Ontology highlight
ABSTRACT:
SUBMITTER: Wu Q
PROVIDER: S-EPMC4747905 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Wu Qian Q Paul Atanu A Su Dan D Mehmood Shahid S Foo Tzeh Keong TK Ochi Takashi T Bunting Emma L EL Xia Bing B Robinson Carol V CV Wang Bin B Blundell Tom L TL
Molecular cell 20160114 3
BRCA1 accumulation at DNA damage sites is an important step for its function in the DNA damage response and in DNA repair. BRCA1-BRCT domains bind to proteins containing the phosphorylated serine-proline-x-phenylalanine (pSPxF) motif including Abraxas, Bach1/FancJ, and CtIP. In this study, we demonstrate that ionizing radiation (IR)-induces ATM-dependent phosphorylation of serine 404 (S404) next to the pSPxF motif. Crystal structures of BRCT/Abraxas show that phosphorylation of S404 is important ...[more]