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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.
Supplier
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.
New
Franken et al., Amsterdam, Netherlands. In Radiat Res, 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.
RON nuclear translocation under hypoxia potentiated chemoresistance to DNA double-strand break-inducing anti-cancer drugs.
New
Chow et al., Zhengzhou, China. In Mol Cancer Ther, 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.
Adipose mesenchymal stromal cells response to ionizing radiation.
New
Muanza et al., Montréal, Canada. In Cytotherapy, 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.
FBXW7 Facilitates Nonhomologous End-Joining via K63-Linked Polyubiquitylation of XRCC4.
New
Sun et al., Ann Arbor, United States. In Mol Cell, 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.
New
Shao et al., Shanghai, China. In Mutat Res Genet Toxicol Environ Mutagen, 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.
DNA-PKcs-Mediated Transcriptional Regulation Drives Prostate Cancer Progression and Metastasis.
New
Impact
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.
Hsp90: A New Player in DNA Repair?
Review
di Masi et al., Roma, Italy. In Biomolecules, 2014
Multiple components of the DNA double strand breaks repair machinery, including BRCA1, BRCA2, CHK1, DNA-PKcs, FANCA, and the MRE11/RAD50/NBN complex, have been described to be client proteins of Hsp90, which acts as a regulator of the diverse DDR pathways.
Regulation of the Target of Rapamycin and Other Phosphatidylinositol 3-Kinase-Related Kinases by Membrane Targeting.
Review
Dames et al., Garching bei München, Germany. In Membranes (basel), 2014
In humans six family members are known to date, namely mammalian/mechanistic target of rapamycin (mTOR), ataxia-telangiectasia mutated (ATM), ataxia- and Rad3-related (ATR), DNA-dependent protein kinase catalytic subunit (DNA-PKcs), suppressor of morphogenesis in genitalia-1 (SMG-1), and transformation/transcription domain-associated protein (TRRAP).
Targeting ATM-deficient CLL through interference with DNA repair pathways.
Review
Reinhardt et al., Köln, Germany. In Front Genet, 2014
We specifically highlight the potential use of PARP1 and DNA-PKcs inhibitors for the treatment of ATM-mutant CLL clones.
Alternative Okazaki Fragment Ligation Pathway by DNA Ligase III.
Review
Iliakis et al., Milano, Italy. In Genes (basel), 2014
Lig4 is responsible for DNA ligation at DNA double strand breaks (DSBs) by the classical, DNA-PKcs-dependent pathway of non-homologous end joining (C-NHEJ).
Preventing Damage Limitation: Targeting DNA-PKcs and DNA Double-Strand Break Repair Pathways for Ovarian Cancer Therapy.
Review
Stronach et al., London, United Kingdom. In Front Oncol, 2014
DNA-dependent protein kinase catalytic subunit (DNA-PKcs) is a core component of NHEJ and it has shown considerable promise as a chemosensitization target in numerous cancer types, including ovarian cancer where it functions to promote platinum-induced survival signaling, via AKT activation.
Nuclear EGFR suppresses ribonuclease activity of polynucleotide phosphorylase through DNAPK-mediated phosphorylation at serine 776.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
GeneRIF
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.
Impact
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.
Impact
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.
Impact
GeneRIF
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.
Impact
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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