Evidence map›Paper›PMID 22045740›Full record

ArticleJournal of cell science2011

Nucleostemin inhibits TRF1 dimerization and shortens its dynamic association with the telomere.

Lingjun Meng, Joseph K Hsu, Qubo Zhu, Tao Lin, Robert Y L Tsai

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Observational
  9. Telomere length and telomerase activity during folliculogenesis in mammals.The Journal of reproduction and development · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Stressing on the nucleolus in cardiovascular disease.Biochimica et biophysica acta · 2014
    Review
  14. Article
  15. 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 1 institution in 1 country.

Lingjun MengInstitute of Biosciences and Technology, Texas A&M Health Science Center, Houston, Texas 77030, USA.
Joseph K Hsu
Qubo Zhu
Tao Lin
Robert Y L Tsai
Texas A&M Health Science Center · US

Funding

Stem-like Cancer Cells in Breast TumorigenesisR01CA113750 · NCI · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI TSAI, ROBERT Y · 2005 to 2009
$1.2M
NCI NIH HHS R01 CA113750
6 · The paper itself

Abstract

TRF1 is a key component of the telomere-capping complex and binds double-strand telomeric DNA as homodimers. So far, it is not clear whether TRF1 dimerization coincides with its telomere binding or is actively controlled before it binds the telomere, and in the latter case, how this event might affect its telomere association. We previously found that TRF1 dimerization and its telomere binding can be increased by GNL3L, which is the vertebrate paralogue of nucleostemin (NS). Here, we show that NS and GNL3L bind TRF1 directly but competitively through two separate domains of TRF1. In contrast to GNL3L, NS prevents TRF1 dimerization through a mechanism not determined by its ability to displace TRF1-bound GNL3L. Furthermore, NS is capable of shortening the dynamic association of TRF1 with the telomere in normal and TRF2(ΔBΔM)-induced telomere-damaged cells without affecting the amount of telomere-bound TRF1 proteins in vivo. Importantly, NS displays a protective function against the formation of telomere-dysfunction-induced foci. This work demonstrates that TRF1 dimerization is actively and oppositely regulated by NS and GNL3L extrachromosomally. Changing the relative amount of TRF1 monomers versus dimers in the nucleoplasm might affect the dynamic association of TRF1 with the telomere and the repair of damaged telomeres.

Indexed as

Cell LineDimerizationGTP-Binding ProteinsHumansNuclear ProteinsProtein BindingProtein Structure, TertiaryTelomereTelomeric Repeat Binding Protein 1GNL3L protein, humanGNL3 protein, humanGTP-Binding ProteinsNuclear ProteinsTelomeric Repeat Binding Protein 1

Identifiers

PMID22045740
PMCPMC3215579
OpenAlexW2120511257

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.