Evidence map›Paper›PMID 25240060›Full record

ArticleGenes & development2014

Regulated assembly and disassembly of the yeast telomerase quaternary complex.

Timothy M Tucey, Victoria Lundblad

Abstract read
In one paragraph

Article in Genes & development, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  1. Article
  2. The canonical RPA complex interacts with Est3 to regulate yeast telomerase activity.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Review
  4. Review
  5. Article
  6. Review
  7. The structurally conserved TELR region on shelterin protein TPP1 is essential for telomerase processivity but not recruitment.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. RNAs as Regulators of Cellular Matchmaking.Frontiers in molecular biosciences · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Telomerase Mechanism of Telomere Synthesis.Annual review of biochemistry · 2017
    Review
  15. Article
  16. Review
  17. Article
  18. Article
  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

2 authors.

Timothy M TuceyDivision of Biological Sciences, University of California at San Diego, La Jolla, California 92093, USA; Salk Institute for Biological Studies, La Jolla, California 92037, USA.
Victoria LundbladSalk Institute for Biological Studies, La Jolla, California 92037, USA lundblad@salk.edu.

Funding

Viral Vector Core (VVC)P30CA014195 · NCI · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI Ye Zheng · 1985 to 2026
$82.8M
GENETIC MECHANISMS AND REGULATIONT32GM007240 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI HAMPTON, RANDOLPH Y. · 1985 to 2019
$23.8M
Telomere Replication and Senescence in YeastR37AG011728 · NIA · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI LUNDBLAD, VICTORIA · 2003 to 2012
$3.8M
NCI NIH HHS P30 CA014195NCI NIH HHS P30CA014195NIA NIH HHS R37 AG011728NIA NIH HHS R37 AG11728NIGMS NIH HHS T32 GM007240
6 · The paper itself

Abstract

The enzyme telomerase, which elongates chromosome termini, is a critical factor in determining long-term cellular proliferation and tissue renewal. Hence, even small differences in telomerase levels can have substantial consequences for human health. In budding yeast, telomerase consists of the catalytic Est2 protein and two regulatory subunits (Est1 and Est3) in association with the TLC1 RNA, with each of the four subunits essential for in vivo telomerase function. We show here that a hierarchy of assembly and disassembly results in limiting amounts of the quaternary complex late in the cell cycle, following completion of DNA replication. The assembly pathway, which is driven by interaction of the Est3 telomerase subunit with a previously formed Est1-TLC1-Est2 preassembly complex, is highly regulated, involving Est3-binding sites on both Est2 and Est1 as well as an interface on Est3 itself that functions as a toggle switch. Telomerase subsequently disassembles by a mechanistically distinct pathway due to dissociation of the catalytic subunit from the complex in every cell cycle. The balance between the assembly and disassembly pathways, which dictate the levels of the active holoenzyme in the cell, reveals a novel mechanism by which telomerase (and hence telomere homeostasis) is regulated.

Indexed as

Cell CycleImmunoprecipitationModels, MolecularMultiprotein ComplexesProtein BindingProtein Structure, QuaternarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTelomeraseEST2 protein, S cerevisiaeEST3 protein, S cerevisiaeMultiprotein ComplexesSaccharomyces cerevisiae ProteinsTelomeraseEst1Est2Est3telomerasetelomeresTLC1

Identifiers

PMID25240060
PMCPMC4180971

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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.