Nuclear-cytoplasmic shuttling of BARD1 contributes to its proapoptotic activity and is regulated by dimerization with BRCA1 (Q28188597)

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Wendy W Y Au

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Megan Fabbro

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Beric R Henderson

The BRCA1/BARD1 heterodimer, a tumor suppressor complex with ubiquitin E3 ligase activity

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language of work or name

English

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publication date

11 March 2004

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published in

Oncogene

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volume

23

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issue

10

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page(s)

1809-20

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cites work

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Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay

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BRCA1 RING domain cancer-predisposing mutations. Structural consequences and effects on protein-protein interactions

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Structure of a BRCA1-BARD1 heterodimeric RING-RING complex

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Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase

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Redistribution of BRCA1 among four different protein complexes following replication blockage

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BARD1 induces BRCA1 intranuclear foci formation by increasing RING-dependent BRCA1 nuclear import and inhibiting BRCA1 nuclear export

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The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation

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Identification of BARD1 as mediator between proapoptotic stress and p53-dependent apoptosis

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In vitro repression of Brca1-associated RING domain gene, Bard1, induces phenotypic changes in mammary epithelial cells

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Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains

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Functional communication between endogenous BRCA1 and its partner, BARD1, during Xenopus laevis development

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Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50

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The BARD1-CstF-50 interaction links mRNA 3' end formation to DNA damage and tumor suppression

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RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

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Loss of Bard1, the heterodimeric partner of the Brca1 tumor suppressor, results in early embryonic lethality and chromosomal instability

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A strong candidate for the breast and ovarian cancer susceptibility gene BRCA1

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Identification of a functional nuclear export sequence in BRCA1.

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Cancer-predisposing mutations within the RING domain of BRCA1: loss of ubiquitin protein ligase activity and protection from radiation hypersensitivity

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Dynamic changes of BRCA1 subnuclear location and phosphorylation state are initiated by DNA damage

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A DNA vector-based RNAi technology to suppress gene expression in mammalian cells

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Mutations in the BRCA1-associated RING domain (BARD1) gene in primary breast, ovarian and uterine cancers

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Identification of a RING protein that can interact in vivo with the BRCA1 gene product

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Genetic interactions between tumor suppressors Brca1 and p53 in apoptosis, cell cycle and tumorigenesis.

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