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- W2024131694 abstract "The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain–containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This specific interaction between BRCA1 and phosphorylated BACH1 is cell cycle regulated and is required for DNA damage–induced checkpoint control during the transition from G 2 to M phase of the cell cycle. Further, we show that two other BRCT domains interact with their respective physiological partners in a phosphorylation-dependent manner. Thirteen additional BRCT domains also preferentially bind phospho-peptides rather than nonphosphorylated control peptides. These data imply that the BRCT domain is a phospho-protein binding domain involved in cell cycle control." @default.
- W2024131694 created "2016-06-24" @default.
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- W2024131694 date "2003-10-24" @default.
- W2024131694 modified "2023-10-10" @default.
- W2024131694 title "The BRCT Domain Is a Phospho-Protein Binding Domain" @default.
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- W2024131694 doi "https://doi.org/10.1126/science.1088753" @default.
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