Evidence map›Paper›PMID 29180619›Full record

ArticleNature communications2017

The STUbL RNF4 regulates protein group SUMOylation by targeting the SUMO conjugation machinery.

Ramesh Kumar, Román González-Prieto, Zhenyu Xiao, Matty Verlaan-de Vries, Alfred C O Vertegaal

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

72 citing papers in PubMed, 114 citations in OpenAlex.

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  18. SUMO and the DNA damage response.Biochemical Society transactions · 2024
    Review
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12 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

5 authors at 1 institution in 2 countries.

Ramesh KumarDepartment of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.
Román González-PrietoDepartment of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.ORCID http://orcid.org/0000-0001-8997-2321
Zhenyu XiaoDepartment of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.
Matty Verlaan-de VriesDepartment of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands.
Alfred C O VertegaalDepartment of Molecular Cell Biology, Leiden University Medical Center, Albinusdreef 2, 2333, ZA, Leiden, The Netherlands. vertegaal@lumc.nl.ORCID http://orcid.org/0000-0002-7989-0493
Leiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SUMO-targeted ubiquitin ligases (STUbLs) mediate the ubiquitylation of SUMOylated proteins to modulate their functions. In search of direct targets for the STUbL RNF4, we have developed TULIP (targets for ubiquitin ligases identified by proteomics) to covalently trap targets for ubiquitin E3 ligases. TULIP methodology could be widely employed to delineate E3 substrate wiring. Here we report that the single SUMO E2 Ubc9 and the SUMO E3 ligases PIAS1, PIAS2, PIAS3, ZNF451, and NSMCE2 are direct RNF4 targets. We confirm PIAS1 as a key RNF4 substrate. Furthermore, we establish the ubiquitin E3 ligase BARD1, a tumor suppressor and partner of BRCA1, as an indirect RNF4 target, regulated by PIAS1. Interestingly, accumulation of BARD1 at local sites of DNA damage increases upon knockdown of RNF4. Combined, we provide an insight into the role of the STUbL RNF4 to balance the role of SUMO signaling by directly targeting Ubc9 and SUMO E3 ligases.

Indexed as

Cell Line, TumorDNA DamageDNA RepairDown-RegulationGene Knockdown TechniquesHumansMutagenesis, Site-DirectedNuclear ProteinsSignal TransductionSumoylationTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein LigasesNuclear ProteinsRNF4 protein, humanTranscription FactorsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Conjugating Enzyme UBC9Ubiquitin-Protein Ligases

Identifiers

PMID29180619
PMCPMC5703878
OpenAlexW2770420481

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.