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O-GlcNAc Transferase is Required to Maintain Satellite Cell Function
Stem Cells, 2021Abstract O-GlcNAcylation is a posttranslational modification considered to be a nutrient sensor that reports nutrient scarcity or surplus. Although O-GlcNAcylation exists in a wide range of cells and/or tissues, its functional role in muscle satellite cells (SCs) remains largely unknown.
Morgan D. Zumbaugh +5 more
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Localization of the O-GlcNAc transferase and O-GlcNAc-modified proteins in rat cerebellar cortex
Brain Research, 2003O-linked N-acetylglucosamine (O-GlcNAc) is a ubiquitous nucleocytoplasmic protein modification that has a complex interplay with phosphorylation on cytoskeletal proteins, signaling proteins and transcription factors. O-GlcNAc is essential for life at the single cell level, and much indirect evidence suggests it plays an important role in nerve cell ...
Yoshihiro, Akimoto +6 more
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O-GlcNAc site-mapping of liver X receptor-α and O-GlcNAc transferase
Biochemical and Biophysical Research Communications, 2018The Liver X Receptor α (LXRα) belongs to the nuclear receptor superfamily and plays an essential role in regulating cholesterol, lipid and glucose metabolism and inflammatory responses. We have previously shown that LXRα is post-translationally modified by O-linked β-N-acetyl-glucosamine (O-GlcNAc) with increased transcriptional activity.
Qiong Fan +6 more
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Biochemical and Biophysical Research Communications, 2020 O-GlcNAcylation is a post-translational modification of thousands of intracellular proteins that dynamically regulates many fundamental cellular processes. Cellular O-GlcNAcylation levels are regulated by a unique couple of enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA), which adds and removes the GlcNAc residue, respectively. Maintenance of
Steffi F Baldini, Vanessa Dehennaut
exaly +5 more sources
2002
Glycosylation of nuclear and cytoplasmic proteins by the addition of a single N- acetylglucosamine monosaccharide (O-GlcNAc) is a major posttranslational modification in higher eukaryotes (Hart 1997). O-GlcNAcylation is characterized by the addition of single GlcNAc residues from a UDP-GlcNAc sugar donor to the hydroxyl groups of serine/threonine ...
Sai Prasad N. Iyer, Gerald W. Hart
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Glycosylation of nuclear and cytoplasmic proteins by the addition of a single N- acetylglucosamine monosaccharide (O-GlcNAc) is a major posttranslational modification in higher eukaryotes (Hart 1997). O-GlcNAcylation is characterized by the addition of single GlcNAc residues from a UDP-GlcNAc sugar donor to the hydroxyl groups of serine/threonine ...
Sai Prasad N. Iyer, Gerald W. Hart
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Phosphoinositide signalling links O-GlcNAc transferase to insulin resistance
Nature, 2008Glucose flux through the hexosamine biosynthetic pathway leads to the post-translational modification of cytoplasmic and nuclear proteins by O-linked beta-N-acetylglucosamine (O-GlcNAc). This tandem system serves as a nutrient sensor to couple systemic metabolic status to cellular regulation of signal transduction, transcription, and protein ...
Xiaoyong, Yang +10 more
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Virtual Screening of Human O-GlcNAc Transferase Inhibitors
Chinese Journal of Chemical Physics, 2016O-GlcNAc transferase (OGT) is one of essential mammalian enzymes, which catalyze the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine (UDP-GlcNAc) to hydroxyl groups of serines and threonines (Ser/Thr) in proteins. Dysregulations of cellular O-GlcNAc have been implicated in diabetes, neurodegenerative disease, and cancer, which brings great
Qingtong Zhou, Eugene I Shakhnovich
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Regulation of ACSS2 by O-GlcNAc Transferase in Glioblastoma Cells
2021O-GlcNAcylation plays an important role in the regulation of various signaling pathways and diseases such as cancer. Many cancers contain elevated O-GlcNAc levels, owed to an increase in O-GlcNAc Transferase (OGT), the enzyme that adds this sugar moiety to proteins.
Michael Smith, Mauricio Reginato
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Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation
Nature Structural & Molecular Biology, 2008N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous ...
Carlos, Martinez-Fleites +5 more
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