Evidence map›Paper›PMID 24619417›Full record

ArticleThe Journal of biological chemistry2014

Epigenetic regulation of a brain-specific glycosyltransferase N-acetylglucosaminyltransferase-IX (GnT-IX) by specific chromatin modifiers.

Yasuhiko Kizuka, Shinobu Kitazume, Kyohei Okahara, Alejandro Villagra, Eduardo M Sotomayor, Naoyuki Taniguchi

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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Aberrant Protein Glycosylation in Brain Cancers, with Emphasis on Glioblastoma.Advances in experimental medicine and biology · 2022
    Article
  7. Epigenetic Regulation of Glycosylation in Cancer and Other Diseases.International journal of molecular sciences · 2021
    Review
  8. Epigenetics of Immunoglobulin G Glycosylation.Experientia supplementum (2012) · 2021
    Article
  9. Epigenetic Regulation of Glycosylation.Advances in experimental medicine and biology · 2021
    Article
  10. 3D Structure and Function of Glycosyltransferases Involved inInternational journal of molecular sciences · 2020
    Review
  11. Article
  12. Metabolism in pluripotency: Both driver and passenger?The Journal of biological chemistry · 2019
    Review
  13. Effects of Acute Cold Stress on LiverInternational journal of molecular sciences · 2018
    Article
  14. Review
  15. Article
  16. The Inhibitory Role of α2,6-Sialylation in Adipogenesis.The Journal of biological chemistry · 2017
    Article
  17. Review
  18. Review
  19. Neurological aspects of human glycosylation disorders.Annual review of neuroscience · 2015
    Review
  20. 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

6 authors at 2 institutions in 2 countries.

Yasuhiko KizukaDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Global Research Cluster, RIKEN, Wako 351-0198, Japan and.
Shinobu KitazumeDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Global Research Cluster, RIKEN, Wako 351-0198, Japan and.
Kyohei OkaharaDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Global Research Cluster, RIKEN, Wako 351-0198, Japan and.
Alejandro VillagraDepartment of Immunology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33613.
Eduardo M SotomayorDepartment of Immunology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, Florida 33613.
Naoyuki TaniguchiDisease Glycomics Team, Systems Glycobiology Research Group, RIKEN-Max Planck Joint Research Center for Systems Chemical Biology, Global Research Cluster, RIKEN, Wako 351-0198, Japan and. Electronic address: tani52@wd5.so-net.ne.jp.
RIKEN · JPMoffitt Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of glycosyltransferase genes is essential for glycosylation. However, the detailed mechanisms of how glycosyltransferase gene expression is regulated in a specific tissue or during disease progression are poorly understood. In particular, epigenetic studies of glycosyltransferase genes are limited, although epigenetic mechanisms, such as histone and DNA modifications, are central to establish tissue-specific gene expression. We previously found that epigenetic histone activation is essential for brain-specific expression of N-acetylglucosaminyltransferase-IX (GnT-IX, also designated GnT-Vb), but the mechanism of brain-specific chromatin activation around GnT-IX gene (Mgat5b) has not been clarified. To reveal the mechanisms regulating the chromatin surrounding GnT-IX, we have investigated the epigenetic factors that are specifically involved with the mouse GnT-IX locus by comparing their involvement with other glycosyltransferase loci. We first found that a histone deacetylase (HDAC) inhibitor enhanced the expression of GnT-IX but not of other glycosyltransferases tested. By overexpression and knockdown of a series of HDACs, we found that HDAC11 silenced GnT-IX. We also identified the O-GlcNAc transferase (OGT) and ten-eleven translocation-3 (TET3) complex as a specific chromatin activator of GnT-IX gene. Moreover, chromatin immunoprecipitation (ChIP) analysis in combination with OGT or TET3 knockdown showed that this OGT-TET3 complex facilitates the binding of a potent transactivator, NeuroD1, to the GnT-IX promoter, suggesting that epigenetic chromatin activation by the OGT-TET3 complex is a prerequisite for the efficient binding of NeuroD1. These results reveal a new epigenetic mechanism of brain-specific GnT-IX expression regulated by defined chromatin modifiers, providing new insights into the tissue-specific expression of glycosyltransferases.

Indexed as

AnimalsBasic Helix-Loop-Helix ProteinsBrainCell LineChromatinDioxygenasesDNA-Binding ProteinsEpigenesis, GeneticGene Expression Regulation, EnzymologicGene Knockdown TechniquesHistone Deacetylase InhibitorsMiceN-AcetylglucosaminyltransferasesNerve Tissue ProteinsOrgan SpecificityProto-Oncogene ProteinsBasic Helix-Loop-Helix ProteinsChromatinDioxygenasesDNA-Binding ProteinsHistone Deacetylase InhibitorsN-acetylglucosaminyltransferase IX, mouseN-AcetylglucosaminyltransferasesNerve Tissue ProteinsNeurod1 protein, mouseProto-Oncogene ProteinsTet3 protein, mouseEpigeneticsGlycobiologyGlycosyltransferasesGnT-IXHistone DeacetylaseNeuroD1O-GlcNAcTET3Transcription

Identifiers

PMID24619417
PMCPMC4036263
OpenAlexW1984167696

What OpenQuestion holds

Textmetadata
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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.