Evidence map›Paper›PMID 27296872›Full record

ArticleMolecular oncology2016

USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication.

Santiago Hernández-Pérez, Elisa Cabrera, Hugo Amoedo, Sara Rodríguez-Acebes, Stephane Koundrioukoff, Michelle Debatisse, Juan Méndez, Raimundo Freire

Open access · bronzeAbstract read
In one paragraph

Article in Molecular oncology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

30 citing papers in PubMed, 46 citations in OpenAlex.

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  15. Coordinating DNA Replication and Mitosis through Ubiquitin/SUMO and CDK1.International journal of molecular sciences · 2021
    Review
  16. Article
  17. Review
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  19. Article
  20. USP37 promotes deubiquitination of HIF2α in kidney cancer.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

8 authors at 3 institutions in 3 countries.

Santiago Hernández-PérezUnidad de Investigación, Hospital Universitario de Canarias, Instituto de Tecnologías Biomédicas, Ofra s/n, La Laguna, Tenerife, Spain.
Elisa CabreraUnidad de Investigación, Hospital Universitario de Canarias, Instituto de Tecnologías Biomédicas, Ofra s/n, La Laguna, Tenerife, Spain.
Hugo AmoedoUnidad de Investigación, Hospital Universitario de Canarias, Instituto de Tecnologías Biomédicas, Ofra s/n, La Laguna, Tenerife, Spain.
Sara Rodríguez-AcebesDNA Replication Group, Spanish National Cancer Research Centre (CNIO), E-28029 Madrid, Spain.
Stephane KoundrioukoffInstitut Gustave Roussy, 94805 Villejuif, France; Sorbonne Universités, UPMC Univ Paris 06, F-75005 Paris, France; CNRS - UMR 8200, 94805 Villejuif, France.
Michelle DebatisseInstitut Gustave Roussy, 94805 Villejuif, France; Sorbonne Universités, UPMC Univ Paris 06, F-75005 Paris, France; CNRS - UMR 8200, 94805 Villejuif, France.
Juan MéndezDNA Replication Group, Spanish National Cancer Research Centre (CNIO), E-28029 Madrid, Spain.
Raimundo FreireUnidad de Investigación, Hospital Universitario de Canarias, Instituto de Tecnologías Biomédicas, Ofra s/n, La Laguna, Tenerife, Spain. Electronic address: rfreire@ull.edu.es.
Hospital Universitario de Canarias · ESCentre National de la Recherche Scientifique · FRSpanish National Cancer Research Centre · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA replication control is a key process in maintaining genomic integrity. Monitoring DNA replication initiation is particularly important as it needs to be coordinated with other cellular events and should occur only once per cell cycle. Crucial players in the initiation of DNA replication are the ORC protein complex, marking the origin of replication, and the Cdt1 and Cdc6 proteins, that license these origins to replicate by recruiting the MCM2-7 helicase. To accurately achieve its functions, Cdt1 is tightly regulated. Cdt1 levels are high from metaphase and during G1 and low in S/G2 phases of the cell cycle. This control is achieved, among other processes, by ubiquitination and proteasomal degradation. In an overexpression screen for Cdt1 deubiquitinating enzymes, we isolated USP37, to date the first ubiquitin hydrolase controlling Cdt1. USP37 overexpression stabilizes Cdt1, most likely a phosphorylated form of the protein. In contrast, USP37 knock down destabilizes Cdt1, predominantly during G1 and G1/S phases of the cell cycle. USP37 interacts with Cdt1 and is able to de-ubiquitinate Cdt1 in vivo and, USP37 is able to regulate the loading of MCM complexes onto the chromatin. In addition, downregulation of USP37 reduces DNA replication fork speed. Taken together, here we show that the deubiquitinase USP37 plays an important role in the regulation of DNA replication. Whether this is achieved via Cdt1, a central protein in this process, which we have shown to be stabilized by USP37, or via additional factors, remains to be tested.

Indexed as

DNA ReplicationUbiquitinationCell Cycle ProteinsCell LineEndopeptidasesG1 PhaseHumansPhosphorylationProtein BindingS PhaseCDT1 protein, humanCell Cycle ProteinsEndopeptidasesUSP37 protein, humanDNA damageDNA damage responseInitiation of DNA replicationProteasomeProtein degradationUbiquitin hydrolase

Identifiers

PMID27296872
PMCPMC5423201
OpenAlexW2419557181

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.