書誌事項
- 公開日
- 2006-07-01
- DOI
-
- 10.1101/gad.1431006
- 公開者
- Cold Spring Harbor Laboratory
この論文をさがす
説明
<jats:p><jats:italic>BRCA1</jats:italic> (<jats:italic>Breast Cancer Susceptibility Gene 1</jats:italic>) possesses an N-terminal Ring domain and tandem C-terminal BRCT motifs. While the Ring domain has E3 ubiquitin ligase activity, the BRCA1 BRCT domains specifically recognize phospho-serine motifs. Here, we demonstrate that BRCA1 Ring domain catalyzes CtIP ubiquitination in a manner that depends on a phosphorylation-mediated interaction between CtIP and BRCA1 BRCT domains. The BRCA1-dependent ubiquitination of CtIP does not target CtIP for degradation. Instead, ubiquitinated CtIP associates with chromatin following DNA damage and participates in G2/M checkpoint control. Thus, we propose that BRCA1 can regulate the functions of its substrates through nonproteasomal pathways that do not involve substrate degradation.</jats:p>
収録刊行物
-
- Genes & Development
-
Genes & Development 20 (13), 1721-1726, 2006-07-01
Cold Spring Harbor Laboratory
