gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 09 Oct 2015.

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, Ku80, CAN, 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
DNA-PKcs interference sensitizes colorectal cancer cells to a mTOR kinase inhibitor WAY-600.
Han et al., Tianjin, China. In Biochem Biophys Res Commun, 23 Nov 2015
We proposed that DNA-dependent protein kinase catalytic subunit (DNA-PKcs) could be the major resistance factor of WAY-600 in CRC cells.
Synthesis of biotinylated inositol hexakisphosphate to study DNA double-strand break repair and affinity capture of IP6-binding proteins.
Hanakahi et al., In Biochemistry, 23 Oct 2015
We found that IP6-biotin could affinity-capture Ku and other required NHEJ factors from human cell extracts, including the DNA-dependent protein kinase catalytic subunit (DNA-PKcs), XRCC4 and XLF.
A common polymorphism in the 5' UTR of ERCC5 creates an upstream ORF that confers resistance to platinum-based chemotherapy.
Willis et al., Leicester, United Kingdom. In Genes Dev, 15 Oct 2015
Importantly, inhibition of DNA-PKcs restores sensitivity to platinum-based compounds by preventing uORF1-dependent ERCC5 expression.
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.
The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.
Lees-Miller et al., Calgary, Canada. In Prog Biophys Mol Biol, Mar 2015
The DNA-dependent protein kinase (DNA-PK) is a serine/threonine protein kinase composed of a large catalytic subunit (DNA-PKcs) and the Ku70/80 heterodimer.
Targeting ATM-deficient CLL through interference with DNA repair pathways.
Reinhardt et al., Köln, Germany. In Front Genet, Dec 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.
Iliakis et al., Milano, Italy. In Genes (basel), Dec 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).
Regulation of the Target of Rapamycin and Other Phosphatidylinositol 3-Kinase-Related Kinases by Membrane Targeting.
Dames et al., Garching bei München, Germany. In Membranes (basel), Dec 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).
LRF maintains genome integrity by regulating the non-homologous end joining pathway of DNA repair.
Pandolfi et al., Boston, United States. In Nat Commun, Dec 2014
Mechanistically, we show that LRF binds and stabilizes DNA-PKcs on DSBs, in turn favouring DNA-PK activity.
The Mechanism of Radiosensitization by YM155, a Novel Small Molecule Inhibitor of Survivin Expression, is Associated with DNA Damage Repair.
Li et al., In Cell Physiol Biochem, Dec 2014
Co-immunoprecipitation assays using nuclear extracts revealed an interaction between survivin, Ku70, x03B3;-H2AX, and DNA-PKcs.
Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a time.
Tainer et al., Berkeley, United States. In Dna Repair (amst), May 2014
X-ray crystal structures, cryo-electron microscopy envelopes, and small angle X-ray scattering (SAXS) solution conformations and assemblies are defining most of the core protein components for NHEJ: Ku70/Ku80 heterodimer; the DNA dependent protein kinase catalytic subunit (DNA-PKcs); the structure-specific endonuclease Artemis along with polynucleotide kinase/phosphatase (PNKP), aprataxin and PNKP related protein (APLF); the scaffolding proteins XRCC4 and XLF (XRCC4-like factor); DNA polymerases, and DNA ligase IV (Lig IV).
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.
share on facebooktweetadd +1mail to friends