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Protein kinase, DNA-activated, catalytic polypeptide

DNA-PKcs, DNA-dependent protein kinase catalytic subunit, P350, DNA-PK catalytic subunit
This gene encodes the catalytic subunit of the DNA-dependent protein kinase (DNA-PK). It functions with the Ku70/Ku80 heterodimer protein in DNA double strand break repair and recombination. The protein encoded is a member of the PI3/PI4-kinase family.[provided by RefSeq, Jul 2010] (from NCBI)
Top mentioned proteins: Atm, IRBP, CAN, Ku80, H2A
Papers using DNA-PKcs antibodies
Inhibition of radiation-induced EGFR nuclear import by C225 (Cetuximab) suppresses DNA-PK activity.
Blagosklonny Mikhail V., In PLoS ONE, 2004
... mouse monoclonal, anti-Ku86 mouse monoclonal and anti-tubulin mouse monoclonal (Santa Cruz Biotechnology, Santa Cruz, CA); anti-DNA-PKcs Thr2609 phosphospecific rabbit polyclonal (Abcam, City, State); anti-RPA2 mouse ...
Papers on DNA-PKcs
Predicting Radiosensitivity with Gamma-H2AX Foci Assay after Single High-Dose-Rate and Pulsed Dose-Rate Ionizing Irradiation.
Franken et al., Amsterdam, Netherlands. In Radiat Res, 20 Feb 2016
In this study, we investigated the induction and decay of γ-H2AX foci of different tumor cell lines and fibroblasts with known mutations in DNA damage repair genes, including ATM, LigIV, DNA-PKcs, Rad51 and Rad54.
Adipose mesenchymal stromal cells response to ionizing radiation.
Muanza et al., Montréal, Canada. In Cytotherapy, 15 Feb 2016
Irradiated aMSCs expressed higher □H2AX and significantly showed faster and more time-efficient IR-induced DNA damage response evident by up-regulated DNA-PKcs and RAD51.
RON nuclear translocation under hypoxia potentiated chemoresistance to DNA double-strand break-inducing anti-cancer drugs.
Chow et al., Zhengzhou, China. In Mol Cancer Ther, 15 Feb 2016
Nuclear RON interacted with adenosine triphosphate (ATP)-dependent DNA helicase 2 (Ku-70) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to activate non-homologous end-joining (NHEJ) DNA repair.
FBXW7 Facilitates Nonhomologous End-Joining via K63-Linked Polyubiquitylation of XRCC4.
Sun et al., Ann Arbor, United States. In Mol Cell, 06 Feb 2016
In response to ionizing radiation, ATM phosphorylates FBXW7 at serine 26 to recruit it to DNA double-strand break (DSB) sites, whereas activated DNA-PKcs phosphorylates XRCC4 at serines 325/326, which promotes binding of XRCC4 to FBXW7.
G2-M phase-correlative bystander effects are co-mediated by DNA-PKcs and ATM after carbon ion irradiation.
Shao et al., Shanghai, China. In Mutat Res Genet Toxicol Environ Mutagen, 01 Feb 2016
Meanwhile, the activity of DNA-PKcs but not ATM was increased in the synchronized G2-M phase cells in spite of both of them were activated in the asynchronous cells after carbon ion irradiation.
Knockdown of Cathepsin L promotes radiosensitivity of glioma stem cells both in vivo and in vitro.
Liang et al., Suzhou, China. In Cancer Lett, 17 Jan 2016
Knockdown of Cathepsin L resulted in a dramatic reduction of CD133 expression, as well as the decreased phosphorylation of DNA repair checkpoint proteins (ATM and DNA-PKcs).
Cyclin D1 silencing suppresses tumorigenicity, impairs DNA double strand break repair and thus radiosensitizes androgenindependent prostate cancer cells to DNA damage.
Pestell et al., L'Aquila, Italy. In Oncotarget, 12 Jan 2016
Concordant with these observations DNA-PKcs-activation and RAD51-accumulation, part of the DNA double-strand break repair machinery, were reduced in shRNA-cyclin D1 treated cells compared to shRNA control.
Inhibition of DNA-PKcs enhances radiosensitivity and increases the levels of ATM and ATR in NSCLC cells exposed to carbon ion irradiation.
Wang et al., Lanzhou, China. In Oncol Lett, Nov 2015
In the present study, normal lung fibroblast MRC-5 and lung cancer A549 cells were treated with NU7026 and CGK733, which are inhibitors of the DNA-dependent protein kinase catalytic subunit (PKcs) and ataxia telangiectasia mutated (ATM) and ataxia telangiectasia and Rad3-related (ATR), respectively, followed by exposure to X-rays and carbon ion irradiation.
DNA-PKcs-Mediated Transcriptional Regulation Drives Prostate Cancer Progression and Metastasis.
Knudsen et al., Philadelphia, United States. In Cancer Cell, Aug 2015
Emerging evidence demonstrates that the DNA repair kinase DNA-PKcs exerts divergent roles in transcriptional regulation of unsolved consequence.
ATM, ATR and DNA-PKcs expressions correlate to adverse clinical outcomes in epithelial ovarian cancers.
Madhusudan et al., Nottingham, United Kingdom. In Bba Clin, 2014
BACKGROUND: Ataxia-telangiectasia mutated (ATM), ataxia-telangiectasia mutated and rad3 related (ATR) and DNA-dependent protein kinase catalytic sub-unit (DNA-PKcs) play critical roles in DNA damage response (DDR) by linking DNA damage sensing to DDR effectors that regulate cell cycle progression and DNA repair.
DNA-Dependent Protein Kinase As Molecular Target for Radiosensitization of Neuroblastoma Cells.
Molenaar et al., Amsterdam, Netherlands. In Plos One, 2014
DNA-PKcs is encoded by the PRKDC (protein kinase, DNA-activated, catalytic polypeptide) gene.
Nuclear EGFR suppresses ribonuclease activity of polynucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776.
Hung et al., Taiwan. In J Biol Chem, 2012
a novel role of nEGFR in radioresistance, and that is, upon ionizing radiation, nEGFR inactivates the ribonuclease activity of PNPase toward c-MYC mRNA through DNAPK-mediated Ser-776 phosphorylation
Genetic variation in DNA repair gene XRCC7 (G6721T) and susceptibility to breast cancer.
Saadat et al., Shīrāz, Iran. In Gene, 2012
Using RFLP-PCR based method, the polymorphism of XRCC7 was determined. The TG (OR=1.20, 95% CI: 0.83-1.74, P=0.320) and TT (OR=1.01, 95% CI: 0.67-1.53, P=0.933) genotypes had no significant effect on risk of breast cancer
Heat shock protein 90α (HSP90α), a substrate and chaperone of DNA-PK necessary for the apoptotic response.
Pommier et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2012
DNA-PK phosphorylates HSP90alpha on threonines 5 and 7 early during apoptosis and both phosphorylated HSP90alpha and DNA-PK colocalize in the apoptotic ring.
Recessive mutations in MCM4/PRKDC cause a novel syndrome involving a primary immunodeficiency and a disorder of DNA repair.
Ennis et al., Dublin, Ireland. In J Med Genet, 2012
Mutations in MCM4/PRKDC represent a novel cause of DNA breakage and NK cell deficiency.
DNAPKcs-dependent arrest of RNA polymerase II transcription in the presence of DNA breaks.
Soutoglou et al., Illkirch-Graffenstaden, France. In Nat Struct Mol Biol, 2012
results point to the pivotal role of DNAPK activity in the eviction of RNAPII from DNA upon encountering a DNA lesion
Mechanistic rationale for inhibition of poly(ADP-ribose) polymerase in ETS gene fusion-positive prostate cancer.
Chinnaiyan et al., Ann Arbor, United States. In Cancer Cell, 2011
We investigate the mechanisms by which ETS fusions mediate their effects, and find that the product of the predominant ETS gene fusion, TMPRSS2:ERG, interacts in a DNA-independent manner with the enzyme poly (ADP-ribose) polymerase 1 (PARP1) and the catalytic subunit of DNA protein kinase (DNA-PKcs).
Recapitulation of premature ageing with iPSCs from Hutchinson-Gilford progeria syndrome.
Izpisua Belmonte et al., Los Angeles, United States. In Nature, 2011
Additionally, our studies identify DNA-dependent protein kinase catalytic subunit (DNAPKcs, also known as PRKDC) as a downstream target of progerin.
Crystal structure of DNA-PKcs reveals a large open-ring cradle comprised of HEAT repeats.
Blundell et al., Cambridge, United Kingdom. In Nature, 2010
crystal structure of human DNA-PKcs at 6.6 A resolution, in which the overall fold is clearly visible for the first time
DNA-PKcs-PIDDosome: a nuclear caspase-2-activating complex with role in G2/M checkpoint maintenance.
Du et al., Kansas City, United States. In Cell, 2009
This phosphorylation is carried out by the nuclear serine/threonine protein kinase DNA-PKcs and promoted by the p53-inducible death-domain-containing protein PIDD within a large nuclear protein complex consisting of DNA-PKcs, PIDD, and caspase-2, which we have named the DNA-PKcs-PIDDosome.
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