Evidence map›Paper›PMID 26075789›Full record

ArticleEpigenetics2015

Undetectable histone O-GlcNAcylation in mammalian cells.

Jessica Gagnon, Salima Daou, Natalia Zamorano, Nicholas V G Iannantuono, Ian Hammond-Martel, Nazar Mashtalir, Eric Bonneil, Hugo Wurtele, Pierre Thibault, El Bachir Affar

Open access · bronzeAbstract read
In one paragraph

Article in Epigenetics, 2015. 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
2.0field-weighted citation impact, top 14% 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, 33 citations in OpenAlex.

  1. Review
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  12. Role ofPhysiological reviews · 2021
    Review
  13. Frontiers in genetics · 2020
    Review
  14. Review
  15. Article
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  17. 'Molecules (Basel, Switzerland) · 2018
    Review
  18. Molecules (Basel, Switzerland) · 2018
    Article
  19. Review
  20. The sweet side of the cell cycle.Biochemical Society transactions · 2017
    Review
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 2 institutions in 1 country.

Jessica Gagnona Maisonneuve-Rosemont Hospital Research Center and Department of Medicine; University of Montréal ; Montréal, Québec , Canada.
Salima Daou
Natalia Zamorano
Nicholas V G Iannantuono
Ian Hammond-Martel
Nazar Mashtalir
Eric Bonneil
Hugo Wurtele
Pierre Thibault
El Bachir Affar
Hôpital Maisonneuve-Rosemont · CAInstitute for Research in Immunology and Cancer · CA

Funding

Canadian Institutes of Health Research MOP-115132
6 · The paper itself

Abstract

O-GlcNAcylation is a posttranslational modification catalyzed by the O-Linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and reversed by O-GlcNAcase (OGA). Numerous transcriptional regulators, including chromatin modifying enzymes, transcription factors, and co-factors, are targeted by O-GlcNAcylation, indicating that this modification is central for chromatin-associated processes. Recently, OGT-mediated O-GlcNAcylation was reported to be a novel histone modification, suggesting a potential role in directly coordinating chromatin structure and function. In contrast, using multiple biochemical approaches, we report here that histone O-GlcNAcylation is undetectable in mammalian cells. Conversely, O-GlcNAcylation of the transcription regulators Host Cell Factor-1 (HCF-1) and Ten-Eleven Translocation protein 2 (TET2) could be readily observed. Our study raises questions on the occurrence and abundance of O-GlcNAcylation as a histone modification in mammalian cells and reveals technical complications regarding the detection of genuine protein O-GlcNAcylation. Therefore, the identification of the specific contexts in which histone O-GlcNAcylation might occur is still to be established.

Indexed as

Epigenesis, GeneticAcylationAnimalsbeta-N-AcetylhexosaminidasesChromatinDioxygenasesDNA-Binding ProteinsGlycosylationHEK293 CellsHistonesHost Cell Factor C1HumansN-AcetylglucosaminyltransferasesProtein Processing, Post-TranslationalProto-Oncogene Proteinsbeta-N-AcetylhexosaminidasesChromatinDioxygenasesDNA-Binding ProteinsHCFC1 protein, humanhexosaminidase CHistonesHost Cell Factor C1N-AcetylglucosaminyltransferasesProto-Oncogene ProteinsTET2 protein, humanUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferaseChromatinEpigeneticsH2B K120ub, Histone H2B lysine 120 monoubiquitinationH2B S112 O-GlcNAc, Histone H2B serine 112 O-GlcNAcHCF-1HCF-1, Host Cell Factor-1HistoneOGA, O-GlcNAcaseO-GlcNAcO-GlcNAc, O-Linked N-acetylglucosamineO-GlcNAcylationOGTOGT, O-Linked N-acetylglucosamine transferasePolycombposttranslational modificationPUGNAc, O-(2-acetamido-2-deoxyglucopyranosylidene) amino N-phenylcarbamateTET2TET2, Ten-Eleven Translocation protein 2UDP-GlcNAc, Uridine Diphosphate N-AcetylglucosamineWGA, Wheat Germ Agglutinin.

Identifiers

PMID26075789
PMCPMC4622518
OpenAlexW1571273830

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.