Evidence map›Paper›PMID 21217703›Full record

ArticleNature structural & molecular biology2011

A conserved motif within RAP1 has diversified roles in telomere protection and regulation in different organisms.

Yong Chen, Rekha Rai, Zi-Ren Zhou, Junko Kanoh, Cyril Ribeyre, Yuting Yang, Hong Zheng, Pascal Damay, Feng Wang, Hisayo Tsujii and 5 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

71 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Shelterin is a dimeric complex with extensive structural heterogeneity.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. The evolution of metazoan shelterin.Genes & development · 2021
    Article
  19. Article
  20. Regulation of Antigenic Variation byPathogens (Basel, Switzerland) · 2021
    Review

11 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

15 authors at 7 institutions in 4 countries.

Yong ChenHoward Hughes Medical Institute, University of Michigan Medical School, Ann Arbor, Michigan, USA.
Rekha Rai
Zi-Ren Zhou
Junko Kanoh
Cyril Ribeyre
Yuting Yang
Hong Zheng
Pascal Damay
Feng Wang
Hisayo Tsujii
Yasushi Hiraoka
David Shore
Hong-Yu Hu
Sandy Chang
Ming Lei
The University of Texas MD Anderson Cancer Center · USUniversity of Geneva · CHChinese Academy of Sciences · CNHoward Hughes Medical Institute · USOsaka University · JPUniversity of Michigan–Ann Arbor · USProtein Research Foundation · JP

Funding

Telomere induced senescence as a supressor of tumorigenesisR01CA129037 · NCI · YALE UNIVERSITY · PI CHANG, SANDY S · 2007 to 2017
$3.1M
Structure of the Telomere Shelterin ComplexR01GM083015 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LEI, MING · 2008 to 2012
$1.2M
The role of the telomere capping protein POT1 in mammalian agingR01AG028888 · NIA · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI CHANG, SANDY S · 2007 to 2009
$934k
NCI NIH HHS R01 CA129037NIA NIH HHS R01 AG028888NIGMS NIH HHS R01 GM083015
6 · The paper itself

Abstract

Repressor activator protein 1 (RAP1) is the most highly conserved telomere protein. It is involved in protecting chromosome ends in fission yeast and promoting gene silencing in Saccharomyces cerevisiae, whereas it represses homology-directed recombination at telomeres in mammals. To understand how RAP1 has such diverse functions at telomeres, we solved the crystal or solution structures of the RAP1 C-terminal (RCT) domains of RAP1 from multiple organisms in complex with their respective protein-binding partners. Our analysis establishes RAP1(RCT) as an evolutionarily conserved protein-protein interaction module. In mammalian and fission yeast cells, this module interacts with TRF2 and Taz1, respectively, targeting RAP1 to chromosome ends for telomere protection. In contrast, S. cerevisiae RAP1 uses its RCT domain to recruit Sir3 to telomeres to mediate gene silencing. Together, our results show that, depending on the organism, the evolutionarily conserved RAP1 RCT motif has diverse functional roles at telomeres.

Indexed as

Amino Acid MotifsAmino Acid SequenceAnimalsCells, CulturedCrystallography, X-RayFungal ProteinsHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein Interaction Domains and MotifsSaccharomycetalesSchizosaccharomycesFungal ProteinsShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2TERF2IP protein, humanTERF2 protein, human

Identifiers

PMID21217703
PMCPMC3688267
OpenAlexW2115979683

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Registered trials

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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.