| First Author | Rulten SL | Year | 2011 |
| Journal | Mol Cell | Volume | 41 |
| Issue | 1 | Pages | 33-45 |
| PubMed ID | 21211721 | Mgi Jnum | J:168260 |
| Mgi Id | MGI:4887518 | Doi | 10.1016/j.molcel.2010.12.006 |
| Citation | Rulten SL, et al. (2011) PARP-3 and APLF function together to accelerate nonhomologous end-joining. Mol Cell 41(1):33-45 |
| abstractText | PARP-3 is a member of the ADP-ribosyl transferase superfamily of unknown function. We show that PARP-3 is stimulated by DNA double-strand breaks (DSBs) in vitro and functions in the same pathway as the poly (ADP-ribose)-binding protein APLF to accelerate chromosomal DNA DSB repair. We implicate PARP-3 in the accumulation of APLF at DSBs and demonstrate that APLF promotes the retention of XRCC4/DNA ligase IV complex in chromatin, suggesting that PARP-3 and APLF accelerate DNA ligation during nonhomologous end-joining (NHEJ). Consistent with this, we show that class switch recombination in Aplf(-/-) B cells is biased toward microhomology-mediated end-joining, a pathway that operates in the absence of XRCC4/DNA ligase IV, and that the requirement for PARP-3 and APLF for NHEJ is circumvented by overexpression of XRCC4/DNA ligase IV. These data identify molecular roles for PARP-3 and APLF in chromosomal DNA double-strand break repair reactions. |
