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The DNA-dependent protein kinase catalytic subunit is phosphorylated in vivo on threonine 3950, a highly conserved amino acid in the protein kinase domain
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Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway
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Protein phosphatase 6 subunit with conserved sit4-associated protein domain targets IκBε
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Three-dimensional structure of the human DNA-PKcs/Ku70/Ku80 complex assembled on DNA and its implications for DNA DSB repair
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Differential involvement of phosphatidylinositol 3-kinase-related protein kinases in hyperphosphorylation of replication protein A2 in response to replication-mediated DNA double-strand breaks
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Clonogenic assay of cells in vitro
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Autophosphorylation of DNA-dependent protein kinase regulates DNA end processing and may also alter double-strand break repair pathway choice
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DNA-PK-dependent phosphorylation of Ku70/80 is not required for non-homologous end joining
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Inhibition of radiation-induced EGFR nuclear import by C225 (Cetuximab) suppresses DNA-PK activity
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Cell cycle dependence of DNA-dependent protein kinase phosphorylation in response to DNA double strand breaks
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The life and death of DNA-PK
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Selective inhibition of the DNA-dependent protein kinase (DNA-PK) by the radiosensitizing agent caffeine
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DNA-PKcs function regulated specifically by protein phosphatase 5
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Phosphatidyl inositol 3-kinase-like serine/threonine protein kinases (PIKKs) are required for DNA damage-induced phosphorylation of the 32 kDa subunit of replication protein A at threonine 21
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Non-homologous end joining requires that the DNA-PK complex undergo an autophosphorylation-dependent rearrangement at DNA ends
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Overlapping binding sites in protein phosphatase 2A for association with regulatory A and α-4 (mTap42) subunits
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PI 3-kinase related kinases: 'big' players in stress-induced signaling pathways
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Initiating cellular stress responses
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Autophosphorylation of the catalytic subunit of the DNA-dependent protein kinase is required for efficient end processing during DNA double-strand break repair
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Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase
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Regulators of serine/threonine protein phosphatases at the dawn of a clinical era?
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The DNA-dependent protein kinase interacts with DNA to form a protein-DNA complex that is disrupted by phosphorylation
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