Evidence map›Paper›PMID 28934491›Full record

ArticleNucleic acids research2017

Phosphorylation regulates human polη stability and damage bypass throughout the cell cycle.

Federica Bertoletti, Valentina Cea, Chih-Chao Liang, Taiba Lanati, Antonio Maffia, Mario D M Avarello, Lina Cipolla, Alan R Lehmann, Martin A Cohn, Simone Sabbioneda

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 23 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

10 authors at 4 institutions in 2 countries.

Federica BertolettiIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Valentina CeaIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Chih-Chao LiangDepartment of Biochemistry, University of Oxford, OX1 3QU, Oxford, UK.
Taiba LanatiIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Antonio MaffiaIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Mario D M AvarelloIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Lina CipollaIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Alan R LehmannGenome Damage and Stability Centre, University of Sussex, BN1 9RQ, Brighton, UK.
Martin A CohnDepartment of Biochemistry, University of Oxford, OX1 3QU, Oxford, UK.
Simone SabbionedaIstituto di Genetica Molecolare-CNR, 27100, Pavia, Italy.
Istituto di Genetica Molecolare · ITUniversity of Oxford · GBUniversity of Pavia · ITUniversity of Sussex · GB

Funding

Medical Research Council MR/N021002/1
6 · The paper itself

Abstract

DNA translesion synthesis (TLS) is a crucial damage tolerance pathway that oversees the completion of DNA replication in the presence of DNA damage. TLS polymerases are capable of bypassing a distorted template but they are generally considered inaccurate and they need to be tightly regulated. We have previously shown that polη is phosphorylated on Serine 601 after DNA damage and we have demonstrated that this modification is important for efficient damage bypass. Here we report that polη is also phosphorylated by CDK2, in the absence of damage, in a cell cycle-dependent manner and we identify serine 687 as an important residue targeted by the kinase. We discover that phosphorylation on serine 687 regulates the stability of the polymerase during the cell cycle, allowing it to accumulate in late S and G2 when productive TLS is critical for cell survival. Furthermore, we show that alongside the phosphorylation of S601, the phosphorylation of S687 and S510, S512 and/or S514 are important for damage bypass and cell survival after UV irradiation. Taken together our results provide new insights into how cells can, at different times, modulate DNA TLS for improved cell survival.

Indexed as

Cell CycleCell LineCell SurvivalCyclin-Dependent Kinase 2DNA DamageDNA-Directed DNA PolymeraseDNA RepairHumansPhosphorylationProtein StabilitySerineUltraviolet RaysY-Family DNA PolymerasesCDK2 protein, humanCyclin-Dependent Kinase 2DNA-Directed DNA PolymeraseRad30 proteinSerineY-Family DNA Polymerases

Identifiers

PMID28934491
PMCPMC5766190
OpenAlexW2738086907

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.