ArticleThe Journal of biological chemistry2013
Identification and functional characterization of a Ku-binding motif in aprataxin polynucleotide kinase/phosphatase-like factor (APLF).
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 40 citations in OpenAlex.
- Article
- Chaperoning of the histone octamer by the acidic domain of DNA repair factor APLF.Science advances · 2022Article
- Zinc finger protein ZNF384 is an adaptor of Ku to DNA during classical non-homologous end-joining.Nature communications · 2021Article
- X-ray scattering reveals disordered linkers and dynamic interfaces in complexes and mechanisms for DNA double-strand break repair impacting cell and cancer biology.Protein science : a publication of the Protein Society · 2021Review
- Stages, scaffolds and strings in the spatial organisation of non-homologous end joining: Insights from X-ray diffraction and Cryo-EM.Progress in biophysics and molecular biology · 2021Article
- The Ku complex: recent advances and emerging roles outside of non-homologous end-joining.Cellular and molecular life sciences : CMLS · 2021Review
- Article
- Ligand binding characteristics of the Ku80 von Willebrand domain.DNA repair · 2020Article
- Rewiring E2F1 with classical NHEJ via APLF suppression promotes bladder cancer invasiveness.Journal of experimental & clinical cancer research : CR · 2019Article
- Evolutionary diversity and novelty of DNA repair genes in asexual Bdelloid rotifers.BMC evolutionary biology · 2018Article
- XLF and APLF bind Ku80 at two remote sites to ensure DNA repair by non-homologous end joining.Nature structural & molecular biology · 2018Article
- DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface.Nucleic acids research · 2018Article
- Structural and functional characterization of the PNKP-XRCC4-LigIV DNA repair complex.Nucleic acids research · 2017Article
- An Intrinsically Disordered APLF Links Ku, DNA-PKcs, and XRCC4-DNA Ligase IV in an Extended Flexible Non-homologous End Joining Complex.The Journal of biological chemistry · 2016Article
- Histone chaperone APLF regulates induction of pluripotency in murine fibroblasts.Journal of cell science · 2016Article
- FASN regulates cellular response to genotoxic treatments by increasing PARP-1 expression and DNA repair activity via NF-κB and SP1.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Attenuated DNA damage repair delays therapy-related myeloid neoplasms in a mouse model.Cell death & disease · 2016Article
- The Ku-binding motif is a conserved module for recruitment and stimulation of non-homologous end-joining proteins.Nature communications · 2016Article
- The Expression Levels of XLF and Mutant P53 Are Inversely Correlated in Head and Neck Cancer Cells.Journal of Cancer · 2016Article
- Non-homologous end joining often uses microhomology: implications for alternative end joining.DNA repair · 2014Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Aprataxin polynucleotide kinase/phosphatase-like factor (APLF) facilitates nonhomologous end joining (NHEJ) and associates with the core NHEJ components XRCC4-DNA ligase IV and Ku. The APLF forkhead-associated (FHA) domain directs interactions with XRCC4, but the APLF-Ku interaction has not been well characterized. Here we describe an evolutionarily conserved amino acid motif within APLF that is required for mediating the physical interaction between APLF and Ku. This APLF Ku-binding motif possesses a similarity to regions identified in other NHEJ factors, WRN and XLF, which also direct interactions with Ku. Indeed, peptides derived from the Ku-binding region of APLF, WRN, or XLF were sufficient to reconstitute the interaction with Ku in vitro. Although APLF is localized predominantly to the nucleus, it does not possess a nuclear localization signal (NLS). Interestingly, the disruption of the APLF-Ku interaction by substituting key residues in the APLF Ku-binding motif was associated with increased relocalization of APLF to the cytoplasm and reduced association with XRCC4, which was rescued by the introduction of an NLS onto APLF. When human cells stably depleted of APLF were reconstituted with APLF Ku-binding mutants, or with an APLF FHA mutant that is known to disrupt interactions with XRCC4, APLF-dependent NHEJ and the retention of APLF at sites of laser-generated DNA damage were impaired. These data suggest functional requirements for Ku and XRCC4 in APLF-dependent NHEJ and a unique role for Ku as a factor required to facilitate the nuclear retention of APLF.
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