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  • Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.

Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation.

FEBS letters (2017-06-06)
Jie Shi, Tihomir Tomašič, Suhela Sharif, Arwin J Brouwer, Marko Anderluh, Rob Ruijtenbeek, Roland J Pieters
ABSTRACT

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 six peptides by Jak2 inhibits their subsequent O-GlcNAcylation. However, O-GlcNAcylation has 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 show that the presence of a phosphate at Tyr364 of ZO3_357_371 slows the O-GlcNAcylation of nearby Ser369, while the presence of a GlcNAc at Ser369 has 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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
PUGNAc, ≥95% (HPLC)
Pricing and availability is not currently available.
Sigma-Aldrich
Uridine 5′-diphospho-N-acetylglucosamine sodium salt, ≥98%
Pricing and availability is not currently available.