Evidence map›Paper›PMID 24828503›Full record

ArticleThe Journal of biological chemistry2014

SCF-FBXO31 E3 ligase targets DNA replication factor Cdt1 for proteolysis in the G2 phase of cell cycle to prevent re-replication.

Pegah Johansson, Jessie Jeffery, Fares Al-Ejeh, Renèe B Schulz, David F Callen, Raman Kumar, Kum Kum Khanna

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-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

34 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  6. ISGylation of NF-κBp65 by SCFArteriosclerosis, thrombosis, and vascular biology · 2023
    Article
  7. Article
  8. Review
  9. Article
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  12. Review
  13. Review
  14. Article
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  16. Article
  17. The SCFThe Journal of biological chemistry · 2018
    Article
  18. Review
  19. Review
  20. Degradation of FBXO31 by APC/C is regulated by AKT- and ATM-mediated phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

7 authors at 2 institutions in 1 country.

Pegah JohanssonFrom the Sahlgrenska University Hospital, Department of Clinical Chemistry, Bruna Stråket 16, 41345 Gothenburg, Sweden.
Jessie JefferySignal Transduction Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland 4006, Australia.
Fares Al-EjehSignal Transduction Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland 4006, Australia.
Renèe B SchulzCentre for Personalised Cancer Medicine and Discipline of Medicine, University of Adelaide, Adelaide, South Australia 5000, Australia.
David F CallenCentre for Personalised Cancer Medicine and Discipline of Medicine, University of Adelaide, Adelaide, South Australia 5000, Australia.
Raman KumarSchool of Paediatrics and Reproductive Health and Discipline of Medicine, University of Adelaide, Adelaide and Women's and Children's Health Research Institute, North Adelaide, South Australia 5006, Australia, and raman.sharma@adelaide.edu.au.
Kum Kum KhannaSignal Transduction Laboratory, QIMR Berghofer Medical Research Institute, Brisbane, Queensland 4006, Australia KumKum.Khanna@qimrberghofer.edu.au.
QIMR Berghofer Medical Research Institute · AUUniversity of Adelaide · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

FBXO31 was originally identified as a putative tumor suppressor gene in breast, ovarian, hepatocellular, and prostate cancers. By screening a set of cell cycle-regulated proteins as potential FBXO31 interaction partners, we have now identified Cdt1 as a novel substrate. Cdt1 DNA replication licensing factor is part of the pre-replication complex and essential for the maintenance of genomic integrity. We show that FBXO31 specifically interacts with Cdt1 and regulates its abundance by ubiquitylation leading to subsequent degradation. We also show that Cdt1 regulation by FBXO31 is limited to the G2 phase of the cell cycle and is independent of the pathways previously described for Cdt1 proteolysis in S and G2 phase. FBXO31 targeting of Cdt1 is mediated through the N terminus of Cdt1, a region previously shown to be responsible for its cell cycle regulation. Finally, we show that Cdt1 stabilization due to FBXO31 depletion results in re-replication. Our data present an additional pathway that contributes to the FBXO31 function as a tumor suppressor.

Indexed as

DNA ReplicationCell CycleCell Cycle ProteinsF-Box ProteinsG2 PhaseHumansProtein BindingProteolysisTumor Suppressor ProteinsUbiquitinationCDT1 protein, humanCell Cycle ProteinsF-Box ProteinsFBXO31 protein, humanTumor Suppressor ProteinsCdt1Cell CycleDNA ReplicationE3 Ubiquitin LigaseFBXO31Genomic InstabilityProtein Degradation

Identifiers

PMID24828503
PMCPMC4140253
OpenAlexW2027182048

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.