Evidence map›Paper›PMID 32609828›Full record

ArticleNucleic acids research2020

DSS1 and ssDNA regulate oligomerization of BRCA2.

Hang Phuong Le, Xiaoyan Ma, Jorge Vaquero, Megan Brinkmeyer, Fei Guo, Wolf-Dietrich Heyer, Jie Liu

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

23 citing papers in PubMed, 34 citations in OpenAlex.

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  11. CRISPR/Cas9-Targeted Disruption of Two Highly HomologousInternational journal of molecular sciences · 2023
    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

7 authors at 1 institution in 1 country.

Hang Phuong LeDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
Xiaoyan MaDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
Jorge VaqueroDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
Megan BrinkmeyerDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
Fei GuoDepartment of Molecular and Cellular Biology, University of California, Davis, Davis, CA 95616-8665, USA.
Wolf-Dietrich HeyerDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
Jie LiuDepartment of Microbiology and Molecular Genetics, University of California, Davis, Davis, CA 95616-8665, USA.
University of California, Davis · US

Funding

Staff InvestigatorsP30CA093373 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI Laura Marcu · 2002 to 2026
$84.9M
RECOMBINATIONAL MECHANISMS OF DNA REPAIR IN EUKARYOTESR01GM058015 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI HEYER, WOLF-DIETRICH · 2000 to 2025
$8.8M
Regulation of Recombinational DNA RepairR01CA092276 · NCI · UNIVERSITY OF CALIFORNIA DAVIS · PI HEYER, WOLF-DIETRICH · 2001 to 2020
$5.2M
Training Program in Oncogenic Signals and Chromosome BiologyT32CA108459 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI HEYER, WOLF-DIETRICH · 2006 to 2020
$3.6M
Structure and Function of the Tumor Suppressor Protein BRCA2R21CA187561 · NCI · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LIU, JIE · 2015 to 2016
$374k
NCI NIH HHS CA92267NCI NIH HHS P30 CA093373NCI NIH HHS R01 CA092276NCI NIH HHS R21 CA187561NCI NIH HHS T32 CA108459NIGMS NIH HHS R01 GM058015
6 · The paper itself

Abstract

The tumor suppressor BRCA2 plays a key role in initiating homologous recombination by facilitating RAD51 filament formation on single-stranded DNA. The small acidic protein DSS1 is a crucial partner to BRCA2 in this process. In vitro and in cells (1,2), BRCA2 associates into oligomeric complexes besides also existing as monomers. A dimeric structure was further characterized by electron microscopic analysis (3), but the functional significance of the different BRCA2 assemblies remains to be determined. Here, we used biochemistry and electron microscopic imaging to demonstrate that the multimerization of BRCA2 is counteracted by DSS1 and ssDNA. When validating the findings, we identified three self-interacting regions and two types of self-association, the N-to-C terminal and the N-to-N terminal interactions. The N-to-C terminal self-interaction of BRCA2 is sensitive to DSS1 and ssDNA. The N-to-N terminal self-interaction is modulated by ssDNA. Our results define a novel role of DSS1 to regulate BRCA2 in an RPA-independent fashion. Since DSS1 is required for BRCA2 function in recombination, we speculate that the monomeric and oligomeric forms of BRCA2 might be active for different cellular events in recombinational DNA repair and replication fork stabilization.

Indexed as

AnimalsBRCA2 ProteinCell LineCricetulusDNA, Single-StrandedHumansProteasome Endopeptidase ComplexProtein MultimerizationBRCA2 ProteinBRCA2 protein, humanDNA, Single-StrandedProteasome Endopeptidase ComplexSEM1 protein, human

Identifiers

PMID32609828
PMCPMC7641332
OpenAlexW3040523952

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.