Journal
SCIENCE
Volume 316, Issue 5828, Pages 1194-1198Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1139476
Keywords
-
Categories
Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NCI NIH HHS [1KO1, CA116275-01, T32 CA009216, T32CA09216, K01 CA116275] Funding Source: Medline
- PHS HHS [1U19A1067751] Funding Source: Medline
Ask authors/readers for more resources
The BRCT repeats of the breast and ovarian cancer predisposition protein BRCA1 are essential for tumor suppression. Phosphopeptide affinity proteomic analysis identified a protein, Abraxas, that directly binds the BRCA1 BRCT repeats through a phospho- Ser-X-X-Phe motif. Abraxas binds BRCA1 to the mutual exclusion of BACH1 (BRCA1-associated C-terminal helicase) and CtIP (CtBP-interacting protein), forming a third type of BRCA1 complex. Abraxas recruits the ubiquitin-interacting motif (UIM)-containing protein RAP80 to BRCA1. Both Abraxas and RAP80 were required for DNA damage resistance, G(2)- M checkpoint control, and DNA repair. RAP80 was required for optimal accumulation of BRCA1 on damaged DNA ( foci) in response to ionizing radiation, and the UIM domains alone were capable of foci formation. The RAP80-Abraxas complex may help recruit BRCA1 to DNA damage sites in part through recognition of ubiquitinated proteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available