USP45 deubiquitylase controls ERCC1–XPF endonuclease-mediated DNA damage responses

@inproceedings{PrezOliva2015USP45DC,
  title={USP45 deubiquitylase controls ERCC1–XPF endonuclease-mediated DNA damage responses},
  author={Ana B P{\'e}rez-Oliva and Christophe Lachaud and Piotr Szyniarowski and Iv{\'a}n Mu{\~n}oz and Thomas Macartney and Ian Hickson and John Rouse and Dario R Alessi},
  booktitle={The EMBO journal},
  year={2015}
}
Reversible protein ubiquitylation plays important roles in various processes including DNA repair. Here, we identify the deubiquitylase USP45 as a critical DNA repair regulator. USP45 associates with ERCC1, a subunit of the DNA repair endonuclease XPF-ERCC1, via a short acidic motif outside of the USP45 catalytic domain. Wild-type USP45, but not a USP45 mutant defective in ERCC1 binding, efficiently deubiquitylates ERCC1 in vitro, and the levels of ubiquitylated ERCC1 are markedly enhanced in… CONTINUE READING
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