O-Linked GlcNAc Biosynthesis and Function

K. Sakabe, Gerald Warren Hart

Research output: Chapter in Book/Report/Conference proceedingChapter


O-GlcNAc is the post-translational modification of nuclear and cytoplasmic proteins on Ser and Thr residues by N-acetylglucosamine. Much like its signaling counterpart phosphorylation, O-GlcNAc cycles dynamically in response to various stimuli regulating protein function, interactions, cytolocalization, and stability. The enzymes involved in the cycling of O-GlcNAc are O-GlcNAc transferase (OGT), which adds the sugar from the donor substrate UDP-GlcNAc, and O-GlcNAcase, which catalyzes the hydrolysis. O-GlcNAc is an abundant post-translational modification, found on proteins from virtually every functional class found in cells. Because of the many processes that O-GlcNAc regulates, it is not surprising that misregulation of this post-translational modification is found in diseases such as type II diabetes, Alzheimer's disease, and cancer.

Original languageEnglish (US)
Title of host publicationEncyclopedia of Biological Chemistry
Subtitle of host publicationSecond Edition
PublisherElsevier Inc.
Number of pages4
ISBN (Electronic)9780123786319
ISBN (Print)9780123786302
StatePublished - Feb 15 2013


  • Alzheimer's disease
  • Cancer
  • Diabetes
  • Hexosamine biosynthetic pathway
  • O-GlcNAc
  • O-GlcNAc transferase
  • O-GlcNAcase
  • Phosphorylation
  • Post-translational modification
  • Signaling
  • UDP-GlcNAc

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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