A little sugar goes a long way: the cell biology of O-GlcNAc

MR Bond, JA Hanover - Journal of Cell Biology, 2015 - rupress.org
MR Bond, JA Hanover
Journal of Cell Biology, 2015rupress.org
Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine
(O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is
important for disease-relevant signaling and enzyme regulation. O-GlcNAcylation requires
uridine diphosphate–GlcNAc, a precursor responsive to nutrient status and other
environmental cues. Alternative splicing of the genes encoding the O-GlcNAc cycling
enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) yields isoforms targeted to …
Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine (O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is important for disease-relevant signaling and enzyme regulation. O-GlcNAcylation requires uridine diphosphate–GlcNAc, a precursor responsive to nutrient status and other environmental cues. Alternative splicing of the genes encoding the O-GlcNAc cycling enzymes O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) yields isoforms targeted to discrete sites in the nucleus, cytoplasm, and mitochondria. OGT and OGA also partner with cellular effectors and act in tandem with other posttranslational modifications. The enzymes of O-GlcNAc cycling act preferentially on intrinsically disordered domains of target proteins impacting transcription, metabolism, apoptosis, organelle biogenesis, and transport.
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