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• W3170669380 abstract "Mammalian DNA base excision repair (BER) is accelerated by poly(ADP-ribose) polymerases (PARPs) and the scaffold protein XRCC1. PARPs are sensors that detect single-strand break intermediates, but the critical role of XRCC1 during BER is unknown. Here, we show that protein complexes containing DNA polymerase β and DNA ligase III that are assembled by XRCC1 prevent excessive engagement and activity of PARP1 during BER. As a result, PARP1 becomes trapped on BER intermediates in XRCC1-deficient cells in a manner similar to that induced by PARP inhibitors, including in patient fibroblasts from XRCC1-mutated disease. This excessive PARP1 engagement and trapping renders BER intermediates inaccessible to enzymes such as DNA polymerase β and impedes their repair. Consequently, PARP1 deletion rescues BER and resistance to base damage in XRCC1-/- cells. These data reveal excessive PARP1 engagement during BER as a threat to genome integrity and identify XRCC1 as an anti-trapper that prevents toxic PARP1 activity." @default.
• W3170669380 created "2021-06-22" @default.
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• W3170669380 date "2021-07-01" @default.
• W3170669380 modified "2023-10-15" @default.
• W3170669380 title "XRCC1 prevents toxic PARP1 trapping during DNA base excision repair" @default.
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• W3170669380 doi "https://doi.org/10.1016/j.molcel.2021.05.009" @default.
• W3170669380 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8294329" @default.
• W3170669380 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34102106" @default.
• W3170669380 hasPublicationYear "2021" @default.
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