Evidence map›Paper›PMID 18443218›Full record

ArticleThe Journal of cell biology2008

Telomere dysfunction and cell survival: roles for distinct TIN2-containing complexes.

Sahn-Ho Kim, Albert R Davalos, Seok-Jin Heo, Francis Rodier, Ying Zou, Christian Beausejour, Patrick Kaminker, Steven M Yannone, Judith Campisi

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
–field-weighted citation impact, top 93% 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

37 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Non-canonical roles of canonical telomere binding proteins in cancers.Cellular and molecular life sciences : CMLS · 2021
    Review
  7. Therapeutic Targets in Telomerase and Telomere Biology of Cancers.Indian journal of clinical biochemistry : IJCB · 2020
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Molecular basis of telomere dysfunction in human genetic diseases.Nature structural & molecular biology · 2015
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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

9 authors at 2 institutions in 1 country.

Sahn-Ho KimLife Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. skim3@hfhs.org
Albert R Davalos
Seok-Jin Heo
Francis Rodier
Ying Zou
Christian Beausejour
Patrick Kaminker
Steven M Yannone
Judith Campisi
Lawrence Berkeley National Laboratory · USBuck Institute for Research on Aging · US

Funding

Senescence and Longevity Modulating Genes, WRN and BLMR01AG011658 · NIA · UNIVERSITY OF CALIFORNIA BERKELEY · PI CAMPISI, JUDITH · 1993 to 2008
$2.7M
Role of WRN in Longevity AssuranceR01AG024399 · NIA · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI CAMPISI, JUDITH · 2004 to 2008
$2.0M
Determinants of Telomerase-Negative Cancer CellsR03CA107798 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KIM, SAHN-HO · 2004 to 2005
$164k
NCI NIH HHS CA107798ANCI NIH HHS R03 CA107798NIA NIH HHS AG011658-12NIA NIH HHS AG024399-02NIA NIH HHS R01 AG011658NIA NIH HHS R01 AG024399
6 · The paper itself

Abstract

Telomeres are maintained by three DNA-binding proteins (telomeric repeat binding factor 1 [TRF1], TRF2, and protector of telomeres 1 [POT1]) and several associated factors. One factor, TRF1-interacting protein 2 (TIN2), binds TRF1 and TRF2 directly and POT1 indirectly. Along with two other proteins, TPP1 and hRap1, these form a soluble complex that may be the core telomere maintenance complex. It is not clear whether subcomplexes also exist in vivo. We provide evidence for two TIN2 subcomplexes with distinct functions in human cells. We isolated these two TIN2 subcomplexes from nuclear lysates of unperturbed cells and cells expressing TIN2 mutants TIN2-13 and TIN2-15C, which cannot bind TRF2 or TRF1, respectively. In cells with wild-type p53 function, TIN2-15C was more potent than TIN2-13 in causing telomere uncapping and eventual growth arrest. In cells lacking p53 function, TIN2-15C was more potent than TIN2-13 in causing telomere dysfunction and cell death. Our findings suggest that distinct TIN2 complexes exist and that TIN2-15C-sensitive subcomplexes are particularly important for cell survival in the absence of functional p53.

Indexed as

AnimalsCell LineCell SurvivalCellular SenescenceChromosome AberrationsHumansMacromolecular SubstancesMiceMutationShelterin ComplexTelomeraseTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2Tumor Suppressor Protein p53ACD protein, humanAcd protein, mouseMacromolecular SubstancesPOT1 protein, humanShelterin ComplexTelomeraseTelomere-Binding ProteinsTelomeric Repeat Binding Protein 1Telomeric Repeat Binding Protein 2TINF2 protein, humanTumor Suppressor Protein p53

Identifiers

PMID18443218
PMCPMC2364703
OpenAlexW1604475572

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.