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Functions of BRCA1 and BRCA2 in the biological response to DNA damage

University of Cambridge, CRC Department of Oncology and The Medical Research Council Cancer Cell Unit, Hutchison/MRC Research Centre, Hills Road, Cambridge CB2 2XZ, UK

View larger version (8K): [in a new window]   Fig. 1. Features of the BRCA proteins. The N-terminal RING domain, nuclear localisation signal (NLS) and C-terminal BRCT domains of BRCA1 are shown, as are the eight BRC repeat motifs in BRCA2. Modified from Venkitaraman with the permission of Elsevier Science Ltd (Venkitaraman, 2001).

View larger version (23K): [in a new window]   Fig. 2. A model for the role of BRCA2 in DSB repair based on Davies et al. (Davies et al., 2001). As discussed in the text, an ‘inactive’ complex between BRCA2 and RAD51 in the nucleus undergoes transition to a form in which RAD51 is ‘active’ in forming nucleoprotein filaments at the sites of DNA damage. The transition may be induced after phosphorylation by kinases such as ATM or ATR activated by DNA damage. The precise role of BRCA1 in these events is unclear, but it is likely to have multiple functions in DNA damage responses. A single RAD51 molecule is shown bound to a single BRCA2 molecule for simplicity. Modified from Venkitaraman, with permission from Elsevier Science (Venkitaraman, 2001).

View larger version (43K): [in a new window]   Fig. 3. Protein partners of BRCA1 in DNA damage responses. There is accumulating evidence that BRCA1 performs multiple functions in the cellular response to DNA damage through its interactions with different protein partners. The list of BRCA1-interacting proteins indicated here is not exhaustive but illustrates points made in the text.

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