O-GlcNAcylation of kinases

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• 作者：Wagner B. Dias¹ ; ^{diaswb@biof.ufrj.br} ; Win D. Cheung ; Gerald W. Hart ; ^{gwhart@jhmi.edu}
• 关键词：O-GlcNAc ; Phosphorylation ; Protein array ; Kinases ; OGT ; Signaling
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：1 June, 2012
• 卷：422
• 期：2
• 页码：224-228
• 文件大小：689 K

摘要

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.