Abstract
The tyrosine kinase Syk is essential for signaling from FcrepsilonRI in mast cells. The Src homology domain mediated binding of Syk to the phosphorylated immunoreceptor tyrosine-based motif (ITAM) of the receptor subunits results in a conformational change and activation. Studies in Syk deficient mast cells have defined the pathways that are activated upstream and downstream of Syk and have demonstrated the functional importance of the linker region of Syk in signaling in mast cells.
MeSH terms
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Animals
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Cell Membrane / enzymology
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Enzyme Precursors / chemistry
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Enzyme Precursors / physiology*
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Intracellular Signaling Peptides and Proteins
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Leukocyte Common Antigens / physiology
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Mast Cells / enzymology*
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Mast Cells / immunology
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Mice
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Models, Biological
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Protein Structure, Tertiary
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Protein-Tyrosine Kinases / chemistry
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Protein-Tyrosine Kinases / physiology*
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Receptors, IgE / chemistry
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Receptors, IgE / metabolism
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Signal Transduction*
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Syk Kinase
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Tyrosine / metabolism
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ZAP-70 Protein-Tyrosine Kinase
Substances
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Enzyme Precursors
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Intracellular Signaling Peptides and Proteins
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Receptors, IgE
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Tyrosine
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Protein-Tyrosine Kinases
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Syk Kinase
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Syk protein, mouse
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ZAP-70 Protein-Tyrosine Kinase
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Zap70 protein, mouse
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Leukocyte Common Antigens