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Updated: May 22, 2026

Identification of Kinase-substrate Pairs Using High Throughput Screening
Published on: August 29, 2015
O-GlcNAcylation of kinases
Wagner B Dias1, Win D Cheung, Gerald W Hart
1Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. diaswb@biof.ufrj.br
None:
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.
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