Functional interaction between the ubiquitin-specific protease 25 and the SYK tyrosine kinase.
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.
Mesh Terms:
Animals, COS Cells, Cell Line, Cercopithecus aethiops, Chromosome Mapping, Genetic Vectors, Humans, Intracellular Signaling Peptides and Proteins, Mutation, Phosphorylation, Plasmids, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Two-Hybrid System Techniques, Ubiquitin Thiolesterase
Animals, COS Cells, Cell Line, Cercopithecus aethiops, Chromosome Mapping, Genetic Vectors, Humans, Intracellular Signaling Peptides and Proteins, Mutation, Phosphorylation, Plasmids, Protein Structure, Tertiary, Protein-Tyrosine Kinases, Two-Hybrid System Techniques, Ubiquitin Thiolesterase
Exp. Cell Res.
Date: Feb. 15, 2010
PubMed ID: 19909739
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