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-gammaH2AX-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.
Mesh Terms:
Amino Acid Sequence, Animals, BRCA1 Protein, Binding Sites, Carrier Proteins, Cell Line, DNA, DNA Breaks, Double-Stranded, DNA Repair, Hela Cells, Humans, Mice, Molecular Sequence Data, Nuclear Proteins, Nucleic Acid Conformation, Protein Structure, Tertiary, Tumor Suppressor Proteins, Ubiquitin, Ubiquitin-Protein Ligases
Science
Date: May. 25, 2007
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