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 [].
SUV2 (SENSITIVE TO UV 2) is a putative plant ATRIP homologue that is a component of the ATR-dependent cell checkpoint response []. The suv2 mutant is defective in cell-cycle arrest in response to DNA damage [].
