The BRCT Domain Is a Phospho-Protein Binding Domain

By Xiaochun Yu, C. C. Chini, M. He, G. Mer, Junjie Chen. Science, 2003

883 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology

View Paper: https://www.semanticscholar.org/paper/adae3b3bbe52eda25775b629e3edede8a29c9cc3

How researchers see this paper

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In Molecular Biology

1. M. Jasin
2. J. Bartek
3. Weiran Feng
4. Yu Zhang
5. Rohit Prakash
6. Michael B. Yaffe
7. T. Stracker
8. J. Petrini

In Oncology

1. J. Bartek
2. Michael B. Yaffe
3. J. Petrini
4. M. Jasin
5. M. Kastan
6. T. Stracker
7. Yves Pommier
8. Yosef Shiloh

Citations in the corpus

• PALB2 is an integral component of the BRCA complex required for homologous recombination repair (2009, methodology): “Rabbit polyclonal anti-pH2AX, BACH1, CtIP, and 53BP1 antibodies used were described previously (9, 27, 35).”
• Homologous recombination and human health: the roles of BRCA1, BRCA2 and associated proteins (2015, background): “As CDK-dependent phosphorylation of CtIP is required for CtIP activation and BRCA1-CtIP interaction, it has been proposed that BRCA1 promotes resection by recruiting CDK-phosphorylated/activated CtIP to DSB sites (Yu et al. 2003b; Yu and Chen 2004; Yun and Hiom 2009; Buis et al. 2012).”
• The MRE11 complex: starting from the ends (2011, background): “FHA and tandem BRCT domains generally function as 'stand-alone' phosphopeptide-binding domain”
• Cell-cycle checkpoints and cancer (2004, background): “Interestingly, the BRCT domains have recently been shown to serve as protein-phosphoprotein-binding module”
• Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1 (2021, background): “Close examination of the data in these papers suggests some recruitment for a construct without the C-terminal pair, but all four being required for a robust recruitment or interaction, placing Ser-25 of 53BP1 as a candidate for interaction with BRCT4 of PTIP.”
• RNF8 transduces the DNA-damage signal via histone ubiquitylation and checkpoint protein assembly. (2007, background): “Instead, this selection for aromatic amino acids at the +3 position closely resembles the optimal phosphopeptide motifs recognized by the tandem BRCT domains of BRCA1 and MDC1 (Manke et al., 2003; Stucki et al., 2005; Yu et al., 2003).”
• A Guide for Functional Analysis of BRCA1 Variants of Uncertain Significance (VUS) (2012, background): “The BRCT domains in BRCA1 interact with phosphorylated protein targets containing the sequence pSer-x-x-Phe [Botuyan et al., 2004; Clapperton et al., 2004; Rodriguez et al., 2003; Shiozaki et al., 2004; Williams et al., 2004; Yu et al., 2003] (Fig.”
• Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis (2010, neutral): “BRIP1, a DNA helicase originally identified as BACH1 and later as FANCJ, binds to the BRCA1 BRCT repeats in S phase following its phosphorylatio”