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  • Peptide microarray analysis of the cross-talk between O-GlcNAcylation and tyrosine phosphorylation
    Shi, Jie ...
    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 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.
    Vir: FEBS Letters [Elektronski vir]. - ISSN 1873-3468 (Vol. 591, iss. 13, 2017, str. 1872-1883)
    Vrsta gradiva - e-članek
    Leto - 2017
    Jezik - angleški
    COBISS.SI-ID - 4336753

    Povezava(-e):

    http://onlinelibrary.wiley.com/doi/10.1002/1873-3468.12708/full
    DOI

vir: FEBS Letters [Elektronski vir]. - ISSN 1873-3468 (Vol. 591, iss. 13, 2017, str. 1872-1883)
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