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- W1979846193 abstract "Germ-line mutations of the BRCA1 gene predispose women to early-onset breast and ovarian cancer by compromising the gene’s presumptive function as a tumor suppressor. Although the biochemical properties of BRCA1 polypeptides are not understood, their expression pattern and subcellular localization suggest a role in cell-cycle regulation. When resting cells are induced to proliferate, the steady-state levels of BRCA1 increase in late G 1 and reach a maximum during S phase. Moreover, in S phase cells, BRCA1 polypeptides are hyperphosphorylated and accumulate into discrete subnuclear foci termed “BRCA1 nuclear dots.” BRCA1 associates in vivo with a structurally related protein termed BARD1. Here we show that the steady-state levels of BARD1, unlike those of BRCA1, remain relatively constant during cell cycle progression. However, immunostaining revealed that BARD1 resides within BRCA1 nuclear dots during S phase of the cell cycle, but not during the G 1 phase. Nevertheless, BARD1 polypeptides are found exclusively in the nuclear fractions of both G 1 - and S-phase cells. Therefore, progression to S phase is accompanied by the aggregation of nuclear BARD1 polypeptides into BRCA1 nuclear dots. This cell cycle-dependent colocalization of BARD1 and BRCA1 indicates a role for BARD1 in BRCA1-mediated tumor suppression." @default.
- W1979846193 created "2016-06-24" @default.
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- W1979846193 date "1997-10-28" @default.
- W1979846193 modified "2023-10-18" @default.
- W1979846193 title "Cell cycle-dependent colocalization of BARD1 and BRCA1 proteins in discrete nuclear domains" @default.
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- W1979846193 doi "https://doi.org/10.1073/pnas.94.22.12075" @default.
- W1979846193 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/23707" @default.
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