The function of the ATR-ATRIP (ATR-interacting protein) protein kinase complex is crucial for the cellular response to replication stress and DNA damage. ATRIP is a regulatory partner of ATR. The binding of ATRIP to replication protein A-coated ssDNA at sites of DNA damage drives ATR activation and enables the ATR-ATRIP complex to stimulate phosphorylation of substrates, such as Rad17 or Chk1, and the initiation of checkpoint signalling []. ATRIP deacetylation by SIRT2 promotes ATR-ATRIP bindingto RPA-ssDNA [].
