RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites
Copyright policy )RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites
Mutations affecting the BRCT domains of the breast cancer–associated tumor suppressor BRCA1 disrupt the recruitment of this protein to DNA double-strand breaks (DSBs). The molecular structures at DSBs recognized by BRCA1 are presently unknown. We report the interaction of the BRCA1 BRCT domain with RAP80, a ubiquitin-binding protein. RAP80 targets a complex containing the BRCA1-BARD1 (BRCA1-associated ring domain protein 1) E3 ligase and the deubiquitinating enzyme (DUB) BRCC36 to MDC1-γH2AX–dependent lysine 6 - and lysine 63 -linked ubiquitin polymers at DSBs. These events are required for cell cycle checkpoint and repair responses to ionizing radiation, implicating ubiquitin chain recognition and turnover in the BRCA1-mediated repair of DSBs.
- Dana-Farber Cancer Institute United States
- Abramson Cancer Center United States
- Harvard University United States
- University of Pennsylvania United States
570, Binding Sites, DNA Repair, BRCA1 Protein, Ubiquitin, Tumor Suppressor Proteins, Molecular Sequence Data, Nuclear Proteins, DNA, Cell Line, Protein Structure, Tertiary, DNA-Binding Proteins, Mice, 616, Animals, Humans, Nucleic Acid Conformation, DNA Breaks, Double-Stranded, Histone Chaperones, Amino Acid Sequence, Carrier Proteins, HeLa Cells
570, Binding Sites, DNA Repair, BRCA1 Protein, Ubiquitin, Tumor Suppressor Proteins, Molecular Sequence Data, Nuclear Proteins, DNA, Cell Line, Protein Structure, Tertiary, DNA-Binding Proteins, Mice, 616, Animals, Humans, Nucleic Acid Conformation, DNA Breaks, Double-Stranded, Histone Chaperones, Amino Acid Sequence, Carrier Proteins, HeLa Cells
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