Evidence map›Paper›PMID 25329641›Full record

ArticlePLoS genetics2014

POT1a and components of CST engage telomerase and regulate its activity in Arabidopsis.

Kyle B Renfrew, Xiangyu Song, Jung Ro Lee, Amit Arora, Dorothy E Shippen

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

30 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. The leaves fall, yet the tree endures.Cellular and molecular life sciences : CMLS · 2025
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Single-Run Catalysis and Kinetic Control of Human Telomerase Holoenzyme.Advances in experimental medicine and biology · 2022
    Review
  9. Article
  10. Telomerase Interaction Partners-Insight from Plants.International journal of molecular sciences · 2021
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  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

5 authors at 1 institution in 1 country.

Kyle B RenfrewDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Xiangyu SongDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Jung Ro LeeDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Amit AroraDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Dorothy E ShippenDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, United States of America.
Texas A&M University · US

Funding

Telomere Structure and Function in ArabidopsisR01GM065383 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI SHIPPEN, DOROTHY · 2002 to 2023
$6.8M
NIGMS NIH HHS R01 GM065383NIGMS NIH HHS R01-GM065383
6 · The paper itself

Abstract

Protection of Telomeres 1 (POT1) is a conserved nucleic acid binding protein implicated in both telomere replication and chromosome end protection. We previously showed that Arabidopsis thaliana POT1a associates with the TER1 telomerase RNP, and is required for telomere length maintenance in vivo. Here we further dissect the function of POT1a and explore its interplay with the CST (CTC1/STN1/TEN1) telomere complex. Analysis of pot1a null mutants revealed that POT1a is not required for telomerase recruitment to telomeres, but is required for telomerase to maintain telomere tracts. We show that POT1a stimulates the synthesis of long telomere repeat arrays by telomerase, likely by enhancing repeat addition processivity. We demonstrate that POT1a binds STN1 and CTC1 in vitro, and further STN1 and CTC1, like POT1a, associate with enzymatically active telomerase in vivo. Unexpectedly, the in vitro interaction of STN1 with TEN1 and POT1a was mutually exclusive, indicating that POT1a and TEN1 may compete for the same binding site on STN1 in vivo. Finally, unlike CTC1 and STN1, TEN1 was not associated with active telomerase in vivo, consistent with our previous data showing that TEN1 negatively regulates telomerase enzyme activity. Altogether, our data support a two-state model in which POT1a promotes an extendable telomere state via contacts with the telomerase RNP as well as STN1 and CTC1, while TEN1 opposes these functions.

Indexed as

ArabidopsisArabidopsis ProteinsChromosomal Proteins, Non-HistoneChromosomes, PlantMultiprotein ComplexesNuclear ProteinsPlants, Genetically ModifiedTelomeraseTelomereTelomere-Binding ProteinsTelomere HomeostasisArabidopsis ProteinsChromosomal Proteins, Non-HistoneCTC1 protein, ArabidopsisMultiprotein ComplexesNuclear ProteinsPOT1A protein, ArabidopsisSTN1 protein, ArabidopsisTelomeraseTelomere-Binding ProteinsTEN1 protein, ArabidopsisTERT protein, Arabidopsis

Identifiers

PMID25329641
PMCPMC4199523
OpenAlexW2074638249

What OpenQuestion holds

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LicenceCC BY
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.