O-GlcNAcylation of kinases

被引：70

作者：

Dias, Wagner B. ^{[1
]}

Cheung, Win D. ^{[1
]}

Hart, Gerald W. ^{[1
]}

机构：

[1] Johns Hopkins Univ, Dept Biol Chem, Baltimore, MD 21205 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 422卷 / 02期

基金：

美国国家卫生研究院;

关键词：

O-GlcNAc; Phosphorylation; Protein array; Kinases; OGT; Signaling; BETA-N-ACETYLGLUCOSAMINE; GLCNAC TRANSFERASE; PROTEIN-KINASE; SUBSTRATE-SPECIFICITY; CROSS-TALK; PHOSPHORYLATION; CELLS; TRANSCRIPTION; CANCER; PHOSPHATASE-1;

D O I：

10.1016/j.bbrc.2012.04.124

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

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. (C) 2012 Elsevier Inc. All rights reserved.

引用

页码：224 / 228

页数：5

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