Inhibition of Aurora-B kinase activity by poly(ADP-ribosyl)ation in response to DNA damage.

@article{Monaco2005InhibitionOA,
  title={Inhibition of Aurora-B kinase activity by poly(ADP-ribosyl)ation in response to DNA damage.},
  author={Lucia Monaco and Ullas Kolthur-Seetharam and Romain Loury and Josiane M{\'e}nissier-de Murcia and Gilbert de Murcia and Paolo Sassone-Corsi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 40},
  pages={14244-8}
}
The cell cycle-regulated Aurora-B kinase is a chromosomal passenger protein that is implicated in fundamental mitotic events, including chromosome alignment and segregation and spindle checkpoint function. Aurora-B phosphorylates serine 10 of histone H3, a function that has been associated with mitotic chromatin condensation. We find that activation of poly(ADP-ribose) polymerase (PARP) 1 by DNA damage results in a rapid block of H3 phosphorylation. PARP-1 is a NAD(+)-dependent enzyme that… CONTINUE READING

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