Evidence map›Paper›PMID 18625707›Full record

ArticleThe Journal of biological chemistry2008

Plk1 phosphorylation of TRF1 is essential for its binding to telomeres.

Zhao-Qiu Wu, Xiaoming Yang, Gregory Weber, Xiaoqi Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

29 citing papers in PubMed, 46 citations in OpenAlex.

  1. Review
  2. TRF1 and TRF2: pioneering targets in telomere-based cancer therapy.Journal of cancer research and clinical oncology · 2024
    Review
  3. Article
  4. Article
  5. The Connection Between Cell Fate and Telomere.Advances in experimental medicine and biology · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Chromatin structure in telomere dynamics.Frontiers in oncology · 2013
    Article
  17. Article
  18. 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

4 authors at 2 institutions in 2 countries.

Zhao-Qiu WuDepartment of Biochemistry and the Cancer Center, Purdue University, West Lafayette, Indiana 47907.
Xiaoming YangCollege of Chemistry, Sichuan University, Chengdu 610064, China.
Gregory WeberDepartment of Biochemistry and the Cancer Center, Purdue University, West Lafayette, Indiana 47907.
Xiaoqi LiuDepartment of Biochemistry and the Cancer Center, Purdue University, West Lafayette, Indiana 47907. Electronic address: liu8@purdue.edu.
Purdue University West Lafayette · USSichuan University · CN

Funding

Functional studies of Plk1 and its interacting proteinsK01CA114401 · NCI · PURDUE UNIVERSITY · PI LIU, XIAOQI · 2005 to 2009
$747k
NCI NIH HHS K01 CA 114401NCI NIH HHS K01 CA114401
6 · The paper itself

Abstract

In a search for Polo-like kinase 1 (Plk1) interaction proteins, we have identified TRF1 (telomeric repeat binding factor 1) as a potential Plk1 target. In this communication we report further characterization of the interaction. We show that Plk1 associates with TRF1, and Plk1 phosphorylates TRF1 at Ser-435 in vivo. Moreover, Cdk1, serving as a priming kinase, phosphorylates TRF1 to generate a docking site for Plk1 toward TRF1. In the presence of nocodazole, ectopic expression of wild type TRF1 but not TRF1 with alanine mutation in the Plk1 phosphorylation site induces apoptosis in cells containing short telomeres but not in cells containing long telomeres. Unexpectedly, down-regulation of TRF1 by RNA interference affects cell proliferation and results in obvious apoptosis in cells with short telomeres but not in cells with long telomeres. Importantly, we observe that telomeric DNA binding ability of TRF1 is cell cycle-regulated and reaches a peak during mitosis. Upon phosphorylation by Plk1 in vivo and in vitro, the ability of TRF1 to bind telomeric DNA is dramatically increased. These results demonstrate that Plk1 interacts with and phosphorylates TRF1 and suggest that Plk1-mediated phosphorylation is involved in both TRF1 overexpression-induced apoptosis and its telomeric DNA binding ability.

Indexed as

ApoptosisCell CycleCell Cycle ProteinsDNAHeLa CellsHumansMitosisModels, BiologicalPhosphorylationPlasmidsPolo-Like Kinase 1Protein BindingProtein Serine-Threonine KinasesProto-Oncogene ProteinsRNA InterferenceTelomereCell Cycle ProteinsDNAPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsTelomeric Repeat Binding Protein 1

Identifiers

PMID18625707
PMCPMC2533076
OpenAlexW2089716206

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.