Evidence map›Paper›PMID 24711392›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

SUMOylation regulates telomere length by targeting the shelterin subunit Tpz1(Tpp1) to modulate shelterin-Stn1 interaction in fission yeast.

Keisuke Miyagawa, Ross S Low, Venny Santosa, Hiroki Tsuji, Bettina A Moser, Shiho Fujisawa, Jennifer L Harland, Olga N Raguimova, Andrew Go, Masaru Ueno and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

35 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Fission yeast RPA-TERT-Tpz1bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The Role of Ubiquitination and SUMOylation in Telomere Biology.Current issues in molecular biology · 2020
    Review
  11. Article
  12. Tpz1Communications biology · 2019
    Article
  13. Article
  14. Article
  15. Article
  16. Emerging roles of CST in maintaining genome stability and human disease.Frontiers in bioscience (Landmark edition) · 2018
    Review
  17. Article
  18. Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017
    Review
  19. Article
  20. Article
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

14 authors at 4 institutions in 2 countries.

Keisuke MiyagawaDepartment of Bioscience, School of Science and Technology, Kwansei Gakuin University, Sanda 669-1337, Japan.
Ross S Low
Venny Santosa
Hiroki Tsuji
Bettina A Moser
Shiho Fujisawa
Jennifer L Harland
Olga N Raguimova
Andrew Go
Masaru Ueno
Akihisa Matsuyama
Minoru Yoshida
Toru M Nakamura
Katsunori Tanaka
University of Illinois Chicago · USKwansei Gakuin University · JPRIKEN Center for Sustainable Resource Science · JPHiroshima University · JP

Funding

Roles of Checkpoint and DNA Repair Proteins in Fission Yeast Telomere MaintenanceR01GM078253 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI NAKAMURA, TORU · 2006 to 2019
$4.1M
NIGMS NIH HHS GM078253NIGMS NIH HHS R01 GM078253
6 · The paper itself

Abstract

Telomeres protect DNA ends of linear eukaryotic chromosomes from degradation and fusion, and ensure complete replication of the terminal DNA through recruitment of telomerase. The regulation of telomerase is a critical area of telomere research and includes cis regulation by the shelterin complex in mammals and fission yeast. We have identified a key component of this regulatory pathway as the SUMOylation [the covalent attachment of a small ubiquitin-like modifier (SUMO) to target proteins] of a shelterin subunit in fission yeast. SUMOylation is known to be involved in the negative regulation of telomere extension by telomerase; however, how SUMOylation limits the action of telomerase was unknown until now. We show that SUMOylation of the shelterin subunit TPP1 homolog in Schizosaccharomyces pombe (Tpz1) on lysine 242 is important for telomere length homeostasis. Furthermore, we establish that Tpz1 SUMOylation prevents telomerase accumulation at telomeres by promoting recruitment of Stn1-Ten1 to telomeres. Our findings provide major mechanistic insights into how the SUMOylation pathway collaborates with shelterin and Stn1-Ten1 complexes to regulate telomere length.

Indexed as

SumoylationTelomere HomeostasisCarrier ProteinsDNA-Binding ProteinsG2 PhaseLigasesLysineModels, BiologicalProtein BindingProtein SubunitsSchizosaccharomycesSchizosaccharomyces pombe ProteinsS PhaseTelomeraseTelomereTelomere-Binding ProteinsCarrier ProteinsDNA-Binding ProteinsLigasesLysinePli1 protein, S pombeProtein SubunitsSchizosaccharomyces pombe ProteinsStn1 protein, S pombeTelomeraseTelomere-Binding ProteinsTpz1 protein, S pombeUbiquitin-Protein Ligasescell cycleCST complexDNA replicationS-phase

Identifiers

PMID24711392
PMCPMC4000806
OpenAlexW2093591854

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.