The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
Structure and Function of Syk Protein-Tyrosine Kinasel
Kiyonao SadaTomoko TakanoShigeru YanagiHirohei Yamamura
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JOURNAL FREE ACCESS

2001 Volume 130 Issue 2 Pages 177-186

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Abstract

Non-receptor type of protein-tyrosine kinase Syk contains 2 Src homology 2 (SH2) domains in tandem and multiple autophosphorylation sites. Syk is activated upon binding of tandem SH2 domains to immunoreceptor tyrosine-based activating motif (ITAM) and plays an essential role in lymphocyte development and activation of immune cells. Syk is critical for tyrosine phosphorylation of multiple proteins which regulate important pathways leading from the receptor, such as Ca2+ mobilization and mitogen-activated protein kinase (MAPK) cascades. Recent findings reveal that expression of Syk appears to be involved in a wide variety of cellular functions and pathogenesis of malignant cancer. These observations have demonstrated that Syk is a key molecule that controls multiple physiological functions in cells.

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© The Japanese Biochemical Society
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