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XB-ART-8284
Proc Natl Acad Sci U S A October 9, 2001; 98 (21): 12078-83.

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

Joukov V , Chen J , Fox EA , Green JB , Livingston DM .


Abstract
The breast and ovarian susceptibility protein 1 (BRCA1) heterodimerizes with its structural relative, the BRCA1-associated RING domain protein (BARD1), which may have tumor suppressing function in its own right. Both proteins have evolved from a common evolutionary ancestor, and both exist in Xenopus laevis where, similar to their mammalian homologs, they form functional heterodimers. Depleting frog embryos of either BARD1 or BRCA1 led to similar and widely defective developmental phenotypes as well as depletion of the other polypeptide due to its decreased stability. Thus, each protein, in part, controls the abundance, stability, and function of the other, and these effects are heterodimerization-dependent. The interdependent nature of BRCA1 and BARD1 function supports the view that BARD1/BRCA1 heterodimers play a major role in breast and ovarian cancer suppression.

PubMed ID: 11593018
PMC ID: PMC59770
Article link: Proc Natl Acad Sci U S A

Genes referenced: ank1 bard1 brca1 odc1 rad51
Morpholinos: bard1 MO1 bard1 MO2 brca1 MO1 brca1 MO2 brca1 MO3

OMIMs: BREAST CANCER [+]

Article Images: [+] show captions
References [+] :
Cantor, BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function. 2001, Pubmed


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