ArticleScientific reports2015
Nuclear Localization of the DNA Repair Scaffold XRCC1: Uncovering the Functional Role of a Bipartite NLS.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- GCN5 and TADA2B constitutively regulate XRCC1 function during DNA repair to maintain cell survival.Cell death and differentiation · 2026Article
- The zinc finger of DNA ligase 3α binds to nucleosomes via an arginine anchor.Nature communications · 2025Article
- Exploring homologous recombination repair and base excision repair pathway genes for possible diagnostic markers in hematologic malignancies.Molecular genetics and genomics : MGG · 2023Article
- Nuclear localization of human MEIOB requires its NLS in the OB domain and interaction with SPATA22.Acta biochimica et biophysica Sinica · 2022Article
- Nuclear-Import Receptors Counter Deleterious Phase Transitions in Neurodegenerative Disease.Journal of molecular biology · 2022Review
- The base excision repair process: comparison between higher and lower eukaryotes.Cellular and molecular life sciences : CMLS · 2021Review
- Phosphopeptide interactions of the Nbs1 N-terminal FHA-BRCT1/2 domains.Scientific reports · 2021Article
- XRCC1 - Strategies for coordinating and assembling a versatile DNA damage response.DNA repair · 2020Review
- Linker region is required for efficient nuclear localization of polynucleotide kinase phosphatase.PloS one · 2020Article
- Ligand binding characteristics of the Ku80 von Willebrand domain.DNA repair · 2020Article
- Identification of an XRCC1 DNA binding activity essential for retention at sites of DNA damage.Scientific reports · 2019Article
- Defective base excision repair in the response to DNA damaging agents in triple negative breast cancer.PloS one · 2019Article
- Variations in nuclear localization strategies among pol X family enzymes.Traffic (Copenhagen, Denmark) · 2018Article
- Characterization of the APLF FHA-XRCC1 phosphopeptide interaction and its structural and functional implications.Nucleic acids research · 2017Article
- Mechanism for G2 phase-specific nuclear export of the kinetochore protein CENP-F.Cell cycle (Georgetown, Tex.) · 2017Article
- p38 MAPK signaling and phosphorylations in the BRCT1 domain regulate XRCC1 recruitment to sites of DNA damage.Scientific reports · 2017Article
- DNA polymerase β contains a functional nuclear localization signal at its N-terminus.Nucleic acids research · 2017Article
- ZNF687 Mutations in Severe Paget Disease of Bone Associated with Giant Cell Tumor.American journal of human genetics · 2016Article
- Article
- Motifs of the C-terminal domain of MCM9 direct localization to sites of mitomycin-C damage for RAD51 recruitment.The Journal of biological chemistryArticle
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8 authors.
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Abstract
We have characterized the nuclear localization signal (NLS) of XRCC1 structurally using X-ray crystallography and functionally using fluorescence imaging. Crystallography and binding studies confirm the bipartite nature of the XRCC1 NLS interaction with Importin α (Impα) in which the major and minor binding motifs are separated by >20 residues, and resolve previous inconsistent determinations. Binding studies of peptides corresponding to the bipartite NLS, as well as its major and minor binding motifs, to both wild-type and mutated forms of Impα reveal pronounced cooperative binding behavior that is generated by the proximity effect of the tethered major and minor motifs of the NLS. The cooperativity stems from the increased local concentration of the second motif near its cognate binding site that is a consequence of the stepwise binding behavior of the bipartite NLS. We predict that the stepwise dissociation of the NLS from Impα facilitates unloading by providing a partially complexed intermediate that is available for competitive binding by Nup50 or the Importin β binding domain. This behavior provides a basis for meeting the intrinsically conflicting high affinity and high flux requirements of an efficient nuclear transport system.
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