Evidence map›Paper›PMID 34850123›Full record

ArticleNucleic acids research2021

TRF2 promotes dynamic and stepwise looping of POT1 bound telomeric overhang.

Tapas Paul, Wilson Liou, Xinyi Cai, Patricia L Opresko, Sua Myong

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.6field-weighted citation impact, top 18% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Emerging accessibility patterns in long telomeric overhangs.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. 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

5 authors at 2 institutions in 1 country.

Tapas PaulDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Wilson LiouDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Xinyi CaiDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
Patricia L OpreskoDepartment of Environmental and Occupational Health, University of Pittsburgh, Hillman Cancer Center, 5117 Centre Avenue, Suite 2.6a, Pittsburgh, PA 15213, USA.
Sua MyongDepartment of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.ORCID 0000-0001-9098-3423
Johns Hopkins University · USUPMC Hillman Cancer Center · US

Funding

Supplement to Promote DiversityR35ES030396 · NIEHS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Patricia L Opresko · 2019 to 2026
$7.5M
Roles of Telomeric Oxidative DNA Lesions in Telomere Length RegulationR01CA207342 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Sua Myong, Patricia L Opresko · 2017 to 2026
$3.7M
Quantitative Analysis of G-Quadruplex Folding and its Role in Gene ExpressionR01GM115631 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI MYONG, SUA · 2016 to 2019
$1.2M
NCI NIH HHS R01 CA207342NIEHS NIH HHS R35 ES030396NIGMS NIH HHS R01 GM115631
6 · The paper itself

Abstract

Human telomeres are protected by shelterin proteins, but how telomeres maintain a dynamic structure remains elusive. Here, we report an unexpected activity of POT1 in imparting conformational dynamics of the telomere overhang, even at a monomer level. Strikingly, such POT1-induced overhang dynamics is greatly enhanced when TRF2 engages with the telomere duplex. Interestingly, TRF2, but not TRF2ΔB, recruits POT1-bound overhangs to the telomere ds/ss junction and induces a discrete stepwise movement up and down the axis of telomere duplex. The same steps are observed regardless of the length of the POT1-bound overhang, suggesting a tightly regulated conformational dynamic coordinated by TRF2 and POT1. TPP1 and TIN2 which physically connect POT1 and TRF2 act to generate a smooth movement along the axis of the telomere duplex. Our results suggest a plausible mechanism wherein telomeres maintain a dynamic structure orchestrated by shelterin.

Indexed as

Fluorescence Resonance Energy TransferFluorescent DyesHumansMicroscopy, FluorescenceProtein BindingRecombinant ProteinsShelterin ComplexTelomereTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2Tripeptidyl-Peptidase 1Fluorescent DyesPOT1 protein, humanRecombinant ProteinsShelterin ComplexTelomere-Binding ProteinsTelomeric Repeat Binding Protein 2TERF2 protein, humanTINF2 protein, humanTripeptidyl-Peptidase 1

Identifiers

PMID34850123
PMCPMC8643667
OpenAlexW3118560148

What OpenQuestion holds

Textmetadata
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.