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Peptide microarray analysis of the cross‐talk between O‐Glc NA cylation and tyrosine phosphorylation
Author(s) -
Shi Jie,
Tomašič Tihomir,
Sharif Suhela,
Brouwer Arwin J.,
Anderluh Marko,
Ruijtenbeek Rob,
Pieters Roland J.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12708
Subject(s) - phosphorylation , peptide , tyrosine phosphorylation , tyrosine , chemistry , biochemistry , protein phosphorylation , microbiology and biotechnology , protein tyrosine phosphatase , biology , protein kinase a
O‐Glc NA cylation of proteins regulates important cellular processes. A few reports noted that O‐Glc NA cylation 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‐Glc NA cylation. However, O‐Glc NA cylation has no detectable effect on their subsequent phosphorylation. A specific peptide ( ZO 3_357_371), derived from the ZO ‐3 protein, was studied in detail. Kinetic results show that the presence of a phosphate at Tyr364 of ZO 3_357_371 slows the O‐Glc NA cylation of nearby Ser369, while the presence of a Glc NA c 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.