Evidence map›Paper›PMID 20154705›Full record

ArticleNature structural & molecular biology2010

A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination.

Dong-Hyun Lee, Yunfeng Pan, Shlomo Kanner, Patrick Sung, James A Borowiec, Dipanjan Chowdhury

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing papers in PubMed
6.6field-weighted citation impact, top 2% 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

93 citing papers in PubMed, 163 citations in OpenAlex.

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33 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

6 authors at 3 institutions in 1 country.

Dong-Hyun Lee[1] Dana Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, USA. [2] Department of Radiation Oncology, Harvard Medical School, Boston, Massachusetts, USA.
Yunfeng Pan
Shlomo Kanner
Patrick Sung
James A Borowiec
Dipanjan Chowdhury
Dana-Farber Cancer Institute · USNew York University · USYale University · US

Funding

Regulation of RPA Activity in DNA RepairR01GM083185 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI BOROWIEC, JAMES A. · 2009 to 2014
$2.1M
NIGMS NIH HHS GM083185NIGMS NIH HHS R01 GM083185
6 · The paper itself

Abstract

Double-stranded DNA breaks (DSBs) induce a phosphorylation-mediated signaling cascade, but the role of phosphatases in this pathway remains unclear. Here we show that human protein phosphatase 4 (PP4) dephosphorylates replication protein A (RPA) subunit RPA2, regulating its role in the DSB response. PP4R2, a regulatory subunit of PP4, mediates the DNA damage-dependent association between RPA2 and the PP4C catalytic subunit. PP4 efficiently dephosphorylates phospho-RPA2 in vitro, and silencing PP4R2 in cells alters the kinetics and pattern of RPA2 phosphorylation. Depletion of PP4R2 impedes homologous recombination (HR) via inefficient loading of the essential HR factor RAD51, causing an extended G2-M checkpoint and hypersensitivity to DNA damage. Cells expressing phosphomimetic RPA2 mutants have a comparable phenotype, suggesting that PP4-mediated dephosphorylation of RPA2 is necessary for an efficient DNA-damage response. These observations provide new insight into the role and regulation of RPA phosphorylation in HR-mediated repair.

Indexed as

AnimalsCatalytic DomainCell CycleCell LineCell Line, TumorCell SurvivalComet AssayDNA RepairFluorescent Antibody TechniqueHeLa CellsHumansImmunoprecipitationKineticsPhosphoprotein PhosphatasesPhosphorylationProtein BindingPhosphoprotein Phosphatasesprotein phosphatase 4Protein SubunitsRad51 RecombinaseReplication Protein ARNA, Small Interfering

Identifiers

PMID20154705
PMCPMC3057140
OpenAlexW2122543263

What OpenQuestion holds

Textmetadata
LicenceTDM
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.