The BRCT Domain Is a Phospho-Protein Binding Domain

@article{Yu2003TheBD,
  title={The BRCT Domain Is a Phospho-Protein Binding Domain},
  author={Xiaochun Yu and Claudia Christiano Silva Chini and Miao He and Georges Mer and Junjie Chen},
  journal={Science},
  year={2003},
  volume={302},
  pages={639 - 642}
}
The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain–containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This… 
Functional Evolution of BRCT Domains from Binding DNA to Protein
TLDR
The results suggested that the BRCT domain expansion and functional change in eukaryote may be driven by the evolution of the DNA damage response system.
A Proteomic Approach to Identify Phosphorylation-Dependent Targets of BRCT Domains
TLDR
The results suggest that the BRCT domain acts as a sensor to protein phosphorylation in response to DNA damage, recruits phosphorylated cellular targets, and mediates signaling complex formation, suggesting a more global role of BRCT domains in genome stability surveillance.
Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.
TLDR
It is shown that a phenylalanine in the +3 position from the phosphoserine of BACH1 is bound to a conserved hydrophobic pocket formed between the two BRCT domains and that recognition of the phosphate group is mediated by lysine and serine side chains from the amino-terminal BRCT domain.
Structural basis for phosphorylation-dependent signaling in the DNA-damage response.
TLDR
The studies have revealed a flexible mode of recognition that allows PNK to interact with numerous negatively charged substrates, and a secondary binding pocket at the interface between tandem repeats, which recognizes the amino-acid 3 residues C-terminal to the phosphoserine.
SYNTHÈSE Structural basis for phosphorylation-dependent signaling in the DNA-damage response 1
The response of eukaryotic cells to DNA damage requires a multitude of protein–protein interactions that mediate the ordered repair of the damage and the arrest of the cell cycle until repair is
Phosphopeptide Binding Specificities of BRCA1 COOH-terminal (BRCT) Domains*
TLDR
The BRCA1 COOH-terminal (BRCT) domains are protein modules found in many proteins that regulate DNA damage responses and are a new family of phosphopeptide-binding domains inDNA damage responses, it is reported here that the BRCT domains also recognizeosphopeptides.
Interactions between BRCT repeats and phosphoproteins: tangled up in two.
TLDR
The C-terminal region of the breast-cancer-associated protein BRCA1 contains a pair of tandem BRCT repeats that are essential for the tumour suppressor function of the protein and may mediate phosphorylation-dependent protein-protein interactions in processes that are central to cell-cycle checkpoint and DNA repair functions.
BRCT domains: phosphopeptide binding and signaling modules.
TLDR
This review seeks to discuss the recent biochemical and structural data that have helped elucidate the molecular basis of BRCT domain function and BRCT-mediated interactions, with special emphasis on the role of phospho-specific interactions in key networks that regulate DNA repair.
Characterization of the DNA Binding and Structural Properties of the BRCT region of the p140 subunit of human Replication Factor C
  • 2006
BRCT domains, present in a large number of proteins that are involved in cellcycle regulation and/or DNA replication or repair, are primarily thought to be involved in protein-protein interactions.
Tandem BRCT Domains: DNA's Praetorian Guard.
TLDR
Emerging views of the origin and evolving roles of tandem BRCT domain repeats in the DNA damage response are discussed.
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