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Mast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants.

ABSTRACT: The aggregation by antigen of the IgE bound to its high affinity receptor on mast cells initiates a complex series of biochemical events that result in the release of inflammatory mediators. The essential role of the protein tyrosine kinase Syk has been appreciated for some time, and newer results have defined the mechanism of its activation. The use of siRNA has defined the relative contribution of Syk, Fyn and Gab2 to signaling and has made possible a screening study to identify previously unrecognized molecules that are involved in these pathways.

SUBMITTER: Siraganian RP

PROVIDER: S-EPMC2998559 | biostudies-literature | 2010 Dec

REPOSITORIES: biostudies-literature

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Mast cell signaling: the role of protein tyrosine kinase Syk, its activation and screening methods for new pathway participants.

Siraganian Reuben P RP de Castro Rodrigo O RO Barbu Emilia A EA Zhang Juan J

FEBS letters 20100807 24

The aggregation by antigen of the IgE bound to its high affinity receptor on mast cells initiates a complex series of biochemical events that result in the release of inflammatory mediators. The essential role of the protein tyrosine kinase Syk has been appreciated for some time, and newer results have defined the mechanism of its activation. The use of siRNA has defined the relative contribution of Syk, Fyn and Gab2 to signaling and has made possible a screening study to identify previously unr ...[more]

PMID: 20696166

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Entropic allostery dominates the phosphorylation-dependent regulation of Syk tyrosine kinase release from immunoreceptor tyrosine-based activation motifs.

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