ArticleCell reports2025
TRF1 and TRF2 form distinct shelterin subcomplexes at telomeres.
Article in Cell reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Beyond End Protection: Shelterin, POT1 Dysfunction, and Telomere Replication Stress in Cancer.Biomolecules · 2026Review
- Inhibition of lagging strand replication by G-rich telomeric DNA and the shelterin subunit POT1.The EMBO journal · 2026Article
- R-loops and D-loops: a delicate balance in genomic stability and instability.Cell communication and signaling : CCS · 2026Review
- Structural basis for TRF2-RAP1 recruitment by EBNA1 at the EBV origin of replication.Scientific reports · 2026Article
- Fluorogenic speed-optimized DNA-PAINT probes enable super-resolution imaging of whole cells.bioRxiv : the preprint server for biology · 2026Article
- Structural organization and function of telomeric chromatin.Nature cell biology · 2026Review
- Discovery of first-in-class inhibitors of the TRF1:TIN2 protein:protein interaction by fragment screening.Scientific reports · 2025Article
- Structural Basis for TRF2-RAP1 Recruitment by EBNA1 at the EBV origin of replication.Research square · 2025Article
- Protocol for fast antibiotic resistance-based gene editing of mammalian cells with CRISPR-Cas9.STAR protocols · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
The shelterin complex protects chromosome ends from aberrant DNA repair and regulates telomerase access to telomeres. Shelterin is composed of six proteins (TRF1, TRF2, TIN2, TPP1, POT1, and RAP1) that can assemble into various subcomplexes in vitro, but their stoichiometry and dynamics in cells remain poorly understood. To quantitatively analyze shelterin function, we generated a panel of human cancer cell lines expressing HaloTagged shelterin proteins from their endogenous loci. We determined both the total and telomeric abundance of each subunit, demonstrating that shelterin proteins are present at telomeres in equal numbers. Using single-molecule live-cell imaging, we showed that TRF1-TIN2-TPP1-POT1 and TRF2-RAP1 form distinct subcomplexes that bind non-overlapping sites on telomeric chromatin. TRF1-TIN2-TPP1-POT1 tightly associates with telomeres, whereas TRF2-RAP1 binds more dynamically, facilitating the recruitment of co-factors that protect chromosome ends. Altogether, our work provides mechanistic insight into shelterin function in telomere maintenance and advances our understanding of telomeric chromatin architecture.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.