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

O-GlcNAcylation of kinases.

Author information

1
Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. diaswb@biof.ufrj.br

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.

PMID:
22564745
PMCID:
PMC3387735
DOI:
10.1016/j.bbrc.2012.04.124
[Indexed for MEDLINE]
Free PMC Article

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