title: O-GlcNAcylation of kinases.
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.
authors.affiliation: Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. diaswb@biof.ufrj.br
authors.forename: Wagner B
authors.initials: WB
authors.lastname: Dias
authors.forename: Win D
authors.initials: WD
authors.lastname: Cheung
authors.forename: Gerald W
authors.initials: GW
authors.lastname: Hart
mesh_terms: D000117:Acetylglucosamine / Q000737:chemistry*; D000215:Acylation; D057809:HEK293 Cells; D006801:Humans; D017351:N-Acetylglucosaminyltransferases / Q000737:chemistry / Q000235:genetics; D010766:Phosphorylation; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000302:isolation & purification; D040081:Protein Array Analysis; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase; D017853:Phosphotransferases (Alcohol Group Acceptor); C018716:N-acetylglucosamine kinase; D000117:Acetylglucosamine