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Studies describe how mutations affect BRCA1 function.
2004 JUN 3 - (NewsRx.com & NewsRx.net) -- Two new structural studies reveal how mutations within the C-terminal region of the BRCA1 protein affect the function of the BRCA1 gene, leading to breast cancer.
Among the 180,000 women who develop breast cancer each year, about 5% are due to inherited germline mutations in the breast cancer susceptibility gene product, BRCA1. BRCA1 plays a number of important roles in the cell including the response to DNA damage. Most of the inherited, early-onset breast cancers result from these mutations.
The C-terminal region of BRCA1 contains tandem repeats called BRCT domains that are generally thought to function as protein-protein interaction modules. Recent studies have shown that these repeats recognize phosphoserine or phosphothreonine (pSer or pThr) peptides, suggesting that some of the interactions of BRCA1 with other proteins may be regulated by protein phosphorylation.
Now, two groups have determined the structures of tandem BRCT repeats bound to phosphopeptides. The studies appear in the June 2004 issue of Nature Structural & Molecular Biology.
Michael Yaffe of the Massachusetts Institute of Technology and colleagues determined the crystal structure of this repeat domain bound to a phosphopeptide derived from Bach1, a known partner of BRCA1. The structure explains why tandem BRCT repeats, rather than single BRCT domains, are required for phosphopeptide ...
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...and TopBP1 together. The association between TopBP1 and Nbs1 involves the first pair of BRCT repeats in TopBP1. In addition, the two tandem BRCT repeats of Nbs1 are required for this binding. Functional studies with mutated forms of TopBP1...
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...terminus of the RhoGAP HsCyk-4 at the central spindle, creating a phospho-epitope recognized by the BRCA1 C-terminal (BRCT) repeats of Ect2. Failure to phosphorylate HsCyk-4 blocks Ect2 recruitment to the central spindle and the subsequent induction...
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...also known as MgcRacGAP) at the midzone. At serine 157, this modification creates a major docking site for the tandem BRCT repeats of the Rho GTP exchange factor Ect2. Cells expressing only a nonphosphorylatable form of HsCYK-4 failed to localize Ect2...
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...rearrangement of the hydrophobic core, and disruption of the native hydrogen bonding network at the interface between the two BRCT repeats contribute to the conformational instability of BRCT-M1775R. Destabilization and global unfolding of the mutated BRCT...
Source: HighBeam Research, Studies describe how mutations affect BRCA1 function.