stability. DNA repair BRCA1-BARD1 appears to have an important function in the recruitment of RAD51 protein to DNA double-strand breaks which is a crucial early step in the homologous recombinational repair of these breaks. It is likely that BRCA1-BARD1 functions as part of a higher-order “homologous recombination mediator complex” along with two other tumor suppressor proteins BRCA2 and PALB2. Interactions BARD1 has been shown to interact with: AURKB, BCL3, BRCA1, BRCA2, BRCC3, BRE, CSTF1, CSTF2, EWSR1, FANCD2, H2AFX, NPM1, P53, RAD51, TACC1, and UBE2D1. Implication in Cancer Treatments If a cancer cell's capacity to repair DNA damage were incapacitated, cancer treatments would be more effective. Inhibiting cancer cells' BRCA1/BARD1 heterodimer from relocating to DNA damage sites would induce tumor cell death rather than repair. One inhibition possibility is the BARD1 BRCT key lysine residue (K619). Inhibiting this lysine residue's ability to bind poly(ADP-ribose) would prevent the BRCA1/BARD1 heterodimer from localizing to DNA damage sites and subsequently prevent DNA damage repair. This would make cancer therapies such as chemotherapy and radiation vastly more effective. References External links Further reading Proteins