O-linked N-acetylglucosamine levels in cerebellar neurons respond reciprocally to pertubations of phosphorylation

Eur J Biochem. 1999 Jun;262(3):824-31. doi: 10.1046/j.1432-1327.1999.00439.x.


The novel intracellular carbohydrate O-linked N-acetylglucosamine (O-GlcNAc) is present on proteins ranging from those of viruses to those of humans and include cytosolic, nuclear and plasma-membrane proteins. In this report we have examined the effect of manipulation of phosphorylation on the levels of O-GlcNAc in cerebellar neurons from early postnatal mice. Our results indicate a reciprocal response of O-GlcNAc levels to phosphorylation. Activation of protein kinase A or C, for example, results in reduced levels of O-GlcNAc specifically in the fraction of cytoskeletal and cytoskeleton-associated proteins, while inhibition of the same kinases results in increased levels of O-GlcNAc. These data are in keeping with a reciprocal action of O-GlcNAc with respect to phosphorylation and suggest that this modification may have a role in signal transduction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylglucosamine / metabolism*
  • Animals
  • Calcimycin / pharmacology
  • Carbohydrate Conformation
  • Cells, Cultured
  • Cerebellum / drug effects
  • Cerebellum / metabolism*
  • Enzyme Activation
  • Enzyme Inhibitors / pharmacology
  • Mice
  • Neurons / cytology
  • Neurons / drug effects
  • Neurons / metabolism*
  • Phosphoric Monoester Hydrolases / antagonists & inhibitors
  • Phosphorylation
  • Protein Kinase C / antagonists & inhibitors
  • Protein Kinase C / metabolism
  • Receptor Protein-Tyrosine Kinases / antagonists & inhibitors
  • Tetradecanoylphorbol Acetate / pharmacology


  • Enzyme Inhibitors
  • Calcimycin
  • Receptor Protein-Tyrosine Kinases
  • Protein Kinase C
  • Phosphoric Monoester Hydrolases
  • Tetradecanoylphorbol Acetate
  • Acetylglucosamine