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lüll More than just strand breaks: the recognition of structural DNA discontinuities by DNA-dependent protein kinase catalytic subunit Dip R; Naegeli HFASEB J 2005[May]; 19 (7): 704-15The DNA-dependent protein kinase (DNA-PK) is a trimeric factor originally identified as an enzyme that becomes activated upon incubation with DNA. Genetic defects in either the catalytic subunit (DNA-PK(CS)) or the two Ku components of DNA-PK result in immunodeficiency, radiosensitivity, and premature aging. This combined phenotype is generally attributed to the requirement for DNA-PK in the repair of DNA double strand breaks during various biological processes. However, recent studies revealed that DNA-PK(CS), a member of the growing family of phosphatidylinositol 3-kinases, participates in signal transduction cascades related to apoptotic cell death, telomere maintenance and other pathways of genome surveillance. These manifold functions of DNA-PK(CS) have been associated with an increasing number of protein interaction partners and phosphorylation targets. Here we review the DNA binding properties of DNA-PK(CS) and highlight its ability to interact with an astounding diversity of nucleic acid substrates. This survey indicates that the large catalytic subunit of DNA-PK functions as a sensor of not only broken DNA molecules, but of a wider spectrum of aberrant, unusual, or specialized structures that interrupt the standard double helical conformation of DNA.|*DNA Repair[MESH]|Catalytic Domain/genetics/*physiology[MESH]|DNA, Cruciform/chemistry/metabolism[MESH]|DNA-Activated Protein Kinase/*chemistry/*metabolism[MESH]|DNA/chemistry/*metabolism[MESH]|Enzyme Activation[MESH]|Homeostasis[MESH]|Models, Molecular[MESH]|Nucleic Acid Conformation[MESH]|Phosphorylation[MESH]|Recombination, Genetic[MESH]|Signal Transduction[MESH]|Structure-Activity Relationship[MESH]|Substrate Specificity[MESH]|Telomere[MESH] |