ArticleScientific reports2018
Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 41 citations in OpenAlex.
- Reversible RNA ADP-ribosylation on uracil bases.Nucleic acids research · 2026Article
- Novel extracellular vesicle release pathway facilitated by toxic superoxide dismutase 1 oligomers.Neurobiology of disease · 2026Article
- TARG1 affects EGFR signaling through the regulation of RNA metabolism.Scientific reports · 2025Article
- Effect of Chronic Stress on Whole Blood Transcriptome: A Meta-Analysis of Publicly Available Datasets from Rodent Models.bioRxiv : the preprint server for biology · 2025Article
- Family-wide analysis of human macrodomains reveals novel activities and identifies PARG as most efficient ADPr-RNA hydrolase.Communications biology · 2025Article
- RACK1 MARylation regulates translation and stress granules in ovarian cancer cells.The Journal of cell biology · 2025Article
- ADP-ribose hydrolases: biological functions and potential therapeutic targets.Expert reviews in molecular medicine · 2024Review
- Monitoring nucleolar-nucleoplasmic protein shuttling in living cells by high-content microscopy and automated image analysis.Nucleic acids research · 2024Article
- Specific and shared biological functions of PARP2 - is PARP2 really a lil' brother of PARP1?Expert reviews in molecular medicine · 2024Review
- IFN-Induced PARPs-Sensors of Foreign Nucleic Acids?Pathogens (Basel, Switzerland) · 2023Review
- Mono-ADP-ribosylation by PARP10 inhibits Chikungunya virus nsP2 proteolytic activity and viral replication.Cellular and molecular life sciences : CMLS · 2023Article
- urPTMdb/TeaProt: Upstream and Downstream Proteomics Analysis.Journal of proteome research · 2023Article
- Protein and RNA ADP-ribosylation detection is influenced by sample preparation and reagents used.Life science alliance · 2023Article
- The expanding universe of PARP1-mediated molecular and therapeutic mechanisms.Molecular cell · 2022Review
- Nucleolar translocation of human DNA topoisomerase II by ATP depletion and its disruption by the RNA polymerase I inhibitor BMH-21.Scientific reports · 2021Article
- TARG1 protects against toxic DNA ADP-ribosylation.Nucleic acids research · 2021Article
- MyoD induces ARTD1 and nucleoplasmic poly-ADP-ribosylation during fibroblast to myoblast transdifferentiation.iScience · 2021Article
- PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.International journal of molecular sciences · 2021Review
- ADP-ribosylation of RNA and DNA: from in vitro characterization to in vivo function.Nucleic acids research · 2021Review
- The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021Review
Corrections and comments
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Authors and funding
16 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Macrodomains are conserved protein folds associated with ADP-ribose binding and turnover. ADP-ribosylation is a posttranslational modification catalyzed primarily by ARTD (aka PARP) enzymes in cells. ARTDs transfer either single or multiple ADP-ribose units to substrates, resulting in mono- or poly-ADP-ribosylation. TARG1/C6orf130 is a macrodomain protein that hydrolyzes mono-ADP-ribosylation and interacts with poly-ADP-ribose chains. Interactome analyses revealed that TARG1 binds strongly to ribosomes and proteins associated with rRNA processing and ribosomal assembly factors. TARG1 localized to transcriptionally active nucleoli, which occurred independently of ADP-ribose binding. TARG1 shuttled continuously between nucleoli and nucleoplasm. In response to DNA damage, which activates ARTD1/2 (PARP1/2) and promotes synthesis of poly-ADP-ribose chains, TARG1 re-localized to the nucleoplasm. This was dependent on the ability of TARG1 to bind to poly-ADP-ribose. These findings are consistent with the observed ability of TARG1 to competitively interact with RNA and PAR chains. We propose a nucleolar role of TARG1 in ribosome assembly or quality control that is stalled when TARG1 is re-located to sites of DNA damage.
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