O-GlcNAcylation of kinases

Biochem Biophys Res Commun. 2012 Jun 1;422(2):224-8. doi: 10.1016/j.bbrc.2012.04.124. Epub 2012 Apr 30.


Recent evidence indicates that site-specific crosstalk between O-GlcNAcylation and phosphorylation and the O-GlcNAcylation of kinases play an important role in regulating cell signaling. However, relatively few kinases have been analyzed for O-GlcNAcylation. Here, we identify additional kinases that are substrates for O-GlcNAcylation using an in vitro OGT assay on a functional kinase array. Forty-two kinases were O-GlcNAcylated in vitro, representing 39% of the kinases on the array. In addition, we confirmed the in vivo O-GlcNAcylation of three identified kinases. Our results suggest that O-GlcNAcylation may directly regulate a substantial number of kinases and illustrates the increasingly complex relationship between O-GlcNAcylation and phosphorylation in cellular signaling.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Acetylglucosamine / chemistry*
  • Acylation
  • HEK293 Cells
  • Humans
  • N-Acetylglucosaminyltransferases / chemistry
  • N-Acetylglucosaminyltransferases / genetics
  • Phosphorylation
  • Phosphotransferases (Alcohol Group Acceptor) / chemistry*
  • Phosphotransferases (Alcohol Group Acceptor) / isolation & purification
  • Protein Array Analysis
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Substrate Specificity


  • Recombinant Proteins
  • N-Acetylglucosaminyltransferases
  • O-GlcNAc transferase
  • Phosphotransferases (Alcohol Group Acceptor)
  • N-acetylglucosamine kinase
  • Acetylglucosamine