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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 27 Aug 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.
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
Recruitment and activation of the ATM kinase in the absence of DNA-damage sensors.
New
Ferguson et al., Ann Arbor, United States. In Nat Struct Mol Biol, 17 Sep 2015
UNASSIGNED: Two kinases, ATM and DNA-PKcs, control rapid responses to DNA double-strand breaks (DSBs).
Unifying the DNA End Processing Roles of the Artemis Nuclease: Ku-Dependent Artemis Resection at Blunt DNA Ends.
New
Lieber et al., United States. In J Biol Chem, 14 Sep 2015
All DNA ends are cut when both DNA-PKcs and Ku accompany Artemis, but not when Ku is omitted.
XRCC4 deficiency in human subjects causes a marked neurological phenotype but no overt immunodeficiency.
New
Ogi et al., Nagoya, Japan. In J Allergy Clin Immunol, 23 Aug 2015
Patients with mutations in genes encoding LIG4, XRCC4-like factor, or the other NHEJ proteins DNA-dependent protein kinase catalytic subunit and Artemis are DSB repair defective and immunodeficient because of the requirement for NHEJ during V(D)J recombination.
DNA-PKcs-Mediated Transcriptional Regulation Drives Prostate Cancer Progression and Metastasis.
New
Impact
Knudsen et al., Philadelphia, United States. In Cancer Cell, 13 Aug 2015
Emerging evidence demonstrates that the DNA repair kinase DNA-PKcs exerts divergent roles in transcriptional regulation of unsolved consequence.
DNA repair prognostic index modelling reveals an essential role for base excision repair in influencing clinical outcomes in ER negative and triple negative breast cancers.
New
Madhusudan et al., Nottingham, United Kingdom. In Oncotarget, Jul 2015
In the current study, a cohort of 880 ER- (including 635 TNBCs) was immuno-profiled for a panel of DNA repair proteins including: Pol β, FEN1, APE1, XRCC1, SMUG1, PARP1, BRCA1, ATR, ATM, DNA-PKcs, Chk1, Chk2, p53, and TOPO2.
The DNA-dependent protein kinase: A multifunctional protein kinase with roles in DNA double strand break repair and mitosis.
Review
New
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.
Alternative Okazaki Fragment Ligation Pathway by DNA Ligase III.
Review
New
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).
Targeting ATM-deficient CLL through interference with DNA repair pathways.
Review
New
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.
Pharmacological inhibition of DNA-PK stimulates Cas9-mediated genome editing.
New
Pelletier et al., Montréal, Canada. In Genome Med, Dec 2014
METHODS: We investigated the possibility of pharmacologically inhibiting DNA-PKcs, a key player in NHEJ, using small molecule inhibitors (NU7441 and KU-0060648), to ameliorate the rates of HDR repair events.
Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a time.
Review
New
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).
The clinical impact of deficiency in DNA non-homologous end-joining.
Review
New
Jeggo et al., Newcastle upon Tyne, United Kingdom. In Dna Repair (amst), Apr 2014
Mutations in NHEJ genes, defining human syndromes deficient in DNA ligase IV (LIG4 Syndrome), XLF-Cernunnos, Artemis or DNA-PKcs, have been identified in such patients.
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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