Two distinct modes of ATR activation orchestrated by Rad17 and Nbs1.

@article{Shiotani2013TwoDM,
  title={Two distinct modes of ATR activation orchestrated by Rad17 and Nbs1.},
  author={Bunsyo Shiotani and Hai Dang Nguyen and Pelle H{\aa}kansson and Alexandre Mar{\'e}chal and Alice Ping Ping Tse and Hidetoshi Tahara and L. Q. Zou},
  journal={Cell reports},
  year={2013},
  volume={3 5},
  pages={1651-62}
}
The ATM- and Rad3-related (ATR) kinase is a master regulator of the DNA damage response, yet how ATR is activated toward different substrates is still poorly understood. Here, we show that ATR phosphorylates Chk1 and RPA32 through distinct mechanisms at replication-associated DNA double-stranded breaks (DSBs). In contrast to the rapid phosphorylation of Chk1, RPA32 is progressively phosphorylated by ATR at Ser33 during DSB resection prior to the phosphorylation of Ser4/Ser8 by DNA-PKcs… CONTINUE READING