ReviewChromosoma2015
A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin.
Review in Chromosoma, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
What it found
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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.
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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.
Who cites it
30 citing papers in PubMed, 51 citations in OpenAlex.
- OGT prevents DNA demethylation and suppresses the expression of transposable elements in heterochromatin by restraining TET activity genome-wide.Nature structural & molecular biology · 2025Article
- Perturbing nuclear glycosylation in the mouse preimplantation embryo slows down embryonic development.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Functional genomic profiling of O-GlcNAc reveals its context-specific interplay with RNA polymerase II.Genome biology · 2025Article
- Genetic gradual reduction of OGT activity unveils the essential role of O-GlcNAc in the mouse embryo.PLoS genetics · 2025Article
- A role for β-1,6- and β-1,3-glucans in kinetochore function in Saccharomyces cerevisiae.Genetics · 2024Article
- O-GlcNAcylation: the sweet side of epigenetics.Epigenetics & chromatin · 2023Review
- Nutrigenomic regulation of sensory plasticity.eLife · 2023Article
- Roles of ten-eleven translocation family proteins and their O-linked β-N-acetylglucosaminylated forms in cancer development.Oncology letters · 2021Review
- Conversion of Germ Cells to Somatic Cell Types inJournal of developmental biology · 2020Review
- Methylation-directed glycosylation of chromatin factors represses retrotransposon promoters.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Engineering a Proximity-Directed O-GlcNAc Transferase for Selective Protein O-GlcNAcylation in Cells.ACS chemical biology · 2020Article
- Review
- Biosynthesis ofThe Journal of biological chemistry · 2019Article
- Article
- Article
- Proteomic analysis of the OGT interactome: novel links to epithelial-mesenchymal transition and metastasis of cervical cancer.Carcinogenesis · 2018Article
- Regulation of chromatin and gene expression by metabolic enzymes and metabolites.Nature reviews. Molecular cell biology · 2018Review
- 'Molecules (Basel, Switzerland) · 2018Review
- O-GlcNAcylation modulates Bmi-1 protein stability and potential oncogenic function in prostate cancer.Oncogene · 2017Article
- H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.Epigenetics & chromatin · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-linked β-N-Acetylglucosamine (O-GlcNAc) is a posttranslational modification that is catalyzed by O-GlcNAc transferase (Ogt) and found on a plethora of nuclear and cytosolic proteins in animals and plants. Studies in different model organisms revealed that while O-GlcNAc is required for selected processes in Caenorhabditis elegans and Drosophila, it has evolved to become required for cell viability in mice, and this has challenged investigations to identify cellular functions that critically require this modification in mammals. Nevertheless, a principal cellular process that engages O-GlcNAcylation in all of these species is the regulation of gene transcription. Here, we revisit several of the primary experimental observations that led to current models of how O-GlcNAcylation affects gene expression. In particular, we discuss the role of the stable association of Ogt with the transcription factors Hcf1 and Tet, the two main Ogt-interacting proteins in nuclei of mammalian cells. We also critically evaluate the evidence that specific residues on core histones, including serine 112 of histone 2B (H2B-S112), are O-GlcNAcylated in vivo and discuss possible physiological effects of these modifications. Finally, we review our understanding of the role of O-GlcNAcylation in Drosophila, where recent studies suggest that the developmental defects in Ogt mutants are all caused by lack of O-GlcNAcylation of a single transcriptional regulator, the Polycomb repressor protein Polyhomeotic (Ph). Collectively, this reexamination of the experimental evidence suggests that a number of recently propagated models about the role of O-GlcNAcylation in transcriptional control should be treated cautiously.
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Registered trials
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.