evidence map›Paper›PMID 19605351›Full record

ArticleThe Journal of biological chemistry2009

HSSB1 and hSSB2 form similar multiprotein complexes that participate in DNA damage response.

Yongjiang Li, Emma Bolderson, Rakesh Kumar, Parameswary A Muniandy, Yutong Xue, Derek J Richard, Michael Seidman, Tej K Pandita, Kum Kum Khanna, Weidong Wang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 1 pooled it
3.5field-weighted citation impact, top 7% 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

76 citing papers in PubMed, 1 synthesis or guideline pooled it, 123 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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 3 countries.

Yongjiang LiLaboratory of Genetics, NIA, National Institutes of Health, NIH Biomedical Research Center, Baltimore, Maryland 21224, USA.
Emma Bolderson
Rakesh Kumar
Parameswary A Muniandy
Yutong Xue
Derek J Richard
Michael Seidman
Tej K Pandita
Kum Kum Khanna
Weidong Wang
QIMR Berghofer Medical Research Institute · AULaboratory of Molecular Genetics · PLNational Institutes of Health · USWashington University in St. Louis · US

Funding

Repair of localized DNA damageZIAAG000746 · NIA · NATIONAL INSTITUTE ON AGING · PI SEIDMAN, MICHAEL · 2009 to 2025
$30.0M
Characterization of a Complex Involved In Rothmund-Thomson SyndromeZIAAG000661 · NIA · NATIONAL INSTITUTE ON AGING · PI WANG, WEIDONG · 2009 to 2019
$6.1M
CHROMATIN MODIFYING FACTORS CONTROL RADIATION RESPONSE AND GENOMIC STABILITYR01CA129537 · NCI · WASHINGTON UNIVERSITY · PI PANDITA, TEJ K · 2008 to 2018
$3.3M
Functional Characterization of the Mammalian MOF Gene ProductR01CA123232 · NCI · WASHINGTON UNIVERSITY · PI PANDITA, TEJ K · 2007 to 2011
$1.5M
ISOLATION OF PROTEIN COMPLEX INVOLVED IN BLOOM SYNDROMEZ01AG000657 · NIA · NATIONAL INSTITUTE ON AGING · PI WANG, WEIDONG · 2000 to 2008
$636k
Double strand break repairZIAAG000747 · NIA · NATIONAL INSTITUTE ON AGING · PI SEIDMAN, MICHAEL · 2009 to 2010
$320k
Intramural NIH HHS Z01 AG000657NCI NIH HHS CA123232NCI NIH HHS CA129537NCI NIH HHS R01 CA123232NCI NIH HHS R01 CA129537
6 · The paper itself

Abstract

hSSB1 (human single strand DNA-binding protein 1) has been shown to participate in homologous recombination (HR)-dependent repair of DNA double strand breaks (DSBs) and ataxia telangiectasia-mutated (ATM)-mediated checkpoint pathways. Here we present evidence that hSSB2, a homolog of hSSB1, plays a role similar to hSSB1 in DNA damage-response pathways. This was evidenced by findings that hSSB2-depleted cells resemble hSSB1-depleted cells in hypersensitivity to DNA-damaging reagents, reduced efficiency in HR-dependent repair of DSBs, and defective ATM-dependent phosphorylation. Notably, hSSB1 and hSSB2 form separate complexes with two identical proteins, INTS3 and hSSBIP1 (C9ORF80). Cells depleted of INTS3 and hSSBIP1 also exhibited hypersensitivity to DNA damage reagents, chromosomal instability, and reduced ATM-dependent phosphorylation. hSSBIP1 was rapidly recruited to laser-induced DSBs, a feature also similar to that reported for hSSB1. Depletion of INTS3 decreased the stability of hSSB1 and hSSBIP1, suggesting that INTS3 may provide a scaffold to allow proper assembly of the hSSB complexes. Thus, our data demonstrate that hSSB1 and hSSB2 form two separate complexes with similar structures, and both are required for efficient HR-dependent repair of DSBs and ATM-dependent signaling pathways.

Indexed as

DNA DamageCell LineDNA-Binding ProteinsDNA RepairHumansMitochondrial ProteinsMultiprotein ComplexesPhosphorylationProtein BindingDNA-Binding ProteinsINIP protein, humanINTS3 protein, humanMitochondrial ProteinsMultiprotein ComplexesNABP2 protein, humanSSBP2 protein, human

Identifiers

PMID19605351
PMCPMC2749126
OpenAlexW2046691395

What OpenQuestion holds

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LicenceCC BY-NC
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.