1998
DOI: 10.1128/mcb.18.6.3563
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XRCC1 Is Specifically Associated with Poly(ADP-Ribose) Polymerase and Negatively Regulates Its Activity following DNA Damage

Abstract: Poly(ADP-ribose) polymerase (PARP; EC 2.4.2.30) is a zinc-finger DNA-binding protein that detects and signals DNA strand breaks generated directly or indirectly by genotoxic agents. In response to these breaks, the immediate poly(ADP-ribosyl)ation of nuclear proteins involved in chromatin architecture and DNA metabolism converts DNA damage into intracellular signals that can activate DNA repair programs or cell death options. To have greater insight into the physiological function of this enzyme, we have used … Show more

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Cited by 850 publications
(640 citation statements)
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References 57 publications
(70 reference statements)
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“…It is conceivable that the steps subsequent to topoisomerase I removal by this repair enzyme could involve some mechanism common to the BER pathway. Recently it has been proposed that BER is accomplished by a multiprotein complex consisting of PARP, XRCC1, DNA polymerase β and DNA ligase II (Caldecott et al, 1996;Mason et al, 1998). Interestingly, EM9 cells with defective XRCC1 are hypersensitive to camptothecin (Caldecott and Jeggo, 1991) but not etoposide (Jeggo et al, 1989).…”
Section: Discussionmentioning
confidence: 99%
“…It is conceivable that the steps subsequent to topoisomerase I removal by this repair enzyme could involve some mechanism common to the BER pathway. Recently it has been proposed that BER is accomplished by a multiprotein complex consisting of PARP, XRCC1, DNA polymerase β and DNA ligase II (Caldecott et al, 1996;Mason et al, 1998). Interestingly, EM9 cells with defective XRCC1 are hypersensitive to camptothecin (Caldecott and Jeggo, 1991) but not etoposide (Jeggo et al, 1989).…”
Section: Discussionmentioning
confidence: 99%
“…Soon thereafter, a stable complex of XRCC1 and LigIIIα was discovered [65] and by the late 1990s XRCC1 was established as a BER scaffold protein [66] in partnership with pol ß and PARP1 [16]. The list of cellular components that interact with XRCC1 has been expanded to include nicked DNA [67,68] and AP site containing DNA, both intermediates in the BER pathway [69].…”
Section: Scaffold Proteinsmentioning
confidence: 99%
“…One of the first proteins recruited is XRCC1, a protein closely associated with BER pathway coordination. PARP1 interacts with XRCC1 to form the protein scaffold upon which the repair complex is built [16]. Furthermore, PARP1 has been linked more directly to BER as it interacts both physically and functionally with pol ß [12,17] and LigIIIα [18], placing it as a member of the short-patch BER pathway (Table II).…”
Section: Introduction Of a Unifying Ber Modelmentioning
confidence: 99%
“…[20][21][22] Its physical interaction with the base excision repair protein, X-ray repair cross complementing 1 (XRCC1), confirms that PARP-1 is a member of a multiprotein complex involved in the DNA polymerase b, XRCC1 and DNA ligase 3 (Polb-XRCC1-Lig3) repair pathway. 23 This pathway repairs 50-80% of ssb in living cells. 24 An alternative pathway of ssb repair involves DNA polymerase d/e, proliferating cell nuclear antigen and DNA ligase1 (Pold/e-PCNA-Lig1 pathway).…”
Section: Introductionmentioning
confidence: 99%