O-GlcNAc and the control of gene expression

Biochim Biophys Acta. 1999 Dec 6;1473(1):161-71. doi: 10.1016/s0304-4165(99)00176-2.


Many eukaryotic proteins contain O-linked N-acetylglucosamine (O-GlcNAc) on their serine and threonine side chain hydroxyls. In contrast to classical cell surface glycosylation, O-GlcNAc occurs on resident nuclear and cytoplasmic proteins. O-GlcNAc exists as a single monosaccharide residue, showing no evidence of further elongation. Like phosphorylation, O-GlcNAc is highly dynamic, transiently modifying proteins. These post-translational modifications give rise to functionally distinct subsets of a given protein. Furthermore, all known O-GlcNAc proteins are also phosphoproteins that reversibly form multimeric complexes that are sensitive to the state of phosphorylation. This observation implies that O-GlcNAc may work in concert with phosphorylation to mediate regulated protein interactions. The proteins that bear the O-GlcNAc modification are very diverse, including RNA polymerase II and many of its transcription factors, numerous chromatin-associated proteins, nuclear pore proteins, proto-oncogenes, tumor suppressors and proteins involved in translation. Here, we discuss the functional implications of O-GlcNAc-modifications of proteins involved in various aspects of gene expression, beginning with proteins involved in transcription and ending with proteins involved in regulating protein translation.

Publication types

  • Review

MeSH terms

  • Acetylglucosamine / metabolism*
  • Chromatin / metabolism
  • Eukaryotic Cells
  • Gene Expression Regulation*
  • Nuclear Proteins / metabolism*
  • Oncogene Proteins / metabolism
  • Phosphoproteins / metabolism
  • Protein Biosynthesis
  • Protein Processing, Post-Translational
  • RNA Polymerase II / metabolism
  • Transcription Factors / metabolism


  • Chromatin
  • Nuclear Proteins
  • Oncogene Proteins
  • Phosphoproteins
  • Transcription Factors
  • RNA Polymerase II
  • Acetylglucosamine