O-GlcNAcylation of kinases

Dias WB, Cheung WD, Hart GW. (2012) O-GlcNAcylation of kinases. Biochem Biophys Res Commun. 422(2):224-8. PMID: 22564745; PMCID: PMC3387735

Abstract

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.

PMCID:PMC3387735

Link to journal: http://www.journals.elsevier.com/biochemical-and-biophysical-research-communications/