Identifying physiological substrates of DNA-dependent protein kinase (DNA-PK)
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AbstractThe DNA-dependent protein kinase (DNA-PK) is required for the repair of DNA double strand breaks (DSB) in human cells. DNA-PK is a serine/threonine protein kinase composed of a 469 kDa catalytic subunit (DNA-PKcs) and a DNA targeting subunit, Ku. Previous studies have demonstrated a requirement of the protein kinase activity of DNA-PK during non homologous end joining-mediated repair of DNA DSBs and during variable (diversity) joining [V(D)J] recombination. However, its physiological substrates are not well defined. Here we have utilized a broad-based proteomics approach to attempt to identify DNA-PK-dependent phosphorylation events. Utilizing a more targeted approach involving immunoprecipitation of DNA-PKcs, an ionizing radiation-dependent interaction between DNA-PKcs and p53 transcription factor was identified in human lymphoblastoid cells.
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