Evidence map›Paper›PMID 37507011›Full record

ArticleThe Journal of biological chemistry2023

PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation.

Archimede Torretta, Constantinos Chatzicharalampous, Carmen Ebenwaldner, Herwig Schüler

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.1field-weighted citation impact, top 3% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Archimede TorrettaDepartment of Chemistry, Center for Molecular Protein Science (CMPS), Lund University, Lund, Sweden.
Constantinos ChatzicharalampousDepartment of Chemistry, Center for Molecular Protein Science (CMPS), Lund University, Lund, Sweden.
Carmen EbenwaldnerDepartment of Chemistry, Center for Molecular Protein Science (CMPS), Lund University, Lund, Sweden.
Herwig SchülerDepartment of Chemistry, Center for Molecular Protein Science (CMPS), Lund University, Lund, Sweden. Electronic address: herwig.schuler@biochemistry.lu.se.
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PARP14/BAL2 is a large multidomain enzyme involved in signaling pathways with relevance to cancer, inflammation, and infection. Inhibition of its mono-ADP-ribosylating PARP homology domain and its three ADP-ribosyl binding macro domains has been regarded as a potential means of therapeutic intervention. Macrodomains-2 and -3 are known to stably bind to ADP-ribosylated target proteins, but the function of macrodomain-1 has remained somewhat elusive. Here, we used biochemical assays of ADP-ribosylation levels to characterize PARP14 macrodomain-1 and the homologous macrodomain-1 of PARP9. Our results show that both macrodomains display an ADP-ribosyl glycohydrolase activity that is not directed toward specific protein side chains. PARP14 macrodomain-1 is unable to degrade poly(ADP-ribose), the enzymatic product of PARP1. The F926A mutation of PARP14 and the F244A mutation of PARP9 strongly reduced ADP-ribosyl glycohydrolase activity of the respective macrodomains, suggesting mechanistic homology to the Mac1 domain of the SARS-CoV-2 Nsp3 protein. This study adds two new enzymes to the previously known six human ADP-ribosyl glycohydrolases. Our results have key implications for how PARP14 and PARP9 will be studied and how their functions will be understood.

Indexed as

ADP-RibosylationPoly(ADP-ribose) PolymerasesProtein DomainsAdenosine Diphosphate RiboseGlycoside HydrolasesHumansNeoplasm ProteinsPoly Adenosine Diphosphate RiboseAdenosine Diphosphate RiboseGlycoside HydrolasesNeoplasm ProteinsPARP14 protein, humanPARP9 protein, humanPoly Adenosine Diphosphate RibosePoly(ADP-ribose) PolymerasesADP-ribosylationADP-ribosyltransferasehydrolasemacrodomainpoly(ADP-ribose) polymerase (PARP)posttranslational modification (PTM)protein domainsignaling

Identifiers

PMID37507011
PMCPMC10470015
OpenAlexW4385262438

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.