Cited by 320Telomeres, Telomerase, and SenescenceDNA Repair MechanismsDNA and Nucleic Acid Chemistry

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Ku70 stimulates fusion of dysfunctional telomeres yet protects chromosome ends from homologous recombination

Celli, Giulia B., Denchi, Eros Lazzerini, de Lange, Titia·2006·Nature Cell Biology

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Abstract

Ku70-Ku80 heterodimers promote the non-homologous end-joining (NHEJ) of DNA breaks and, as shown here, the fusion of dysfunctional telomeres. Paradoxically, this heterodimer is also located at functional mammalian telomeres and interacts with components of shelterin, the protein complex that protects telomeres. To determine whether Ku contributes to telomere protection, we analysed Ku70(-/-) mouse cells. Telomeres of Ku70(-/-) cells had a normal DNA structure and did not activate a DNA damage signal. However, Ku70 repressed exchanges between sister telomeres - a form of homologous recombination implicated in the alternative lengthening of telomeres (ALT) pathway. Sister telomere exchanges occurred at approximately 15% of the chromosome ends when Ku70 and the telomeric protein TRF2 were absent. Combined deficiency of TRF2 and another NHEJ factor, DNA ligase IV, did not elicit this phenotype. Sister telomere exchanges were not elevated at telomeres with functional TRF2, indicating that TRF2 and Ku70 act in parallel to repress recombination. We conclude that mammalian chromosome ends are highly susceptible to homologous recombination, which can endanger cell viability if an unequal exchange generates a critically shortened telomere. Therefore, Ku- and TRF2-mediated repression of homologous recombination is an important aspect of telomere protection.

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Authors: Celli, G. B., Denchi, E. L., & de Lange, T.
Affiliations: Rockefeller University (US)
ORCID: Denchi, Eros Lazzerini
Venue: Nature Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2006-07-16
Volume: 8
Issue: 8
Pages: 885-890
ISSN: 1465-7392 (ISSN-L)
1476-4679
DOI: 10.1038/ncb1444
OpenAlex: W1990507848
Cited by: 320
References: 35
Citations by year: 2026: 3 · 2025: 6 · 2024: 10 · 2023: 11 · 2022: 7 · 2021: 8 · 2020: 15 · 2019: 10 · 2018: 13 · 2017: 12 · 2016: 8 · 2015: 15 · 2014: 22 · 2013: 30 · 2012: 17
FWCI: 15.65
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature Cell Biology (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM 49046)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: Ku70, Ku80, telomere protection, homologous recombination, alternative lengthening of telomeres, TRF2, shelterin, non-homologous end joining, DNA ligase IV, telomere dysfunction
MeSH terms: Ku Autoantigen, DNA Ligase ATP, Animals, DNA Repair, DNA-Binding Proteins, Microscopy, Fluorescence, Models, Biological, DNA Ligases, Recombination, Genetic, Sister Chromatid Exchange, Immunoblotting, Signal Transduction, Telomere, Protein Serine-Threonine Kinases, Mice, Knockout, Chromosomes, Mammalian, Antigens, Nuclear, Telomeric Repeat Binding Protein 2, Mice, Checkpoint Kinase 2

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Ku70 stimulates fusion of dysfunctional telomeres yet protects chromosome ends from homologous recombination

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