The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity.
Although the protein product of the BRCA1 tumor suppressor gene has been implicated in a surprisingly diverse array of biological processes, the molecular mechanism by which BRCA1 loss promotes tumor formation remains unclear. Nonetheless, a pivotal advance has been achieved by recent studies that establish BRCA1 and its partner polypeptide BARD1 as enzymatic mediators of protein ubiquitination. The potent ubiquitin E3 ligase activity of the BRCA1/BARD1 heterodimer may be responsible for many of the biological properties attributed to BRCA1, including its ability to suppress tumor formation in normal cells.
Baer
Richard
R
Department of Pathology and Institute of Cancer Genetics, College of Physicians & Surgeons, Columbia University, 1150 St. Nicholas Avenue, New York, New York 10032, USA. rb670@columbia.edu
Ludwig
Thomas
T
D000595:Amino Acid Sequence; D000818:Animals; D019313:BRCA1 Protein / Q000737:chemistry* / Q000378:metabolism*; D001943:Breast Neoplasms / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism*; D019281:Dimerization; D005260:Female; D016147:Genes, Tumor Suppressor; D006801:Humans; D008025:Ligases / Q000378:metabolism*; D008958:Models, Molecular; D009154:Mutation; D017434:Protein Structure, Tertiary; D025521:Tumor Suppressor Proteins; D025801:Ubiquitin / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases
D019313:BRCA1 Protein; D002352:Carrier Proteins; D025521:Tumor Suppressor Proteins; D025801:Ubiquitin; C102449:BARD1 protein, human; D044767:Ubiquitin-Protein Ligases; D008025:Ligases