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Updated: Jun 18, 2026

Identifying Protein-protein Interaction Sites Using Peptide Arrays
Published on: November 18, 2014
Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase
Michael Cholay1, Céline Reverdy, Richard Benarous
1Hybrigenics SA, 3-5 Impasse Reille 75014 Paris, France.
Abstract:
The SYK non-receptor tyrosine kinase is a key effector of immune receptors signaling in hematopoietic cells. Here, we identified and characterized a novel interaction between SYK and the ubiquitin-specific protease 25 (USP25). We report that the second SH2 domain of SYK physically interacts with a tyrosine-rich, C-terminal region of USP25 independently of tyrosine phosphorylation. Moreover, we showed that SYK specifically phosphorylates USP25 and alters its cellular levels. This study thus uncovers a new SYK substrate and reveals a novel SYK function, namely the regulation of USP25 cellular levels.
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