Evidence map›Paper›PMID 16880378›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

A critical role for TPP1 and TIN2 interaction in high-order telomeric complex assembly.

Matthew S O'Connor, Amin Safari, Huawei Xin, Dan Liu, Zhou Songyang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
8.1field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

133 citing papers in PubMed, 247 citations in OpenAlex.

  1. A unified photosensitizer platform forbioRxiv : the preprint server for biology · 2026
    Article
  2. Telomere Crisis Shapes Cancer Evolution.Cold Spring Harbor perspectives in biology · 2026
    Review
  3. Article
  4. Review
  5. Protection of the Telomeric Junction by the Shelterin Complex.Journal of the American Chemical Society · 2024
    Article
  6. Protection of the Telomeric Junction by the Shelterin Complex.bioRxiv : the preprint server for biology · 2024
    Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. HGG advances · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Telomere maintenance in African trypanosomes.Frontiers in molecular biosciences · 2023
    Review
  18. Article
  19. Article
  20. Article

73 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Matthew S O'ConnorVerna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.
Amin Safari
Huawei Xin
Dan Liu
Zhou Songyang
Baylor College of Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mammalian telomeric proteins function through dynamic interactions with each other and telomere DNA. We previously reported the formation of a high-molecular-mass telomeric complex (the mammalian telosome) that contains the six core proteins TRF1, TRF2, RAP1, TIN2, POT1, and TPP1 (formerly named PTOP/PIP1/TINT1) and mediates telomere end-capping and length control. In this report, we sought to elucidate the mechanism of six-protein complex (or shelterin) formation and the function of this complex. Through reconstitution experiments, we demonstrate here that TIN2 and TPP1 are key components in mediating the six-protein complex assembly. We demonstrate that not only TIN2 but also TPP1 are required to bridge the TRF1 and TRF2 subcomplexes. Specifically, TPP1 helps to stabilize the TRF1-TIN2-TRF2 interaction and promote six-protein complex formation. Consistent with this model, overexpression of TPP1 enhanced TIN2-TRF2 association. Conversely, knocking down TPP1 reduced the ability of endogenous TRF1 to associate with the TRF2 complex. Our results suggest that coordinated interactions among TPP1, TIN2, TRF1, and TRF2 may ensure robust assembly of the telosome, telomere targeting of its subunits, and, ultimately, regulated telomere maintenance.

Indexed as

AnimalsHeLa CellsHumansInsectaModels, BiologicalNuclear ProteinsProtein BindingProtein Structure, TertiaryShelterin ComplexTATA Box Binding Protein-Like ProteinsTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2ACD protein, humanNuclear ProteinsShelterin ComplexTATA Box Binding Protein-Like ProteinsTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2TERF2 protein, humanTINF2 protein, human

Identifiers

PMID16880378
PMCPMC1567669
OpenAlexW2145952889

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.