BACKGROUND Spleen tyrosine kinase (Syk) is a non-receptor protein tyrosine kinase expressed in a wide range of hematopoietic cells.1 Syk has not only been recognized as a key player in both innate and adaptive immunity, but there is also evidence of a role for Syk in non-immune cells and in the maintenance of vascular integrity,2 as well as the pathogenesis of malignant cancer.3 Syk contains two SH2 domains in tandem, and multiple auto-phosphorylation sites. Syk is activated upon binding of tandem SH2 domains to the immuno-receptor tyrosine-based activating motif (ITAM) of various types of receptors such as Fc-gamm-R, CR3, Dectin-1, and apoptotic cell-recognizing receptor. Syk is critical for the tyrosine phosphorylation of multiple proteins which regulate important pathways downstream of the receptor, such as Ca2+ mobilization, mitogen-activated protein kinase (MAPK) cascades, PI-3 kinase pathway and many other signaling pathways.4
1. Nilsson, S. et al: Physiol Rev 81:1535–65, 2001.
2. Tremblay, G. B. et al: Mol Endocrinol. 11: 353-365, 1997.
3. Mathews, J & Gustafsson, J. A.: Mol. Interv. 3:281-92, 2003.
4. Tremblay, A. et al: Mol Cell 3, 513–519, 1999.
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