Evidence map›Paper›PMID 25154416›Full record

ArticleMolecular and cellular biology2014

14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation.

Ashraf Dar, David Wu, Nicholas Lee, Etsuko Shibata, Anindya Dutta

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

31 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. 14-3-3ζ suppresses RANKL signaling by destabilizing TRAF6.The Journal of biological chemistry · 2024
    Article
  7. Article
  8. Review
  9. [NKD1 promotes glucose uptake in colon cancer cells by activating YWHAE transcription].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. NOTCH1 regulates the viability of cholangiocarcinoma cells via 14-3-3 theta.Journal of cell communication and signaling · 2019
    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.

Ashraf DarDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
David WuDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
Nicholas LeeDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
Etsuko ShibataDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA.
Anindya DuttaDepartment of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia, USA ad8q@virginia.edu.
University of Virginia · US

Funding

The role of MCM8-9 in genomic instability of cancersR01CA060499 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Anindya Dutta · 1994 to 2026
$8.6M
Effect of anti-S phase agents on human chromosomesR01CA166054 · NCI · UNIVERSITY OF VIRGINIA · PI DUTTA, ANINDYA · 2013 to 2017
$1.6M
NCI NIH HHS CA166054NCI NIH HHS CA60499NCI NIH HHS R01 CA060499NCI NIH HHS R01 CA166054
6 · The paper itself

Abstract

Cdt2 is the substrate recognition adaptor of CRL4(Cdt2) E3 ubiquitin ligase complex and plays a pivotal role in the cell cycle by mediating the proteasomal degradation of Cdt1 (DNA replication licensing factor), p21 (cyclin-dependent kinase [CDK] inhibitor), and Set8 (histone methyltransferase) in S phase. Cdt2 itself is attenuated by SCF(FbxO11)-mediated proteasomal degradation. Here, we report that 14-3-3 adaptor proteins interact with Cdt2 phosphorylated at threonine 464 (T464) and shield it from polyubiquitination and consequent proteasomal degradation. Depletion of 14-3-3 proteins promotes the interaction of FbxO11 with Cdt2. Overexpressing 14-3-3 proteins shields Cdt2 that has a phospho-mimicking mutation (T464D [change of T to D at position 464]) but not Cdt2(T464A) from ubiquitination. Furthermore, the delay of the cell cycle in the G2/M phase and decrease in cell proliferation seen upon depletion of 14-3-3γ is partly due to the accumulation of the CRL4(Cdt2) substrate, Set8 methyltransferase. Therefore, the stabilization of Cdt2 is an important function of 14-3-3 proteins in cell cycle progression.

Indexed as

14-3-3 ProteinsBinding SitesCell CycleF-Box ProteinsHalf-LifeHEK293 CellsHeLa CellsHumansNuclear ProteinsPhosphorylationProteasome Endopeptidase ComplexProtein-Arginine N-MethyltransferasesThreonineUbiquitinationUbiquitin-Protein Ligases14-3-3 ProteinsDTL protein, humanF-Box ProteinsFBXO11 protein, humanNuclear ProteinsProteasome Endopeptidase ComplexProtein-Arginine N-MethyltransferasesThreonineUbiquitin-Protein Ligases

Identifiers

PMID25154416
PMCPMC4386460
OpenAlexW2315291074

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.