reviewAnnual Review of BiochemistryMar 3, 2011Closed access

Cross Talk Between O-GlcNAcylation and Phosphorylation: Roles in Signaling, Transcription, and Chronic Disease

Johns Hopkins University · Johns Hopkins Medicine

PubMed
Indexed incrossrefpubmed

Abstract

O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundant and cycles on proteins with a timescale similar to protein phosphorylation. O-GlcNAc occurs in organisms ranging from some bacteria to protozoans and metazoans, including plants and nematodes up the evolutionary tree to man. O-GlcNAcylation is mostly on nuclear proteins, but it occurs in all intracellular compartments, including mitochondria. Recent glycomic analyses have shown that O-GlcNAcylation has…

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Authors

4

Topics & keywords

Keywords
  • Phosphorylation
  • Biology
  • Transcription factor
  • Serine
  • Nuclear transport
  • Threonine
  • Cytoplasm
  • Cell biology
UN Sustainable Development Goals
  • Good health and well-being
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