Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase

  • Exp Cell Res. 2010 Feb 15;316(4):667-75. doi: 10.1016/j.yexcr.2009.10.023.
Michael Cholay  1 ,  Céline Reverdy ,  Richard Benarous ,  Frédéric Colland ,  Laurent Daviet
Affiliations
  • 1. Hybrigenics SA, 3-5 Impasse Reille 75014 Paris, France.
PMID: 19909739 DOI: 10.1016/j.yexcr.2009.10.023
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.