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Cited by 284

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP

Open access
Yu, Xiaochun, Fu, Shuang, Lai, Maoyi, Baer, Richard, Chen, Junjie·2006·Genes & Development

Abstract

BRCA1 (Breast Cancer Susceptibility Gene 1) 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.

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Metadata

Authors
Yu, X., Fu, S., Lai, M., Baer, R., & Chen, J.
Venue
Genes & Development
Published
2006-07-01
Volume
20
Issue
13
Pages
1721-1726
ISSN
  • 0890-9369 (ISSN-L)
  • 1549-5477
OpenAlex
W2048839078
Cited by
284
References
7
Type
posted content
Language
en
Open access
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CoChat. (2026). Citation check: BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP. https://app.cochat.ai/papers/10.1101/gad.1431006
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Yu, X., Fu, S., Lai, M., Baer, R., & Chen, J. (2006). BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIP. Genes & Development. https://doi.org/10.1101/gad.1431006

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