ArticleEnvironmental and molecular mutagenesis2011
XRCC1 coordinates disparate responses and multiprotein repair complexes depending on the nature and context of the DNA damage.
Article in Environmental and molecular mutagenesis, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 67 citations in OpenAlex.
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- How Do ROS Induce NETosis? Oxidative DNA Damage, DNA Repair, and Chromatin Decondensation.Biomolecules · 2024Review
- DNA Repair Protein XRCC1 Stimulates Activity of DNA Polymerase λ under Conditions of Microphase Separation.International journal of molecular sciences · 2024Article
- Replication Protein A Enhances Kinetics of Uracil DNA Glycosylase on ssDNA and Across DNA Junctions: Explored with a DNA Repair Complex Produced with SpyCatcher/SpyTag Ligation.Chembiochem : a European journal of chemical biology · 2023Article
- 8-Oxoguanine: from oxidative damage to epigenetic and epitranscriptional modification.Experimental & molecular medicine · 2022Review
- ROS induces NETosis by oxidizing DNA and initiating DNA repair.Cell death discovery · 2021Article
- Article
- Eukaryotic Base Excision Repair: New Approaches Shine Light on Mechanism.Annual review of biochemistry · 2019Review
- Identification of an XRCC1 DNA binding activity essential for retention at sites of DNA damage.Scientific reports · 2019Article
- Domain analysis of PNKP-XRCC1 interactions: Influence of genetic variants of XRCC1.The Journal of biological chemistry · 2019Article
- Anti-Cancer Potential of Homemade Fresh Garlic Extract Is Related to Increased Endoplasmic Reticulum Stress.Nutrients · 2018Article
- XRCC1-mediated repair of strand breaks independent of PNKP binding.DNA repair · 2017Article
- Kinetics of poly(ADP-ribosyl)ation, but not PARP1 itself, determines the cell fate in response to DNA damage in vitro and in vivo.Nucleic acids research · 2017Article
- Application of Laser Micro-irradiation for Examination of Single and Double Strand Break Repair in Mammalian Cells.Journal of visualized experiments : JoVE · 2017Article
- Principal Aspects Regarding the Maintenance of Mammalian Mitochondrial Genome Integrity.International journal of molecular sciences · 2017Review
- Monitoring of the spatial and temporal dynamics of BER/SSBR pathway proteins, including MYH, UNG2, MPG, NTH1 and NEIL1-3, during DNA replication.Nucleic acids research · 2017Article
- Poly(ADP-ribose) polymerase 1 escorts XPC to UV-induced DNA lesions during nucleotide excision repair.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- p38 MAPK signaling and phosphorylations in the BRCT1 domain regulate XRCC1 recruitment to sites of DNA damage.Scientific reports · 2017Article
- Coordination of DNA single strand break repair.Free radical biology & medicine · 2017Review
- Protecting DNA from errors and damage: an overview of DNA repair mechanisms in plants compared to mammals.Cellular and molecular life sciences : CMLS · 2017Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
XRCC1 is a scaffold protein capable of interacting with several DNA repair proteins. Here we provide evidence for the presence of XRCC1 in different complexes of sizes from 200 to 1500 kDa, and we show that immunoprecipitates using XRCC1 as bait are capable of complete repair of AP sites via both short patch (SP) and long patch (LP) base excision repair (BER). We show that POLβ and PNK colocalize with XRCC1 in replication foci and that POLβ and PNK, but not PCNA, colocalize with constitutively present XRCC1-foci as well as damage-induced foci when low doses of a DNA-damaging agent are applied. We demonstrate that the laser dose used for introducing DNA damage determines the repertoire of DNA repair proteins recruited. Furthermore, we demonstrate that recruitment of POLβ and PNK to regions irradiated with low laser dose requires XRCC1 and that inhibition of PARylation by PARP-inhibitors only slightly reduces the recruitment of XRCC1, PNK, or POLβ to sites of DNA damage. Recruitment of PCNA and FEN-1 requires higher doses of irradiation and is enhanced by XRCC1, as well as by accumulation of PARP-1 at the site of DNA damage. These data improve our understanding of recruitment of BER proteins to sites of DNA damage and provide evidence for a role of XRCC1 in the organization of BER into multiprotein complexes of different sizes.
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