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Super-Resolution Fluorescence Imaging of Telomeres Reveals TRF2-Dependent T-loop Formation
Open accessAbstract
We have applied a super-resolution fluorescence imaging method, stochastic optical reconstruction microscopy (STORM), to visualize the structure of functional telomeres and telomeres rendered dysfunctional through removal of shelterin proteins. The STORM images showed that functional telomeres frequently exhibit a t-loop configuration. Conditional deletion of individual components of shelterin showed that TRF2 was required for the formation and/or maintenance of t-loops, whereas deletion of TRF1, Rap1, or the POT1 proteins (POT1a and POT1b) had no effect on the frequency of t-loop occurrence. Within the shelterin complex, TRF2 uniquely serves to protect telomeres from two pathways that are initiated on free DNA ends: classical nonhomologous end-joining (NHEJ) and ATM-dependent DNA damage signaling. The TRF2-dependent remodeling of telomeres into t-loop structures, which sequester the ends of chromosomes, can explain why NHEJ and the ATM signaling pathway are repressed when TRF2 is present.
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“Telomeres are repetitive DNA sequences, bound by the six-subunit shelterin complex [86] that facilitates the formation of telomere loops (t-loop) to hide the telomere end [87,88], thus protecting the natural chromosome ends from signaling pathways that sense and act at DNA breaks.”
From Mechanisms and Regulation of Cellular Senescence (2021) · cites this paper as [88]
In the citing paper
“In agreement, TRF2 overexpression delays replicative senescence onset [101], indicating that TRF2 capacity to sequester the telomere terminus via the t-loop conformation [88] might suppress the DNA damage signal from too short telomere ends and protect them from ATM signaling.”
From Mechanisms and Regulation of Cellular Senescence (2021) · cites this paper as [88]
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Kumar, N. M. A., Ghosh, M., Parthasarathy, M., Basak, S., Akula, D., & Singh, M. (2022) · Biomolecular NMR Assignments · doi:10.1007/s12104-022-10074-7 · Cited by 2
“The 3’ single-stranded region of telomere DNA forms folded secondary structures such as the telomere t/D-loop and G-quadruplexes (Griffith et al. 1999; Doksani et al. 2013).”
Targeting telomeric RNA quadruplexes with natural metabolites to prevent cancer
Choudhir, G., Kumar, S., & Kumar, A. (2024) · In Silico Pharmacology · doi:10.1007/s40203-024-00283-4 · Cited by 3
“TRF2, a shelterin interacts with RG4 to increase genome stability (Mei et al. 2021) that helps in t-loop formation and its maintenance (Doksani et al. 2013).”
Inhibition of MRN activity by a telomere protein motifPreprint
Khayat, F., Cannavò, E., Alshmery, M., Foster, W. R., Chahwan, C., Maddalena, M., Smith, C. D., Oliver, A. W., Watson, A. T., Carr, A. M., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.30.437761 · Cited by 2
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Telomeric lncRNA TERRA localizes to stress granules in human ALT cellsPreprint
Larini, L., Goretti, E., Zulian, E., Busarello, E., Marino, S. M., Hajikazemi, M., Paeschke, K., Tebaldi, T., Cusanelli, E., & Juríková, K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.18.599513 · Cited by 2
“The absence of TRF2 at telomeres induces telomere deprotection through alteration of telomere structure and ATM signalling activation 50,51 .”
BackgroundTetrameric TRF2 forms t-loop to protect telomeres from ATM signaling and cNHEJPreprint
Goldfarb, A. M., Sasi, N. K., Dilgen, T. C., Cai, S. W., Myler, L. R., & de Lange, T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.27.600884 · Cited by 2
“T-loop assay was performed as described previously ( 17 ) with minor modifications.”
InfluentialAging-induced stem cell dysfunction: Molecular mechanisms and potential therapeutic avenues
Grajeda, Y., Arias, N., Barrios, A., Pervin, S., & Singh, R. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-820071-1.00005-0 · Cited by 1
Telomeres: Structure and Function
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R-loops and D-loops: a delicate balance in genomic stability and instability
Qin, Z., Lu, M., Zhao, J., Hou, J., Guo, J., Wu, J., Wang, C., Zhu, X., & Ma, T. (2026) · Cell Communication and Signaling · doi:10.1186/s12964-026-03033-5 · Cited by 1
“…by the shelterin component TRF2, which bends and wraps duplex telomeric DNA to facilitate invasion of the 3 ′ G-overhang; recent in vivo evidence indicates that this process can proceed independently of RAD51, distinguishing t-loop assembly from canonical recombinase-driven invasion [163, 303].”
Self-citationSingle-Molecule Choreography between Telomere Proteins and G Quadruplexes
Hopfner, K. (2014) · Structure · doi:10.1016/j.str.2014.05.011 · Cited by 1
“Together with other new and exciting imaging methods that address the structure and dynamics of physiological telomeres (Doksani et al., 2013; Wang et al., 2011), we therefore move from static to dynamic pictures of ier Ltd All rights reserved Myong, S., Bruno, M.M., Pyle, A.M., and Ha, T. (2007).”
MethodThe lighthouse at the end of the chromosome*
Benslimane, Y., & Harrington, L. A. (2015) · F1000Research · doi:10.12688/f1000research.6664.1 · Cited by 1
Telomerase Elongation Cycle: Clues from DNA Sequence Variations
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[Ocular manifestations in hereditary diseases with defects in DNA repair].
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L’importance des télomères dans les infections par les Herpèsvirus humains-6A/B
Collin, V., & Flamand, L. (2022) · médecine/sciences · doi:10.1051/medsci/2022008 · Cited by 1
Telomerase and Its Therapeutic Implications in Cancer
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Tandem Trimer Pyrrole-Imidazole Polyamide Probes Targeting 18 Base Pairs in Human Telomere Sequences
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An Overview of Intracytoplasmic Sperm Injection (ICSI): Its Development and Popularity
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Metadata
- Authors
- Doksani, Y., Wu, J. Y., de Lange, T., & Zhuang, X.
- Affiliations
- Rockefeller University (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Zhuang, Xiaowei
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2013-10
- Volume
- 155
- Issue
- 2
- Pages
- 345-356
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC4062873
- OpenAlex
- W2164580633
- Cited by
- 493
- References
- 69
- Citations by year
- 2026: 12 · 2025: 21 · 2024: 46 · 2023: 36 · 2022: 31 · 2021: 51 · 2020: 40 · 2019: 37 · 2018: 47 · 2017: 42 · 2016: 45 · 2015: 45 · 2014: 36 · 2013: 4
- FWCI
- 30.17
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute on Aging (R56AG016642, AG016642, R01AG016642)
- National Institute of General Medical Sciences (R01GM068518, R37GM049046, R01GM049046, GM 068518, GM096450, R01GM096450, GM049046)
- 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
- telomeres, T-loop, TRF2, shelterin, TRF1, Rap1, POT1, super-resolution fluorescence microscopy, storms, non-homologous end joining, ATM signaling, DNA damage response, telomere dysfunction, telomere protection
- MeSH terms
- Shelterin Complex, Animals, DNA-Binding Proteins, Fibroblasts, Microscopy, Fluorescence, Telomere, Telomere-Binding Proteins, Telomeric Repeat Binding Protein 2, Mice
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