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. 2003 Jul;12(1):247-54.
doi: 10.1016/s1097-2765(03)00281-8.

BRCA1-independent ubiquitination of FANCD2

Cassandra J Vandenberg  1 , Fanni Gergely, Chong Yi Ong, Paul Pace, Donna L Mallery, Kevin Hiom, Ketan J Patel
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Free article

BRCA1-independent ubiquitination of FANCD2

Cassandra J Vandenberg et al. Mol Cell. 2003 Jul.
Free article

Abstract

Monoubiquitination of the FANCD2 protein is a key step in the Fanconi anemia (FA) tumor suppressor pathway, coinciding with this molecule's accumulation at sites of genome damage. Strong circumstantial evidence points to a requirement for the BRCA1 gene product in this step. Here, we show that the purified BRCA1/BARD1 complex, together with E1 and UbcH5a, is sufficient to reconstitute the monoubiquitination of FANCD2 in vitro. Although siRNA-mediated knockdown of BRCA1 in human cells results in defective targeting of FANCD2 to sites of DNA damage, it does not lead to a defect in FANCD2 ubiquitination. Furthermore, ablation of the RING finger domains of either BRCA1 or BARD1 in the chicken B cell line DT40 also leaves FANCD2 modification intact. Consequently, while BRCA1 affects the accumulation of FANCD2 at sites of DNA damage, BRCA1/BARD1 E3 ligase activity is not essential for the monoubiquitination of FANCD2.

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