{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Lin X"],"funding":["Herbert Irving Comprehensive Cancer Center (HICCC)","NCI NIH HHS","NIH","NIH HHS"],"pagination":["gkaf086"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11838041"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["53(4)"],"pubmed_abstract":["Poly-ADP-ribose polymerases 1 and 2 (PARP1 and 2) are critical sensors of DNA-strand breaks and targets for cancer therapy. Upon DNA damage, PARP1 and 2 synthesize poly-ADP-ribose (PAR) chains on themselves and other substrates, facilitating DNA single-strand break repair by recruiting PAR-binding DNA repair factors, including X-ray repair cross-complementing group 1 (XRCC1) and aprataxin and polynucleotide kinase phosphatase-like factor (APLF). While diverse DNA lesions activate PARP1, PARP2 is selectively activated by 5' phosphorylated nicks. They function independently and compensate for each other. Previous studies suggest that PARP1 and its PAR chains act upstream to recruit PARP2 to DNA damage sites. Here, we report that the scaffold protein XRCC1 mediates PARP1- and PAR-dependent re"],"journal":["Nucleic acids research"],"pubmed_title":["XRCC1 mediates PARP1- and PAR-dependent recruitment of PARP2 to DNA damage sites."],"pmcid":["PMC11838041"],"funding_grant_id":["R01 CA293675","CA271595","P30CA013696","P01 CA092584","P30 CA013696"],"pubmed_authors":["Lee BJ","Call N","Zha S","Bhandari SK","Huang X","Leung KSK","Tomkinson AE","Lin X","Wolfe KF"],"additional_accession":[]},"is_claimable":false,"name":"XRCC1 mediates PARP1- and PAR-dependent recruitment of PARP2 to DNA damage sites.","description":"Poly-ADP-ribose polymerases 1 and 2 (PARP1 and 2) are critical sensors of DNA-strand breaks and targets for cancer therapy. Upon DNA damage, PARP1 and 2 synthesize poly-ADP-ribose (PAR) chains on themselves and other substrates, facilitating DNA single-strand break repair by recruiting PAR-binding DNA repair factors, including X-ray repair cross-complementing group 1 (XRCC1) and aprataxin and polynucleotide kinase phosphatase-like factor (APLF). While diverse DNA lesions activate PARP1, PARP2 is selectively activated by 5' phosphorylated nicks. They function independently and compensate for each other. Previous studies suggest that PARP1 and its PAR chains act upstream to recruit PARP2 to DNA damage sites. Here, we report that the scaffold protein XRCC1 mediates PARP1- and PAR-dependent re","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Feb","modification":"2025-04-04T00:56:34.815Z","creation":"2025-04-04T00:56:34.815Z"},"accession":"S-EPMC11838041","cross_references":{"pubmed":["39970298"],"doi":["10.1093/nar/gkaf086"]}}