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X-ray repair complementing defective repair in Chinese hamster cells 4

XRCC4
The protein encoded by this gene functions together with DNA ligase IV and the DNA-dependent protein kinase in the repair of DNA double-strand break by non-homologous end joining and the completion of V(D)J recombination events. The non-homologous end-joining pathway is required both for normal development and for suppression of tumors. This gene functionally complements XR-1 Chinese hamster ovary cell mutant, which is impaired in DNA double-strand breaks produced by ionizing radiation and restriction enzymes. Alternative transcription initiation and alternative splicing generates several transcript variants. [provided by RefSeq, Sep 2008] (from NCBI)
Top mentioned proteins: CAN, DNA-PKcs, Ku80, XLF, IRBP
Papers on XRCC4
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.
In cellulo phosphorylation of XRCC4 Ser320 by DNA-PK induced by DNA damage.
New
Matsumoto et al., Tokyo, Japan. In J Radiat Res (tokyo), Jan 2016
UNASSIGNED: XRCC4 is a protein associated with DNA Ligase IV, which is thought to join two DNA ends at the final step of DNA double-strand break repair through non-homologous end joining.
Versatility in phospho-dependent molecular recognition of the XRCC1 and XRCC4 DNA-damage scaffolds by aprataxin-family FHA domains.
New
Smerdon et al., London, United Kingdom. In Dna Repair (amst), Nov 2015
Their primary binding targets are casein kinase 2-phosphorylated forms of the XRCC1 and XRCC4 scaffold molecules which respectively coordinate single-stranded and double-stranded DNA break repair pathways.
Occupational exposure of workers to pesticides: Toxicogenetics and susceptibility gene polymorphisms.
New
Dihl et al., Teresina, Brazil. In Genet Mol Biol, Jul 2015
The exposure of workers from Piauí, Brazil, to these hazardous chemicals was assessed and cytogenetic alterations were evaluated using the buccal micronucleus assay, hematological and lipid parameters, butyrylcholinesterase (BChE) activity and genetic polymorphisms of enzymes involved in the metabolism of pesticides, such as PON1, as well as of the DNA repair system (OGG1, XRCC1 and XRCC4).
DNA repair. PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repair.
New
Impact
Jackson et al., Cambridge, United Kingdom. In Science, Feb 2015
XRCC4 and XLF are two structurally related proteins that function in DNA double-strand break (DSB) repair.
Blood-based DNA methylation of DNA repair genes in the non-homologous end-joining (NEHJ) pathway in patient with glioma.
Zhang et al., Shanghai, China. In Int J Clin Exp Pathol, 2014
UNLABELLED: To investigate the blood-based DNA methylation of repair genes including LIG4, XRCC4, XRCC5, XRCC6 and XRCC7 that involved in non-homologous end-joining (NEHJ) DNA repair pathway in patients with glioma.
Structural insights into NHEJ: building up an integrated picture of the dynamic DSB repair super complex, one component and interaction at a time.
Review
Tainer et al., Berkeley, United States. In Dna Repair (amst), 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
Jeggo et al., Newcastle upon Tyne, United Kingdom. In Dna Repair (amst), 2014
Mutations in XRCC4 or Ku70,80 in patients have not been identified.
XRCC4 and XLF form long helical protein filaments suitable for DNA end protection and alignment to facilitate DNA double strand break repair.
Review
Lees-Miller et al., Calgary, Canada. In Biochem Cell Biol, 2013
One of the most critical steps in NHEJ is ligation of DNA ends by DNA ligase IV (LIG4), which interacts with, and is stabilized by, the scaffolding protein X-ray cross-complementing gene 4 (XRCC4).
A human XRCC4-XLF complex bridges DNA.
GeneRIF
Junop et al., Hamilton, Canada. In Nucleic Acids Res, 2012
Evidence for how XRCC4-XLF complexes robustly bridge DNA molecules.
XRCC4 controls nuclear import and distribution of Ligase IV and exchanges faster at damaged DNA in complex with Ligase IV.
GeneRIF
Mielke et al., Düsseldorf, Germany. In Dna Repair (amst), 2012
XRCC4 modulates the dynamic interaction of the Ligase IV/XRCC4 complex with the NHEJ machinery at double-stranded DNA breaks
Haplotypes of DNA repair and cell cycle control genes, X-ray exposure, and risk of childhood acute lymphoblastic leukemia.
GeneRIF
Buffler et al., Berkeley, United States. In Cancer Causes Control, 2011
haplotypes in NBN and XRCC4, and CDKN2A were associated with structural and numerical change subtypes, respectively, in childhood acute lymphoblastic leukemia
Crystallization and preliminary X-ray diffraction analysis of the human XRCC4-XLF complex.
GeneRIF
Junop et al., Hamilton, Canada. In Acta Crystallogr Sect F Struct Biol Cryst Commun, 2011
Multiple truncations of the XLF and XRCC4 proteins were cocrystallized, but yielded low-resolution diffraction (~20 A)
DNA repair genes polymorphisms in multiple myeloma: no association with XRCC1 (Arg399Gln) polymorphism, but the XRCC4 (VNTR in intron 3 and G-1394T) and XPD (Lys751Gln) polymorphisms is associated with the disease in Turkish patients.
GeneRIF
Pehlivan et al., Gaziantep, Turkey. In Hematology, 2011
Data show that when the genotype frequencies of XPD and XRCC1 genes were examined in the patient and control groups, no significant difference was detected, while a significant association was found in XRCC4 polymorphisms.
Tidying up loose ends: the role of polynucleotide kinase/phosphatase in DNA strand break repair.
Review
GeneRIF
Glover et al., Edmonton, Canada. In Trends Biochem Sci, 2011
Studies indicate that PNKP serves a crucial role in the repair of DNA strand breaks through interactions with other DNA repair proteins, notably XRCC1 and XRCC4.
More forks on the road to replication stress recovery.
Review
Nickoloff et al., Fort Collins, United States. In J Mol Cell Biol, 2011
In recent years, several proteins involved in DSB repair by non-homologous end joining (NHEJ) have been implicated in the replication stress response, including DNA-PKcs, Ku, DNA Ligase IV-XRCC4, Artemis, XLF and Metnase.
ATM damage response and XLF repair factor are functionally redundant in joining DNA breaks.
Impact
Alt et al., Boston, United States. In Nature, 2011
Deficiencies for classical NHEJ factors, such as XRCC4, abrogate lymphocyte development, owing to a strict requirement for classical NHEJ to join V(D)J recombination DSB intermediates.
Mechanism and regulation of class switch recombination.
Review
Impact
Schrader et al., Worcester, United States. In Annu Rev Immunol, 2007
Proteins required for the subsequent S-S recombination include DNA-PK, ATM, Mre11-Rad50-Nbs1, gammaH2AX, 53BP1, Mdc1, and XRCC4-ligase IV.
Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair.
Impact
Kastan et al., Memphis, United States. In Nat Cell Biol, 2007
These two proteins were also required for efficient recruitment of the repair cofactor XRCC4 to DSBs, and for efficient DSB repair.
Endonuclease-independent LINE-1 retrotransposition at mammalian telomeres.
Impact
Moran et al., Ann Arbor, United States. In Nature, 2007
Similar insertions were not detected among EN(i) retrotransposition events generated in controls or in XR-1 CHO cells deficient for XRCC4, an NHEJ factor that is required for DNA ligation but has no known function in telomere maintenance.
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