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Article

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.

Cell - 27 Jan 2006

Ahnesorg Peter, Smith Philippa, Jackson Stephen P

Abstract excerpt

DNA nonhomologous end-joining (NHEJ) is a predominant pathway of DNA double-strand break repair in mammalian cells, and defects in it cause radiosensitivity at the cellular and whole-organism levels. Central to NHEJ is the protein complex containing DNA Ligase IV and XRCC4. By searching for additional XRCC4-interacting factors, we identified a previously uncharacterized 33 kDa protein, XRCC4-like factor (XLF,...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 16439205
DOI: 10.1016/j.cell.2005.12.031

Genes

XRCC4

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.PMID 16439205Read ↗

Evolutionary and functional conservation of the DNA non-homologous end-joining protein, XLF/Cernunnos.Semantic proximity Read ↗

Interplay between Cernunnos-XLF and Nonhomologous End-joining Proteins at DNA Ends in the CellSemantic proximity Read ↗

Deficiency of XLF and PAXX prevents DNA double-strand break repair by non-homologous end joining in lymphocytesSemantic proximity Read ↗

Crystal structure of human XLF: a twist in nonhomologous DNA end-joining.Semantic proximity Read ↗

Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity.Semantic proximity Read ↗

Defective DNA repair and increased genomic instability in Cernunnos-XLF-deficient murine ES cells.Semantic proximity Read ↗

Lymphocyte-specific compensation for XLF/cernunnos end-joining functions in V(D)J recombination.Semantic proximity Read ↗

Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.Semantic proximity Read ↗

Cernunnos Interacts with the XRCC4·DNA-ligase IV Complex and Is Homologous to the Yeast Nonhomologous End-joining Factor Nej1Semantic proximity Read ↗

Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF.Semantic proximity Read ↗

Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4Semantic proximity Read ↗

PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repairSemantic proximity Read ↗

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