Dataset for: Peptide Microarray Analysis of the Cross-talk Between O-GlcNAcylation and Tyrosine Phosphorylation

O-GlcNAcylation of proteins regulates important cellular processes. A few reports noted that O-GlcNAcylation exhibits cross-talk with tyrosine phosphorylation. With an activity-based microarray analysis of 256 tyrosine kinase peptide substrates, we found that phosphorylation of 6 peptides by Jak2 inhibited their subsequent O-GlcNAcylation. However, O-GlcNAcylation had no detectable effect on their subsequent phosphorylation. A specific peptide (ZO3_357_371), derived from the ZO-3 protein, was studied in detail. Kinetic results showed that the presence of a phosphate at Tyr364 of ZO3_357_371 slowed the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 had no significant effect on the phosphorylation of this peptide at Tyr364. These findings provide a glimpse into the new paradigm for cellular signaling control by cross-talk.