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The Journal of Immunology, 2006, 176: 7243-7253.
Copyright © 2006 by The American Association of Immunologists

Regulation of Microtubule Formation in Activated Mast Cells by Complexes of {gamma}-Tubulin with Fyn and Syk Kinases1

Vadym Sulimenko*, Eduarda Dráberová*, Tetyana Sulimenko*, Libor Macurek*, Vera Richterová*, Petr Dráber{dagger} and Pavel Dráber2,*

* Department of Biology of Cytoskeleton and {dagger} Department of Signal Transduction, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Prague, Czech Republic

Aggregation of the high-affinity IgE receptors (Fc{epsilon}RIs) on the surface of granulated mast cells initiates a chain of signaling events culminating in the release of allergy mediators. Although microtubules are involved in mast cell degranulation, the molecular mechanism that controls microtubule rearrangement after Fc{epsilon}RI triggering is poorly understood. In this study, we show that the activation of bone marrow-derived mast cells (BMMCs) induced by Fc{epsilon}RI aggregation or treatment with pervanadate leads to a rapid polymerization of microtubules. This polymerization was not dependent on the presence of Lyn kinase as determined by experiments with BMMCs isolated from Lyn-negative mice. One of the key regulators of microtubule polymerization is {gamma}-tubulin. Immunoprecipitation experiments revealed that {gamma}-tubulin from activated cells formed complexes with Fyn and Syk protein tyrosine kinases and several tyrosine phosphorylated proteins from both wild-type and Lyn–/– BMMCs. Pretreatment of the cells with Src-family or Syk-family selective tyrosine kinase inhibitors, PP2 or piceatannol, respectively, inhibited the formation of microtubules and reduced the amount of tyrosine phosphorylated proteins in {gamma}-tubulin complexes, suggesting that Src and Syk family kinases are involved in the initial stages of microtubule formation. This notion was corroborated by pull-down experiments in which {gamma}-tubulin complex bounds to the recombinant Src homology 2 and Src homology 3 domains of Fyn kinase. We propose that Fyn and Syk kinases are involved in the regulation of binding properties of {gamma}-tubulin and/or its associated proteins, and thus modulate the microtubule nucleation in activated mast cells.




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