ArticleNucleic acids research2005
The leucine rich region of DNA-PKcs contributes to its innate DNA affinity.
Article in Nucleic acids research, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 26 citations in OpenAlex.
- Unlocking the Therapeutic Potential of DNA-PKcs in Cancer: Comprehensive Insights into Mechanisms and Clinical Applications.Cancers · 2025Review
- Two distinct long-range synaptic complexes promote different aspects of end processing prior to repair of DNA breaks by non-homologous end joining.Molecular cell · 2023Article
- DNA-PKcs: A Targetable Protumorigenic Protein Kinase.Cancer research · 2022Review
- Uncovering DNA-PKcs ancient phylogeny, unique sequence motifs and insights for human disease.Progress in biophysics and molecular biology · 2021Article
- Discovery and development of novel DNA-PK inhibitors by targeting the unique Ku-DNA interaction.Nucleic acids research · 2020Article
- C1D family proteins in coordinating RNA processing, chromosome condensation and DNA damage response.Cell division · 2016Review
- The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.Progress in biophysics and molecular biology · 2015Review
- Unraveling the complexities of DNA-dependent protein kinase autophosphorylation.Molecular and cellular biology · 2014Article
- DNA double strand break repair via non-homologous end-joining.Translational cancer research · 2013Article
- The N-terminal region of the DNA-dependent protein kinase catalytic subunit is required for its DNA double-stranded break-mediated activation.The Journal of biological chemistry · 2013Article
- Reversion of the ErbB malignant phenotype and the DNA damage response.Experimental and molecular pathology · 2012Review
- N-terminal constraint activates the catalytic subunit of the DNA-dependent protein kinase in the absence of DNA or Ku.Nucleic acids research · 2012Article
- Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ.Antioxidants & redox signaling · 2011Review
- Choosing the right path: does DNA-PK help make the decision?Mutation research · 2011Review
- Inhibition of homologous recombination by DNA-dependent protein kinase requires kinase activity, is titratable, and is modulated by autophosphorylation.Molecular and cellular biology · 2011Article
- Acetylation of RTN-1C regulates the induction of ER stress by the inhibition of HDAC activity in neuroectodermal tumors.Oncogene · 2009Article
- Repair of ionizing radiation-induced DNA double-strand breaks by non-homologous end-joining.The Biochemical journal · 2009Review
- trans Autophosphorylation at DNA-dependent protein kinase's two major autophosphorylation site clusters facilitates end processing but not end joining.Molecular and cellular biology · 2007Article
- The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain.Molecular and cellular biology · 2007Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
DNA-PK is a protein complex that consists of a DNA-binding, regulatory subunit [Ku] and a larger approximately 465 kDa catalytic subunit [DNA-PKcs], a serine/threonine protein kinase. The kinase activity of DNA-PKcs resides between residues 3745 and 4013, a PI3 kinase domain. Another recognized domain within this large protein is a leucine zipper (LZ) motif or perhaps more appropriately designated a leucine rich region (LRR) that spans residues 1503-1602. Whereas, DNA-PK's kinase activity has been shown to be absolutely indispensable for its function in non-homologous end joining (NHEJ), little is known about the functional relevance of the LRR. Here we show that DNA-PKcs with point mutations in the LRR can only partially reverse the radiosensitive phenotype and V(D)J recombination deficits of DNA-PKcs deficient cells. Disruption of the LRR motif affects the ability to purify DNA-PKcs via its binding to DNA-cellulose, but does not affect its interaction with Ku or its catalytic activity. These data suggest that the LRR region of DNA-PKcs may contribute to its intrinsic DNA affinity, and moreover, that intrinsic DNA binding is important for optimal function of DNA-PKcs in repairing double strand breaks in living cells.
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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.