Evidence map›Paper›PMID 32350109›Full record

ArticleThe Journal of biological chemistry2020

Multisite SUMOylation restrains DNA polymerase η interactions with DNA damage sites.

Claire Guérillon, Stine Smedegaard, Ivo A Hendriks, Michael L Nielsen, Niels Mailand

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
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  3. SUMO and the DNA damage response.Biochemical Society transactions · 2024
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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

5 authors at 1 institution in 1 country.

Claire GuérillonUbiquitin Signaling Group, Protein Signaling Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen, Denmark.ORCID 0000-0002-1982-6596
Stine SmedegaardUbiquitin Signaling Group, Protein Signaling Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen, Denmark.
Ivo A HendriksProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen, Denmark.ORCID 0000-0002-1439-3701
Michael L NielsenProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen, Denmark.ORCID 0000-0002-0067-9039
Niels MailandUbiquitin Signaling Group, Protein Signaling Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, Copenhagen, Denmark niels.mailand@cpr.ku.dk.ORCID 0000-0002-6623-709X
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Translesion DNA synthesis (TLS) mediated by low-fidelity DNA polymerases is an essential cellular mechanism for bypassing DNA lesions that obstruct DNA replication progression. However, the access of TLS polymerases to the replication machinery must be kept tightly in check to avoid excessive mutagenesis. Recruitment of DNA polymerase η (Pol η) and other Y-family TLS polymerases to damaged DNA relies on proliferating cell nuclear antigen (PCNA) monoubiquitylation and is regulated at several levels. Using a microscopy-based RNAi screen, here we identified an important role of the SUMO modification pathway in limiting Pol η interactions with DNA damage sites in human cells. We found that Pol η undergoes DNA damage- and protein inhibitor of activated STAT 1 (PIAS1)-dependent polySUMOylation upon its association with monoubiquitylated PCNA, rendering it susceptible to extraction from DNA damage sites by SUMO-targeted ubiquitin ligase (STUbL) activity. Using proteomic profiling, we demonstrate that Pol η is targeted for multisite SUMOylation, and that collectively these SUMO modifications are essential for PIAS1- and STUbL-mediated displacement of Pol η from DNA damage sites. These findings suggest that a SUMO-driven feedback inhibition mechanism is an intrinsic feature of TLS-mediated lesion bypass functioning to curtail the interaction of Pol η with PCNA at damaged DNA to prevent harmful mutagenesis.

Indexed as

DNA DamageAmino Acid MotifsCatalytic DomainCell Line, TumorDNA-Directed DNA PolymeraseDNA RepairHumansNuclear ProteinsPeptidesProliferating Cell Nuclear AntigenProtein Inhibitors of Activated STATProteomicsRNA InterferenceRNA, Small InterferingSmall Ubiquitin-Related Modifier ProteinsSumoylationDNA-Directed DNA PolymeraseNuclear ProteinsPeptidesPIAS1 protein, humanProliferating Cell Nuclear AntigenProtein Inhibitors of Activated STATRad30 proteinRNA, Small InterferingRNF111 protein, humanSmall Ubiquitin-Related Modifier ProteinsUbiquitin-Protein LigasesY-Family DNA PolymerasesDNA damageDNA damage responseDNA polymerasepost-translational modification (PTM)proliferating cell nuclear antigen (PCNA)sumoylationtranslesion DNA synthesis (TLS)

Identifiers

PMID32350109
PMCPMC7307195
OpenAlexW3022400785

What OpenQuestion holds

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LicenceCC BY
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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.