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. Epub 2009 Nov 10.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • COS Cells
  • Cell Line
  • Chlorocebus aethiops
  • Chromosome Mapping
  • Genetic Vectors / genetics
  • Humans
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Mutation / genetics
  • Phosphorylation
  • Plasmids / genetics
  • Protein Structure, Tertiary
  • Protein-Tyrosine Kinases / genetics
  • Protein-Tyrosine Kinases / metabolism*
  • Syk Kinase
  • Two-Hybrid System Techniques
  • Ubiquitin Thiolesterase / genetics
  • Ubiquitin Thiolesterase / metabolism*

Substances

  • Intracellular Signaling Peptides and Proteins
  • USP25 protein, human
  • Protein-Tyrosine Kinases
  • SYK protein, human
  • Syk Kinase
  • Ubiquitin Thiolesterase