ArticleDNA repair2015
Poly(ADP-ribose)-binding promotes Exo1 damage recruitment and suppresses its nuclease activities.
Article in DNA repair, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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.
Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- Meta-analysis of DNA double-strand break response kinetics.Nucleic acids research · 2017Pooled it
- The Role of Arp2/3 in End-Resection During DNA Double-Strand Break Repair.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Decoding replication stress responses through post-translational modifications.Nature chemical biology · 2025Review
- Rad27/FEN1 prevents accumulation of Okazaki fragments and ribosomal DNA copy number changes.FEBS letters · 2025Article
- Poly(ADP) ribose polymerase promotes DNA polymerase theta-mediated end joining by activation of end resection.Nature communications · 2022Article
- Identification of DNA Damage Repair-Associated Prognostic Biomarkers for Prostate Cancer Using Transcriptomic Data Analysis.International journal of molecular sciences · 2021Article
- HPF1-dependent PARP activation promotes LIG3-XRCC1-mediated backup pathway of Okazaki fragment ligation.Nucleic acids research · 2021Article
- MIF is a 3' flap nuclease that facilitates DNA replication and promotes tumor growth.Nature communications · 2021Article
- BKM120 sensitizes BRCA-proficient triple negative breast cancer cells to olaparib through regulating FOXM1 and Exo1 expression.Scientific reports · 2021Article
- Functional Roles of Poly(ADP-Ribose) in Stress Granule Formation and Dynamics.Frontiers in cell and developmental biology · 2021Review
- AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair.The Journal of biological chemistry · 2020Article
- PARP-1 and its associated nucleases in DNA damage response.DNA repair · 2019Review
- Human Exonuclease 1 (EXO1) Regulatory Functions in DNA Replication with Putative Roles in Cancer.International journal of molecular sciences · 2018Review
- Review
- Simultaneous dual-channel imaging to quantify interdependent protein recruitment to laser-induced DNA damage sites.Nucleus (Austin, Tex.) · 2018Article
- Dna2 initiates resection at clean DNA double-strand breaks.Nucleic acids research · 2017Article
- Interplay of catalysis, fidelity, threading, and processivity in the exo- and endonucleolytic reactions of human exonuclease I.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Sharpening the ends for repair: mechanisms and regulation of DNA resection.Acta biochimica et biophysica Sinica · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Exonuclease 1 (Exo1) has important roles in DNA metabolic transactions that are essential for genome maintenance, telomere regulation and cancer suppression. However, the mechanisms for regulating Exo1 activity in these processes remain incompletely understood. Here, we report that Exo1 activity is regulated by a direct interaction with poly(ADP-ribose) (PAR), a prominent posttranslational modification at the sites of DNA damage. This PAR-binding activity promotes the early recruitment of Exo1 to sites of DNA damage, where it is retained through an interaction with PCNA, which interacts with the C-terminus of Exo1. The effects of both PAR and PCNA on Exo1 damage association are antagonized by the 14-3-3 adaptor proteins, which interact with the central domain of Exo1. Although PAR binding inhibits both the exonuclease activity and the 5' flap endonuclease activity of purified Exo1, the pharmacological blockade of PAR synthesis does not overtly affect DNA double-strand break end resection in a cell free Xenopus egg extract. Thus, the counteracting effects of PAR on Exo1 recruitment and enzymatic activity may enable appropriate resection of DNA ends while preventing unscheduled or improper processing of DNA breaks in cells.
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Registered trials
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.