Is there more to BARD1 than BRCA1?

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Abstract
BRCA1-associated ring domain 1 (BARD1) is the main binding partner of BRCA1 and is essential for the tumour-suppressor functions of BRCA1. The BARD1–BRCA1 heterodimer has ubiquitin ligase activity that targets proteins involved in cell-cycle regulation and DNA repair for degradation. BARD1 has a BRCA1-independent function in mediating p53-dependent apoptosis. It binds to p53, facilitating its phosphorylation and stabilization. BARD1 is expressed in most proliferative tissues, including that of the breast, ovary and uterus. It is transcriptionally upregulated in response to DNA damage, hypoxia and hormone signalling. Its translation is activated by cell-cycle-dependent phosphorylation. BARD1 is mutated or truncated in breast, ovarian and uterine tumour samples. Depletion of BARD1 leads to early embryonic lethality in mice, and genomic instability in vitro and in vivo; phenotypes that are also observed for BRCA1 or BRCA2 deficiencies.