Journal
EMBO JOURNAL
Volume 30, Issue 19, Pages 4047-4058Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2011.280
Keywords
telomerase; telomeres; TPP1; replication; UPF1
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Funding
- ETH Zurich [ETH-15 08-1, ETH-03 08-3]
- Swiss National Science Foundation [3100A0-120090, PP00P3-123356, 323500-115044]
- European Research Council (BFTERRA)
- Fondazione Cariplo [2008-2507]
- Biomedical Research Foundation of the Academy of Athens (BRFAA)
- General Secretariat of Research and Technology/Greek Ministry of Development [05NON-EU-449]
- Swiss National Science Foundation in the laboratory of J Lingner at EPFL
- Swiss National Science Foundation (SNF) [PP00P3_123356] Funding Source: Swiss National Science Foundation (SNF)
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Eukaryotic up-frameshift 1 (UPF1) is a nucleic acid-dependent ATPase and 5'-to-3' helicase, best characterized for its roles in cytoplasmic RNA quality control. We previously demonstrated that human UPF1 binds to telomeres in vivo and its depletion leads to telomere instability. Here, we show that UPF1 is present at telomeres at least during S and G2/M phases and that UPF1 association with telomeres is stimulated by the phosphoinositide 3-kinase (PI3K)-related protein kinase ataxia telangiectasia mutated and Rad3-related (ATR) and by telomere elongation. UPF1 physically interacts with the telomeric factor TPP1 and with telomerase. Akin to UPF1 binding to telomeres, this latter interaction is mediated by ATR. Moreover, the ATPase activity of UPF1 is required to prevent the telomeric defects observed upon UPF1 depletion, and these defects stem predominantly from inefficient telomere leading-strand replication. Our results portray a scenario where UPF1 orchestrates crucial aspects of telomere biology, including telomere replication and telomere length homeostasis. The EMBO Journal (2011) 30, 4047-4058. doi:10.1038/emboj.2011.280; Published online 9 August 2011
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