The JI
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     
 

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Request Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sulimenko, V.
Right arrow Articles by Dráber, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sulimenko, V.
Right arrow Articles by Dráber, P.
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.




This article has been cited by other articles:


Home page
 JCBHome page
N. B. Martin-Cofreces, J. Robles-Valero, J. R. Cabrero, M. Mittelbrunn, M. Gordon-Alonso, C.-H. Sung, B. Alarcon, J. Vazquez, and F. Sanchez-Madrid
MTOC translocation modulates IS formation and controls sustained T cell signaling
J. Cell Biol., September 9, 2008; 182(5): 951 - 962.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
H. Hehnly, D. Sheff, and M. Stamnes
Shiga Toxin Facilitates Its Retrograde Transport by Modifying Microtubule Dynamics
Mol. Biol. Cell, October 1, 2006; 17(10): 4379 - 4389.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Website Copyright © 2006 by The American Association of Immunologists, Inc. All rights reserved.
All Contents Copyright © 2006 by The American Association of Immunologists, Inc. All rights reserved.