Evidence map›Paper›PMID 25086041›Full record

ArticleThe Journal of biological chemistry2014

PARP12, an interferon-stimulated gene involved in the control of protein translation and inflammation.

Iain Welsby, David Hutin, Cyril Gueydan, Veronique Kruys, Anthony Rongvaux, Oberdan Leo

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

84 citing papers in PubMed, 127 citations in OpenAlex.

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  7. PARP12-mediated mono-ADP-ribosylation as a checkpoint for necroptosis and apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2025
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24 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

6 authors at 2 institutions in 2 countries.

Iain WelsbyLaboratoire d'Immunobiologie, Université Libre de Bruxelles, Gosselies, Belgium; Institute for Medical Immunology, Université Libre de Bruxelles, Gosselies, Belgium.
David HutinLaboratoire d'Immunobiologie, Université Libre de Bruxelles, Gosselies, Belgium.
Cyril GueydanLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, Gosselies, Belgium.
Veronique KruysLaboratoire de Biologie Moléculaire du Gène, Université Libre de Bruxelles, Gosselies, Belgium; Center for Microscopy and Molecular Imaging (CMMI), Gosselies 6041, Belgium, and.
Anthony RongvauxDepartment of Immunobiology, Yale University, New Haven, Connecticut 06520.
Oberdan LeoLaboratoire d'Immunobiologie, Université Libre de Bruxelles, Gosselies, Belgium; Institute for Medical Immunology, Université Libre de Bruxelles, Gosselies, Belgium,. Electronic address: oleo@ulb.ac.be.
Université Libre de Bruxelles · BEYale University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transcriptome analyses have recently identified PARP12, a member of a large family of ADP-ribosyl transferases, as an interferon-induced gene (ISG), whose function remains incompletely characterized. We demonstrate herein that PARP12 is a genuine ISG, whose expressed protein displays at least two distinct subcellular locations and related functions. Upon ectopic expression or exposure to oxidative stress, PARP12 is recruited to stress-granules (SGs), known sites of mRNA translational arrest. Accordingly, PARP12 was found to block mRNA translation, possibly upon association to the translational machinery. Both the N-terminal domain (containing an RNA-binding domain characterized by the presence of five CCCH-type Zn-fingers) and integrity of the catalytic domain are required for this suppressive function. In contrast, stimulation with LPS leads to the localization of PARP12 to p62/SQSTM1 (an adaptor protein involved in innate signaling and autophagy) containing structures, unrelated to SGs. Deletion of the N-terminal domain promotes the association of the protein to p62/SQSTM1, suggesting that the RNA-binding domain is responsible for the subcellular localization of PARP12. Association to p62/SQSTM1 was found to correlate with increased NF-κB signaling, suggesting a role for PARP12 in inflammation. Collectively, these observations suggest that PARP12 can alternate between two distinct subcellular compartments associated to two distinct cellular functions. The present work therefore identifies PARP12 as an ISG with a potential role in cellular defenses against viral infections.

Indexed as

Protein BiosynthesisAmino Acid SequenceAnimalsCytoplasmic GranulesEnzyme InductionHEK293 CellsHeLa CellsHumansInflammationInterferon-betaMiceMolecular Sequence DataNF-kappa BPoly(ADP-ribose) PolymerasesProtein TransportTranscriptional ActivationInterferon-betaNF-kappa BPARP12 protein, mousePoly(ADP-ribose) PolymerasesUbiquitinADP-ribosylationInterferonInterferon-stimulated Gene (ISG)NF-κB (NF-κB)Poly(ADP-ribose) Polymerase (PARP)Stress GranuleTranslation Regulation

Identifiers

PMID25086041
PMCPMC4176246
OpenAlexW2060519709

What OpenQuestion holds

Textmetadata
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.