ReviewThe Journal of biological chemistry2025
Understanding O-GlcNAc transferase (OGT): Every amino acid matters.
Review in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
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.
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Who cites it
4 citing papers in PubMed.
- O-GlcNAc transferase governs spermatogenic mitotic-to-meiotic transition and progression by coordinating transcription and alternative splicing programs.Cellular & molecular biology letters · 2026Article
- Starvation-induced HSC70 O-GlcNAcylation activates chaperone-mediated autophagy.The Journal of biological chemistry · 2026Article
- Serum Starvation Promotes the Proteolysis of OGT by Activating AMPK and the CUL1/SKP1/SKP2 E3 Ubiquitin Ligase in 3T3-L1 Cells.Biomolecules & therapeutics · 2026Article
- Deciphering O‑GlcNAc-Dependent Signaling Via Integrated Proteomics and Phosphoproteomics.ACS omega · 2026Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) mediate all the "writing" and "erasing" of intracellular O-GlcNAc modification events on the serine or threonine residues of proteins. Decades of investigations have revealed many O-GlcNAc substrates, spanning almost all areas of biological research. The question remains, however: why is there only one OGT? Here, we provide a tentative answer to the "one OGT" question. We propose that OGT is a sensor of various biological stimuli and responds accordingly by incurring post-translational modifications (PTMs) or through its short linear motifs (SLiMs). Both PTMs and SLiMs reside in its intrinsic disordered regions, tetratricopeptide repeats, or catalytic domains and contribute to altering its enzymatic activity, protein-protein interaction, subcellular localization, and protein stability. OGA follows the same pattern, although to a lesser extent. We propose that OGT, or OGA, can sense biological cues and, via its PTMs or SLiMs, adjust the downstream OGT interactome and O-GlcNAcome correspondingly.
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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.