Evidence map›Paper›PMID 29268763›Full record

ArticleJournal of experimental & clinical cancer research : CR2017

Interaction of the epigenetic integrator UHRF1 with the MYST domain of TIP60 inside the cell.

Waseem Ashraf, Christian Bronner, Liliyana Zaayter, Tanveer Ahmad, Ludovic Richert, Mahmoud Alhosin, Abdulkhaleg Ibrahim, Ali Hamiche, Yves Mely, Marc Mousli

Abstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Mannosylated PAMAM G2 dendrimers mediated rate programmed delivery of efavirenz target HIV viral latency at reservoirs.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2024
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  9. Protein acetylation: a novel modus of obesity regulation.Journal of molecular medicine (Berlin, Germany) · 2021
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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.

Waseem AshrafLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France.
Christian BronnerInstitut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM U964 CNRS UMR 7104, Université de Strasbourg, Illkirch, France.
Liliyana ZaayterLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France.
Tanveer AhmadLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France.
Ludovic RichertLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France.
Mahmoud AlhosinDepartment of Biochemistry, Faculty of Science, King Abdulaziz University, Jeddah, Saudi Arabia.
Abdulkhaleg IbrahimInstitut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM U964 CNRS UMR 7104, Université de Strasbourg, Illkirch, France.
Ali HamicheInstitut de Génétique et de Biologie Moléculaire et Cellulaire, INSERM U964 CNRS UMR 7104, Université de Strasbourg, Illkirch, France.
Yves MelyLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France.
Marc MousliLaboratoire de Biophotonique et Pharmacologie, UMR 7213 CNRS, Faculté de Pharmacie, Université de Strasbourg, 74, Route du Rhin, 67401, Illkirch Cedex, France. marc.mousli@unistra.fr.

Funding

Agence Nationale de la Recherche ANR-10-IDEX-0002-02Agence Nationale de la Recherche ANR-10-LABX-0030-INRTAgence Nationale de la Recherche ANR-12-BS08-0003-02Fondation pour la Recherche Médicale FRM DCM20111223038
6 · The paper itself

Abstract

backgroundThe nuclear epigenetic integrator UHRF1 is known to play a key role with DNMT1 in maintaining the DNA methylation patterns during cell division. Among UHRF1 partners, TIP60 takes part in epigenetic regulations through its acetyltransferase activity. Both proteins are involved in multiple cellular functions such as chromatin remodeling, DNA damage repair and regulation of stability and activity of other proteins. The aim of this work was to investigate the interaction between UHRF1 and TIP60 in order to elucidate the dialogue between these two proteins.

methodsBiochemical (immunoprecipitation and pull-down assays) and microscopic (confocal and fluorescence lifetime imaging microscopy; FLIM) techniques were used to analyze the interaction between TIP60 and UHRF1 in vitro and in vivo. Global methylation levels were assessed by using a specific kit. The results were statistically analyzed using Graphpad prism and Origin.

resultsOur study shows that UHRF1, TIP60 and DNMT1 were found in the same epigenetic macro-molecular complex. In vitro pull-down assay showed that deletion of either the zinc finger in MYST domain or deletion of whole MYST domain from TIP60 significantly reduced its interaction with UHRF1. Confocal and FLIM microscopy showed that UHRF1 co-localized with TIP60 in the nucleus and confirmed that both proteins interacted together through the MYST domain of TIP60. Moreover, overexpression of TIP60 reduced the DNA methylation levels in HeLa cells along with downregulation of UHRF1 and DNMT1.

conclusionOur data demonstrate for the first time that TIP60 through its MYST domain directly interacts with UHRF1 which might be of high interest for the development of novel oncogenic inhibitors targeting this interaction.

Indexed as

CCAAT-Enhancer-Binding ProteinsDNA (Cytosine-5-)-Methyltransferase 1DNA MethylationEpigenesis, GeneticHeLa CellsHumansLysine Acetyltransferase 5Protein BindingProtein DomainsUbiquitin-Protein LigasesCCAAT-Enhancer-Binding ProteinsDNA (Cytosine-5-)-Methyltransferase 1DNMT1 protein, humanKAT5 protein, humanLysine Acetyltransferase 5Ubiquitin-Protein LigasesUHRF1 protein, humanCancerCell cycleEpigeneticsFluorescence lifetime imaging microscopy (FLIM)Fluorescence resonance energy transfer (FRET)Protein-protein interactionTIP60UHRF1

Identifiers

PMID29268763
PMCPMC5740878

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Registered trials

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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.