Cited by 314Telomeres, Telomerase, and SenescenceDNA and Nucleic Acid ChemistryDNA Repair Mechanisms

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POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end

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Hockemeyer, Dirk, Sfeir, Agnel J, Shay, Jerry W, Wright, Woodring E, de Lange, Titia·2005·The EMBO Journal

DOI 10.1038/sj.emboj.7600733PMC PMC1176460

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Abstract

The hallmarks of telomere dysfunction in mammals are reduced telomeric 3' overhangs, telomere fusions, and cell cycle arrest due to a DNA damage response. Here, we report on the phenotypes of RNAi-mediated inhibition of POT1, the single-stranded telomeric DNA-binding protein. A 10-fold reduction in POT1 protein in tumor cells induced neither telomere fusions nor cell cycle arrest. However, the 3' overhang DNA was reduced and all telomeres elicited a transient DNA damage response in G1, indicating that extensive telomere damage can occur without cell cycle arrest or telomere fusions. RNAi to POT1 also revealed its role in generating the correct sequence at chromosome ends. The recessed 5' end of the telomere, which normally ends on the sequence ATC-5', was changed to a random position within the AATCCC repeat. Thus, POT1 determines the structure of the 3' and 5' ends of human chromosomes, and its inhibition generates a novel combination of telomere dysfunction phenotypes in which chromosome ends behave transiently as sites of DNA damage, yet remain protected from nonhomologous end-joining.

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A biomarker that identifies senescent human cells in culture and in aging skin in vivo.
Dimri, G. P., Lee, X., Basile, G., Acosta, M., Scott, G., Roskelley, C., Medrano, E. E., Linskens, M., Rubelj, I., & Pereira-Smith, O. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9363 · Cited by 7,477
A DNA damage checkpoint response in telomere-initiated senescence
Fagagna, F. D. D., Reaper, P. M., Clay-Farrace, L., Fiegler, H., Carr, P., von Zglinicki, T., Saretzki, G., Carter, N. P., & Jackson, S. P. (2003) · Nature · doi:10.1038/nature02118 · Cited by 2,917 · cited 1×
“In addition, dysfunctional telomeres can induce the ATM kinase and become associated with DNA damage response factors such as 53BP1, g-H2AX, and the Mre11 complex (d’Adda di Fagagna et al, 2003; Takai et al, 2003; Herbig et al, 2004; Celli and de Lange, 2005).”
Background
Mammalian Telomeres End in a Large Duplex Loop
Griffith, J. D., Comeau, L., Rosenfield, S., Stansel, R. M., Bianchi, A., Moss, H., & de Lange, T. (1999) · Cell · doi:10.1016/s0092-8674(00)80760-6 · Cited by 2,447
Telomere shortening associated with chromosome instability is arrested in immortal cells which express telomerase activity.
Counter, C. M., Avilion, A. A., LeFeuvre, C. E., Stewart, N. G., Greider, C. W., Harley, C. B., & Bacchetti, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05245.x · Cited by 2,096 · cited 1×
“NHEJ-mediated chromosome end fusions are a prominent consequence of TRF2 inhibition and can occur when telomeres become critically short (Counter et al, 1992; van Steensel et al, 1998; Smogorzewska et al, 2002).”
Background
TRF2 Protects Human Telomeres from End-to-End Fusions
van Steensel, B., Smogorzewska, A., & de Lange, T. (1998) · Cell · doi:10.1016/s0092-8674(00)80932-0 · Cited by 1,709
DNA Damage Foci at Dysfunctional Telomeres
Takai, H., Smogorzewska, A., & de Lange, T. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00542-6 · Cited by 1,409
Telomere Shortening Triggers Senescence of Human Cells through a Pathway Involving ATM, p53, and p21CIP1, but Not p16INK4a
Herbig, U., Jobling, W. A., Chen, B. P. C., Chen, D. J., & Sedivy, J. M. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00256-4 · Cited by 1,344
p53- and ATM-Dependent Apoptosis Induced by Telomeres Lacking TRF2
Karlseder, J., Broccoli, D., Dai, Y., Hardy, S., & de Lange, T. (1999) · Science · doi:10.1126/science.283.5406.1321 · Cited by 1,086
Pot1, the Putative Telomere End-Binding Protein in Fission Yeast and Humans
Baumann, P., & Cech, T. R. (2001) · Science · doi:10.1126/science.1060036 · Cited by 1,028
Long G Tails at Both Ends of Human Chromosomes Suggest a C Strand Degradation Mechanism for Telomere Shortening
Makarov, V. L., Hirose, Y., & Langmore, J. P. (1997) · Cell · doi:10.1016/s0092-8674(00)81908-x · Cited by 959

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Authors: Hockemeyer, D., Sfeir, A. J., Shay, J. W., Wright, W. E., & de Lange, T.
Affiliations: Rockefeller University (US)
The University of Texas Southwestern Medical Center (US)
ORCID: Hockemeyer, Dirk
Sfeir, Agnel J
Shay, Jerry W
Wright, Woodring E
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 2005-06-23
Volume: 24
Issue: 14
Pages: 2667-2678
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1038/sj.emboj.7600733
PMC: PMC1176460
OpenAlex: W2138398263
Cited by: 314
References: 34
Citations by year: 2026: 9 · 2025: 8 · 2024: 9 · 2023: 11 · 2022: 3 · 2021: 7 · 2020: 16 · 2019: 11 · 2018: 6 · 2017: 15 · 2016: 14 · 2015: 13 · 2014: 21 · 2013: 13 · 2012: 21
FWCI: 12.84
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springernature.com/gp/researchers/text-and-data-mining (tdm)
www.springernature.com/gp/researchers/text-and-data-mining (vor)
Locations: The EMBO Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: U.S. Department of Defense
Ellison Medical Foundation
National Institutes of Health ((AG01228), GM49046)
National Institute on Aging (R56AG016642, AG 01228, AG16642, R01AG001228, R01AG016642)
National Institute of General Medical Sciences (GM 49046, R37GM049046, R01GM049046)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Telomeres, Telomerase, and Senescence
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Keywords: POT1, telomere dysfunction, DNA damage response, chromosome ends, telomere fusion, cell cycle arrest, non-homologous end joining, telomeric repeats, RNAi knockdown, cancer cells
MeSH terms: Shelterin Complex, Chromosomes, Human, DNA Damage, HeLa Cells, Humans, Telomere, Alternative Splicing, Protein Isoforms, Telomere-Binding Proteins, Cell Proliferation

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POT1 protects telomeres from a transient DNA damage response and determines how human chromosomes end

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