Sobhian, B.Shao, G.Lilli, D. R.Culhane, AedinMoreau, LisaXia, B.Livingston, DavidGreenberg, R. A.2016-10-192007Sobhian, B., G. Shao, D. R. Lilli, A. C. Culhane, L. A. Moreau, B. Xia, D. M. Livingston, and R. A. Greenberg. 2007. “RAP80 Targets BRCA1 to Specific Ubiquitin Structures at DNA Damage Sites.” Science 316 (5828) (May 25): 1198–1202. doi:10.1126/science.1139516. http://dx.doi.org/10.1126/science.1139516.0036-8075http://nrs.harvard.edu/urn-3:HUL.InstRepos:29048877Mutations 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 lysine6 - and lysine63-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.en-USJournal Article2016-10-1910.1126/science.1139516