Ontology highlight
ABSTRACT:
SUBMITTER: Parsons JL
PROVIDER: S-EPMC3526271 | biostudies-other | 2012 Dec
REPOSITORIES: biostudies-other
Parsons Jason L JL Khoronenkova Svetlana V SV Dianova Irina I II Ternette Nicola N Kessler Benedikt M BM Datta Pran K PK Dianov Grigory L GL
Nucleic acids research 20121005 22
We examined the mechanism regulating the cellular levels of PNKP, the major kinase/phosphatase involved in the repair of oxidative DNA damage, and find that it is controlled by ATM phosphorylation and ubiquitylation-dependent proteasomal degradation. We discovered that ATM-dependent phosphorylation of PNKP at serines 114 and 126 in response to oxidative DNA damage inhibits ubiquitylation-dependent proteasomal degradation of PNKP, and consequently increases PNKP stability that is required for DNA ...[more]