Evidence map›Paper›PMID 38000390›Full record

ArticleNucleic acids research2024

DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids.

Kang Zhu, Marcin J Suskiewicz, Chatrin Chatrin, Øyvind Strømland, Bryan W Dorsey, Vincent Aucagne, Dragana Ahel, Ivan Ahel

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

33 citing papers in PubMed, 50 citations in OpenAlex.

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  19. The rise of ADP-ribose-ubiquitin.Nature structural & molecular biology · 2025
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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

8 authors at 3 institutions in 4 countries.

Kang ZhuSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Marcin J SuskiewiczCentre de Biophysique Moléculaire, CNRS UPR 4301, Orléans, France.ORCID 0000-0002-3279-6571
Chatrin ChatrinSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Øyvind StrømlandSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Bryan W DorseyRibon Therapeutics, 35 Cambridgepark Dr., Suite 300, Cambridge MA 02140, USA.
Vincent AucagneCentre de Biophysique Moléculaire, CNRS UPR 4301, Orléans, France.
Dragana AhelSir William Dunn School of Pathology, University of Oxford, Oxford, UK.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, UK.ORCID 0000-0002-9446-3756
University of Oxford · GBCentre National de la Recherche Scientifique · FRRibon Therapeutics (United States) · US

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Cancer Research UK 22284Wellcome Trust 210634Wellcome Trust 210634/Z/18/Z
6 · The paper itself

Abstract

Although ubiquitylation had traditionally been considered limited to proteins, the discovery of non-proteinaceous substrates (e.g. lipopolysaccharides and adenosine diphosphate ribose (ADPr)) challenged this perspective. Our recent study showed that DTX2 E3 ligase efficiently ubiquitylates ADPr. Here, we show that the ADPr ubiquitylation activity is also present in another DELTEX family member, DTX3L, analysed both as an isolated catalytic fragment and the full-length PARP9:DTX3L complex, suggesting that it is a general feature of the DELTEX family. Since structural predictions show that DTX3L possesses single-stranded nucleic acids binding ability and given the fact that nucleic acids have recently emerged as substrates for ADP-ribosylation, we asked whether DELTEX E3s might catalyse ubiquitylation of an ADPr moiety linked to nucleic acids. Indeed, we show that DTX3L and DTX2 are capable of ubiquitylating ADP-ribosylated DNA and RNA synthesized by PARPs, including PARP14. Furthermore, we demonstrate that the Ub-ADPr-nucleic acids conjugate can be reversed by two groups of hydrolases, which remove either the whole adduct (e.g. SARS-CoV-2 Mac1 or PARP14 macrodomain 1) or just the Ub (e.g. SARS-CoV-2 PLpro). Overall, this study reveals ADPr ubiquitylation as a general function of the DELTEX family E3s and presents the evidence of reversible ubiquitylation of ADP-ribosylated nucleic acids.

Indexed as

ADP-RibosylationNucleic AcidsUbiquitin-Protein LigasesAdenosine Diphosphate RiboseHumansOkadaic AcidProteinsAdenosine Diphosphate Ribosedinophysistoxin 2DTX3 protein, humanNucleic AcidsOkadaic AcidProteinsUbiquitin-Protein Ligases

Identifiers

PMID38000390
PMCPMC10810221
OpenAlexW4389004873

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Registered trials

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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.