ArticleCell cycle (Georgetown, Tex.)2009
A novel form of the telomere-associated protein TIN2 localizes to the nuclear matrix.
Article in Cell cycle (Georgetown, Tex.), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
30 citing papers in PubMed, 48 citations in OpenAlex.
- C-Terminal Extended Domain-Independent Telomere Maintenance: Modeling the Function of TIN2 Isoforms inInternational journal of molecular sciences · 2025Article
- Article
- Truncating TINF2 p.Tyr312Ter variant and inherited breast cancer susceptibility.Familial cancer · 2023Article
- TIN2 deficiency leads to ALT-associated phenotypes and differentiation defects in embryonic stem cells.Stem cell reports · 2022Article
- TIN2 is an architectural protein that facilitates TRF2-mediated trans- and cis-interactions on telomeric DNA.Nucleic acids research · 2021Article
- Review
- The role of telomerase in the etiology of primary spontaneous pneumothorax.Turk gogus kalp damar cerrahisi dergisi · 2021Article
- The Long Linker Region of Telomere-Binding Protein TRF2 Is Responsible for Interactions with Lamins.International journal of molecular sciences · 2021Article
- Extra-telomeric impact of telomeres: Emerging molecular connections in pluripotency or stemness.The Journal of biological chemistry · 2020Review
- Nuclear envelope attachment of telomeres limits TERRA and telomeric rearrangements in quiescent fission yeast cells.Nucleic acids research · 2020Article
- TIN2 Functions with TPP1/POT1 To Stimulate Telomerase Processivity.Molecular and cellular biology · 2019Article
- The C-Terminal Extension Unique to the Long Isoform of the Shelterin Component TIN2 Enhances Its Interaction with TRF2 in a Phosphorylation- and Dyskeratosis Congenita Cluster-Dependent Fashion.Molecular and cellular biology · 2018Article
- Ubiquitin C-terminal hydrolase isozyme L1 is associated with shelterin complex at interstitial telomeric sites.Epigenetics & chromatin · 2017Article
- Solving the Telomere Replication Problem.Genes · 2017Review
- Review
- Mammalian telomeres and their partnership with lamins.Nucleus (Austin, Tex.) · 2016Review
- Exon-centric regulation of ATM expression is population-dependent and amenable to antisense modification by pseudoexon targeting.Scientific reports · 2016Article
- Telomere- and Telomerase-Associated Proteins and Their Functions in the Plant Cell.Frontiers in plant science · 2016Review
- Article
- Rapamycin induces pluripotent genes associated with avoidance of replicative senescence.Cell cycle (Georgetown, Tex.) · 2013Article
Corrections and comments
- Commented on by
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Telomeres are specialized heterochromatin at the ends of linear chromosomes. Telomeres are crucial for maintaining genome stability and play important roles in cellular senescence and tumor biology. Six core proteins-TRF1, TRF2, TIN2, POT1, TPP1 and Rap1 (termed the telosome or shelterin complex)-regulate telomere structure and function. One of these proteins, TIN2, regulates telomere length and structure indirectly by interacting with TRF1, TRF2 and TPP1, but no direct function has been attributed to TIN2. Here we present evidence for a TIN2 isoform (TIN2L) that differs from the originally described TIN2 isoform (TIN2S) in two ways: TIN2L contains an additional 97 amino acids, and TIN2L associates strongly with the nuclear matrix. Stringent salt and detergent conditions failed to extract TIN2L from the nuclear matrix, despite removing other telomere components, including TIN2S. In human mammary epithelial cells, each isoform showed a distinct nuclear distribution both as a function of cell cycle position and telomere length. Our results suggest a dual role for TIN2 in mediating the function of the shelterin complex and tethering telomeres to the nuclear matrix.
Indexed as
Identifiers
What OpenQuestion holds
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.