ArticleBiochemistry2008
The BARD1 C-terminal domain structure and interactions with polyadenylation factor CstF-50.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed, 0 citations in OpenAlex.
- Distinct mechanisms of recognition of phosphorylated RNAPII C-terminal domain by BRCT repeats of the BRCA1-BARD1 complex.The Journal of biological chemistry · 2026Article
- BARD1: A Friend or Foe in Pancreatic Ductal Adenocarcinoma?International journal of molecular sciences · 2025Review
- Multiprotein Assemblies, Phosphorylation and Dephosphorylation in Neuronal Cytoskeleton.bioRxiv : the preprint server for biology · 2023Article
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- Article
- Review
- The BRCT Domains of the BRCA1 and BARD1 Tumor Suppressors Differentially Regulate Homology-Directed Repair and Stalled Fork Protection.Molecular cell · 2018Article
- Structural basis to stabilize the domain motion of BARD1-ARD BRCT by CstF50.Scientific reports · 2017Article
- Antagonizing functions of BARD1 and its alternatively spliced variant BARD1δ in telomere stability.Oncotarget · 2017Article
- Oxidative stress controls the choice of alternative last exons via a Brahma-BRCA1-CstF pathway.Nucleic acids research · 2017Article
- C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response.Cell division · 2016Review
- Functional Analysis of BARD1 Missense Variants in Homology-Directed Repair of DNA Double Strand Breaks.Human mutation · 2015Article
- Dysregulated transcription across diverse cancer types reveals the importance of RNA-binding protein in carcinogenesis.BMC genomics · 2015Article
- HDAC inhibitors repress BARD1 isoform expression in acute myeloid leukemia cells via activation of miR-19a and/or b.PloS one · 2013Article
- BRCT domains: easy as one, two, three.Cell cycle (Georgetown, Tex.) · 2011Review
- Impact of BRCA1 BRCT domain missense substitutions on phosphopeptide recognition.Biochemistry · 2011Article
- Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.RNA (New York, N.Y.) · 2011Article
- Tandem BRCT Domains: DNA's Praetorian Guard.Genes & cancer · 2010Article
- Molecular mechanisms of eukaryotic pre-mRNA 3' end processing regulation.Nucleic acids research · 2010Review
- Effect of interdomain dynamics on the structure determination of modular proteins by small-angle scattering.European biophysics journal : EBJ · 2010Article
Corrections and comments
- Erratum issuedNazeer, I [added]; Kleiman, F E [added]
Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The BARD1 N-terminal RING domain binds BRCA1 while the BARD1 C-terminal ankyrin and tandem BRCT repeat domains bind CstF-50 to modulate mRNA processing and RNAP II stability in response to DNA damage. Here we characterize the BARD1 structural biochemistry responsible for CstF-50 binding. The crystal structure of the BARD1 BRCT domain uncovers a degenerate phosphopeptide binding pocket lacking the key arginine required for phosphopeptide interactions in other BRCT proteins. Small angle X-ray scattering together with limited proteolysis results indicates that ankyrin and BRCT domains are linked by a flexible tether and do not adopt a fixed orientation relative to one another. Protein pull-down experiments utilizing a series of purified BARD1 deletion mutants indicate that interactions between the CstF-50 WD-40 domain and BARD1 involve the ankyrin-BRCT linker but do not require ankyrin or BRCT domains. The structural plasticity imparted by the ANK-BRCT linker helps to explain the regulated assembly of different protein BARD1 complexes with distinct functions in DNA damage signaling including BARD1-dependent induction of apoptosis plus p53 stabilization and interactions. BARD1 architecture and plasticity imparted by the ANK-BRCT linker are suitable to allow the BARD1 C-terminus to act as a hub with multiple binding sites to integrate diverse DNA damage signals directly to RNA polymerase.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.