Claspin is phosphorylated in the Chk1-binding domain by a kinase distinct from Chk1.

@article{Bennett2008ClaspinIP,
  title={Claspin is phosphorylated in the Chk1-binding domain by a kinase distinct from Chk1.},
  author={Lara N Bennett and Conor Larkin and David A F Gillespie and Paul R. Clarke},
  journal={Biochemical and biophysical research communications},
  year={2008},
  volume={369 3},
  pages={
          973-6
        }
}
Chk1 protein kinase plays a critical role in checkpoints that restrict progression through the cell cycle if DNA replication has not been completed or DNA damage has been sustained. ATR-dependent activation of Chk1 is mediated by Claspin. Phosphorylation of Claspin at two sites (Thr916 and Ser945 in humans) in response to DNA replication arrest or DNA damage recruits Chk1 to Claspin. Chk1 is subsequently phosphorylated by ATR and fully activated to control cell cycle progression. We show that… CONTINUE READING