A novel non-canonical PIP-box mediates PARG interaction with PCNA

@inproceedings{Kaufmann2017ANN,
  title={A novel non-canonical PIP-box mediates PARG interaction with PCNA},
  author={Tanja Kaufmann and Irina Grishkovskaya and Anton A. Polyansky and Sebastian Kostrhon and Eva Kukolj and Karin M. Olek and Sebastien Herbert and Etienne Beltzung and Karl Mechtler and Thomas Peterbauer and Josef Gotzmann and Lijuan Zhang and Markus Hartl and Bojan Zagrovic and Kareem Elsayad and Kristina Djinovi{\'c}-Carugo and Dea Slade},
  booktitle={Nucleic acids research},
  year={2017}
}
Poly(ADP-ribose) glycohydrolase (PARG) regulates cellular poly(ADP-ribose) (PAR) levels by rapidly cleaving glycosidic bonds between ADP-ribose units. PARG interacts with proliferating cell nuclear antigen (PCNA) and is strongly recruited to DNA damage sites in a PAR- and PCNA-dependent fashion. Here we identified PARG acetylation site K409 that is essential for its interaction with PCNA, its localization within replication foci and its recruitment to DNA damage sites. We found K409 to be part… CONTINUE READING

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