BRCA1isabreastandovariancancertumorsuppressorproteinthatassociateswithBARD1toformaRING/RINGheterodimer.TheBRCA1/BARD1RINGcomplexfunctionsasanubiquitin(Ub)ligasewithactivitysubstantiallygreaterthanindividualBRCA1orBARD1subunits.TheBRCA1tumorsuppressorformsaheterodimerwiththeBARD1protein,andtheresultingcomplexfunctionsasanE3ubiquitinligasethatcatalyzesthesynthesisofpolyubiquitinchains.UbcH5candUbcH7alsointeractwiththeBRCA1/BARD1complexwithsimilaraffinity(notshownonthisfigure).Althoughtheinvivosubstrate(s)isnotyetknown,BRCA1hasbeenobservedtoundergoautoubiquitinationandiscapableofmonoubiquitinatinghistones2Aand2AXinvitro

Contributor:KosiGramatikoff,PhD

REFERENCES:EllenEetal.LossofBard1,theHeterodimericPartneroftheBrca1TumorSuppressor,ResultsinEarlyEmbryonicLethalityandChromosomalInstABIlityMol.Cell.Biol.,Jul2003;23:5056-5063.F.Wu-Baeretal.TheBRCA1/BARD1HeterodimerAssemblesPolyubiquitinChainsthroughanUnconventionalLinkageInvolvingLysineResidueK6ofUbiquitinJ.Biol.Chem.,September12,2003;278(37):34743-34746.P.-Y.Wuetal.Aconservedcatalyticresidueintheubiquitin-conjugatingenzymefamilyEMBOJ.,October1,2003;22(19):5241-5250.PeterS.Brzovicetal.BindingandrecognitionintheassemblyofanactiveBRCA1/BARD1ubiquitin-ligasecomplexPNAS,May2003;100:5646-5651UlricaK.Westermarketal.BARD1ParticipateswithBRCA1inHomology-DirectedRepairofChromosomeBreaksMol.Cell.Biol.,Nov2003;23:7926-7936.

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