Evidence map›Paper›PMID 22918237›Full record

ArticleCell cycle (Georgetown, Tex.)2012

4E-BP1 participates in maintaining spindle integrity and genomic stability via interacting with PLK1.

Zeng-Fu Shang, Lan Yu, Bing Li, Wen-Zhi Tu, Yu Wang, Xiao-Dan Liu, Hua Guan, Bo Huang, Wei-Qing Rang, Ping-Kun Zhou

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-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

24 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Regulation of 4E-BP1 activity in the mammalian oocyte.Cell cycle (Georgetown, Tex.) · 2017
    Article
  11. Article
  12. Translation regulator ballet in meiotic spindle.Cell cycle (Georgetown, Tex.) · 2017
    Article
  13. A researcher's guide to the galaxy of IRESs.Cellular and molecular life sciences : CMLS · 2017
    Review
  14. Article
  15. Article
  16. Mitotic protein kinase CDK1 phosphorylation of mRNA translation regulator 4E-BP1 Ser83 may contribute to cell transformation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Review
  18. Article
  19. CDK1 substitutes for mTOR kinase to activate mitotic cap-dependent protein translation.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

10 authors at 4 institutions in 2 countries.

Zeng-Fu ShangDepartment of Radiation Toxicology and Oncology, Beijing Institute of Radiation Medicine, Beijing, PR China.
Lan Yu
Bing Li
Wen-Zhi Tu
Yu Wang
Xiao-Dan Liu
Hua Guan
Bo Huang
Wei-Qing Rang
Ping-Kun Zhou
Beijing Radiation Center · CNBeijing Administration Institute · CNUniversity of South China · CNThe University of Texas Southwestern Medical Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The essential function of eIF4E-binding protein 1 (4E-BP1) in translation initiation has been well established; however, the role of 4E-BP1 in normal cell cycle progression is coming to attention. Here, we revealed the role of 4E-BP1 on mitotic regulation and chromosomal DNA dynamics during mitosis. First, we have observed the co-localization of the phosphorylated 4E-BP1 at T37/46 with Polo-like kinase 1 (PLK1) at the centrosomes during. Depression of 4E-BP1 by small interfering RNA in HepG2 or HeLa cells resulted in an increased outcome of polyploidy and aberrant mitosis, including chromosomal DNA misaligned and multi-polar spindles or multiple centrosomes. We observed that 4E-BP1 interacted with PLK1 directly in vitro and in vivo in mitotic cells, and the C-terminal aa 77-118 of 4E-BP1 mediates its interaction with PLK1. PLK1 can phosphorylate 4E-BP1 in vitro. Furthermore, the depletion of 4E-BP1 sensitized HepG2 and HeLa cells to the microtubule disruption agent paclitaxel. These results demonstrate that 4E-BP1, beyond its role in translation regulation, can function as a regulator of mitosis via interacting with PLK1, and possibly plays a role in genomic stability maintaining.

Indexed as

Genomic InstabilityAdaptor Proteins, Signal TransducingCell Cycle ProteinsCentrosomeChromosomes, HumanDNA, NeoplasmDrug Screening Assays, AntitumorHeLa CellsHep G2 CellsHumansMitosisPaclitaxelPhosphoproteinsPhosphorylationPolo-Like Kinase 1PolyploidyAdaptor Proteins, Signal TransducingCell Cycle ProteinsDNA, NeoplasmEIF4EBP1 protein, humanPaclitaxelPhosphoproteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene Proteins

Identifiers

PMID22918237
PMCPMC3466556
OpenAlexW2137808177

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.