gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 10 Nov 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 Is Involved in Ig Class Switch Recombination in Human B Cells.
Pan-Hammarström et al., Stockholm, Sweden. In J Immunol, 06 Dec 2015
DNA-dependent protein kinase, catalytic subunit (DNA-PKcs) is a component of the classical NHEJ machinery and has a critical function during V(D)J recombination.
Lamin A Is an Endogenous SIRT6 Activator and Promotes SIRT6-Mediated DNA Repair.
Zhou et al., Hong Kong, Hong Kong. In Cell Rep, 04 Dec 2015
Lamin A promotes SIRT6-dependent DNA-PKcs (DNA-PK catalytic subunit) recruitment to chromatin, CtIP deacetylation, and PARP1 mono-ADP ribosylation in response to DNA damage.
Marked contribution of alternative end-joining to chromosome-translocation-formation by stochastically induced DNA double-strand-breaks in G2-phase human cells.
Iliakis et al., Essen, Germany. In Mutat Res Genet Toxicol Environ Mutagen, 30 Nov 2015
Incorrect joining of DNA ends generating chromosome translocations can be catalyzed either by the dominant DNA-PKcs-dependent, classical non-homologous end-joining (c-NHEJ), or by an alternative end-joining (alt-EJ) process, functioning as backup to abrogated c-NHEJ, or homologous recombination repair.
Radiation-induced hyperproliferation of intestinal crypts results in elevated genome instability with inactive p53-related genomic surveillance.
Zhang et al., Lanzhou, China. In Life Sci, 26 Nov 2015
γ-H2AX, 53BP1 and DNA-PKcs were used as DNA repair surrogates to investigate the inherent ability of intestinal crypt cells to recognize and repair double-strand breaks.
Common cancer-associated imbalances in the DNA damage response confer sensitivity to single agent ATR inhibition.
Curtin et al., Abingdon, United Kingdom. In Oncotarget, 15 Nov 2015
Loss of the DNA-binding component, Ku80, caused hypersensitivity to VE-821, but loss of its partner catalytic subunit, DNA-PKcs, did not.
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.
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).
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).
Hsp90: A New Player in DNA Repair?
di Masi et al., Roma, Italy. In Biomolecules, Dec 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.
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