Evidence map›Paper›PMID 27217568›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

O-linked N-acetylglucosamine transferase (OGT) interacts with the histone chaperone HIRA complex and regulates nucleosome assembly and cellular senescence.

Jong-Sun Lee, Zhiguo Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.8field-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

26 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  8. Article
  9. Review
  10. The O-GlcNAc dichotomy: when does adaptation become pathological?Clinical science (London, England : 1979) · 2023
    Review
  11. Article
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  16. Article
  17. Metabolic Stress and Cardiovascular Disease in Diabetes Mellitus: The Role of ProteinArteriosclerosis, thrombosis, and vascular biology · 2019
    Review
  18. Pak2 kinase promotes cellular senescence and organismal aging.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. 'Molecules (Basel, Switzerland) · 2018
    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

2 authors at 2 institutions in 1 country.

Jong-Sun LeeMayo Graduate School, Biochemistry and Molecular Biology Track, Mayo Clinic College of Medicine, Rochester, MN 55905;
Zhiguo ZhangMayo Graduate School, Biochemistry and Molecular Biology Track, Mayo Clinic College of Medicine, Rochester, MN 55905; Epigenomics Developmental Program, Center for Individualized Medicine, Mayo Clinic College of Medicine, Rochester, MN 55905 zhang.zhiguo@mayo.edu.
Mayo Clinic · USMayo Clinic in Arizona · US

Funding

The role of a histone H4 phosphorylation in drug resistanceR01CA157489 · NCI · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA157489
6 · The paper itself

Abstract

The histone chaperone HIRA complex, consisting of histone cell cycle regulator (HIRA), Ubinuclein1 (UBN1), and calcineurin binding protein 1 (CABIN1), deposits histone variant H3.3 to genic regions and regulates gene expression in various cellular processes, including cellular senescence. How HIRA-mediated nucleosome assembly of H3.3-H4 is regulated remains not well understood. Here, we show that O-linked N-acetylglucosamine (GlcNAc) transferase (OGT), an enzyme that catalyzes O-GlcNAcylation of serine or threonine residues, interacts with UBN1, modifies HIRA, and promotes nucleosome assembly of H3.3. Depletion of OGT or expression of the HIRA S231A O-GlcNAcylation-deficient mutant compromises formation of the HIRA-H3.3 complex and H3.3 nucleosome assembly. Importantly, OGT depletion or expression of the HIRA S231A mutant delays premature cellular senescence in primary human fibroblasts, whereas overexpression of OGT accelerates senescence. Taken together, these results support a model in which OGT modifies HIRA to regulate HIRA-H3.3 complex formation and H3.3 nucleosome assembly and reveal the mechanism by which OGT functions in cellular senescence.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsCellular SenescenceHEK293 CellsHistone ChaperonesHistonesHumansN-AcetylglucosaminyltransferasesNuclear ProteinsNucleosomesProtein BindingProtein DomainsTranscription FactorsAdaptor Proteins, Signal TransducingCABIN1 protein, humanCell Cycle ProteinsHIRA protein, humanHistone ChaperonesHistonesN-AcetylglucosaminyltransferasesNuclear ProteinsNucleosomesTranscription FactorsUBN1 protein, humanUDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferasecellular senescenceHIRAhistone H3.3nucleosome assemblyOGT

Identifiers

PMID27217568
PMCPMC4988580
OpenAlexW2395389823

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.