Evidence map›Paper›PMID 21098111›Full record

ArticleThe Journal of cell biology2010

Phosphorylated Rad18 directs DNA polymerase η to sites of stalled replication.

Tovah A Day, Komariah Palle, Laura R Barkley, Naoko Kakusho, Ying Zou, Satoshi Tateishi, Alain Verreault, Hisao Masai, Cyrus Vaziri

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

48 citing papers in PubMed, 76 citations in OpenAlex.

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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

9 authors at 6 institutions in 3 countries.

Tovah A DayDepartment of Genetics and Genomics and 2 Center for Human Genetics, Boston University School of Medicine, Boston, MA 02118, USA.
Komariah Palle
Laura R Barkley
Naoko Kakusho
Ying Zou
Satoshi Tateishi
Alain Verreault
Hisao Masai
Cyrus Vaziri
Boston University · USTokyo Metropolitan Institute of Medical Science · JPUniversity of North Carolina at Chapel Hill · USCenter for Human Genetics · USInstitute for Research in Immunology and Cancer · CAKumamoto University · JP

Funding

UNC-CH CENTER FOR ENVIRONMENTAL HEALTH &SUSCEPTIBILITYP30ES010126 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Melissa A. Troester · 2001 to 2026
$36.3M
A Novel Carcinogen-Induced Cell Cycle CheckpointR01ES009558 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI VAZIRI, CYRUS · 2002 to 2016
$4.8M
A Novel Role for the Fanconi Anemia Pathway in Replication of B[a]P-Adducted DNAR01ES016280 · NIEHS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI VAZIRI, CYRUS · 2008 to 2012
$1.5M
NOVEL CARCINOGEN INDUCED CELL CYCLE CHECKPOINTR29ES009558 · NIEHS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI VAZIRI, CYRUS · 1998 to 2001
$221k
NIEHS NIH HHS ES016280NIEHS NIH HHS ES09558NIEHS NIH HHS P30 ES010126NIEHS NIH HHS R01 ES009558NIEHS NIH HHS R01 ES016280NIEHS NIH HHS R29 ES009558
6 · The paper itself

Abstract

The E3 ubiquitin ligase Rad18 guides DNA Polymerase eta (Polη) to sites of replication fork stalling and mono-ubiquitinates proliferating cell nuclear antigen (PCNA) to facilitate binding of Y family trans-lesion synthesis (TLS) DNA polymerases during TLS. However, it is unclear exactly how Rad18 is regulated in response to DNA damage and how Rad18 activity is coordinated with progression through different phases of the cell cycle. Here we identify Rad18 as a novel substrate of the essential protein kinase Cdc7 (also termed Dbf4/Drf1-dependent Cdc7 kinase [DDK]). A serine cluster in the Polη-binding motif of Rad 18 is phosphorylated by DDK. Efficient association of Rad18 with Polη is dependent on DDK and is necessary for redistribution of Polη to sites of replication fork stalling. This is the first demonstration of Rad18 regulation by direct phosphorylation and provides a novel mechanism for integration of S phase progression with postreplication DNA repair to maintain genome stability.

Indexed as

DNA ReplicationCell Cycle ProteinsCell Line, TumorCells, CulturedDNA-Binding ProteinsDNA-Directed DNA PolymeraseHumansMicroscopy, FluorescencePhosphorylationProliferating Cell Nuclear AntigenProtein Serine-Threonine KinasesS PhaseTransfectionUbiquitin-Protein LigasesY-Family DNA PolymerasesCDC7 protein, humanCell Cycle ProteinsDNA-Binding ProteinsDNA-Directed DNA PolymeraseProliferating Cell Nuclear AntigenProtein Serine-Threonine KinasesRAD18 protein, humanRad30 proteinUbiquitin-Protein LigasesY-Family DNA Polymerases

Identifiers

PMID21098111
PMCPMC2995173
OpenAlexW2141115493

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.