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Journal of Signal Transduction
Volume 2012 (2012), Article ID 694386, 10 pages
In Vivo Consequences of Disrupting SH3-Mediated Interactions of the Inducible T-Cell Kinase
1Department of Biology, Molecular Biology Institute and Center for Microbial Sciences, San Diego State University, San Diego, CA 92182, USA
2Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, IA 50011, USA
Received 20 January 2012; Accepted 24 February 2012
Academic Editor: Peter van der Geer
Copyright © 2012 Roman M. Levytskyy et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- C. S Guy and D. A. A Vignali, “Organization of proximal signal initiation at the TCR:CD3 complex,” Immunological Reviews, vol. 232, no. 1, pp. 7–21, 2009.
- A. H Andreotti, P. L Schwartzberg, R. E Joseph, and L. J Berg, “T-cell signaling regulated by the Tec family kinase, Itk,” Cold Spring Harbor perspectives in biology, vol. 2, no. 7, article a002287, 2010.
- L. J Berg, L. D Finkelstein, J. A Lucas, and P. L Schwartzberg, “Tec family kinases in T lymphocyte development and function,” Annual Review of Immunology, vol. 23, pp. 549–600, 2005.
- D Beach, R Gonen, Y Bogin, I. G Reischl, and D Yablonski, “Dual role of SLP-76 in mediating T cell receptor-induced activation of phospholipase C-γ1,” Journal of Biological Chemistry, vol. 282, no. 5, pp. 2937–2946, 2007.
- C. D Tsoukas, J. A Grasis, C. D Browne, and K. A Ching, “Inducible T cell tyrosine kinase (ITK): structural requirements and actin polymerization,” Advances in Experimental Medicine and Biology, vol. 584, pp. 29–41, 2006.
- J. A Grasis and C. D Tsoukas, “Itk: the rheostat of the T cell response,” Journal of Signal Transduction, vol. 2011, Article ID 297868, 23 pages, 2011.
- B. B Au-Yeung, S. D Katzman, and D. J Fowell, “Cutting edge: Itk-dependent signals required for CD4+ T cells to exert, but not gain, Th2 effector function,” Journal of Immunology, vol. 176, no. 7, pp. 3895–3899, 2006.
- W. C Yang, Y Collette, J. A Nunès, and D Olive, “Tec kinases: a family with multiple roles in immunity,” Immunity, vol. 12, no. 4, pp. 373–382, 2000.
- S. C Bunnell, M Diehn, M. B Yaffe, P. R Findell, L. C Cantley, and L. J Berg, “Biochemical interactions integrating Itk with the T cell receptor-initiated signaling cascade,” Journal of Biological Chemistry, vol. 275, no. 3, pp. 2219–2230, 2000.
- M. S Jordan, J. E Smith, J. C Burns et al., “Complementation in trans of altered thymocyte development in mice expressing mutant forms of the adaptor molecule SLP76,” Immunity, vol. 28, no. 3, pp. 359–369, 2008.
- J. A Grasis, D. M Guimond, N. R Cam et al., “In vivo significance of ITK-SLP-76 interaction in cytokine production,” Molecular and Cellular Biology, vol. 30, no. 14, pp. 3596–3609, 2010.
- K. N Brazin, D. B Fulton, and A. H Andreotti, “A specific intermolecular association between the regulatory domains of a Tec family kinase,” Journal of Molecular Biology, vol. 302, no. 3, pp. 607–623, 2000.
- L Min, W Wu, R. E Joseph, D. B Fulton, L Berg, and A. H Andreotti, “Disrupting the intermolecular self-association of Itk enhances T cell signaling,” Journal of Immunology, vol. 184, no. 8, pp. 4228–4235, 2010.
- K. A Ching, Y Kawakami, T Kawakami, and C. D Tsoukas, “Emt/Itk associates with activated TCR complexes: role of the pleckstrin homology domain,” Journal of Immunology, vol. 163, no. 11, pp. 6006–6013, 1999.
- S. D Heyeck, H. M Wilcox, S. C Bunnell, and L. J Berg, “Lck phosphorylates the activation loop tyrosine of the Itk kinase domain and activates Itk kinase activity,” Journal of Biological Chemistry, vol. 272, no. 40, pp. 25401–25408, 1997.
- T Zal and N. R. J Gascoigne, “Photobleaching-corrected FRET efficiency imaging of live cells,” Biophysical Journal, vol. 86, no. 6, pp. 3923–3939, 2004.
- M. C Montoya, D Sancho, G Bonello et al., “Role of ICAM-3 in the initial interaction of T lymphocytes and APCs,” Nature Immunology, vol. 3, no. 2, pp. 159–168, 2002.
- K. R Schulz, E. A Danna, P. O Krutzik, and G. P Nolan, “Single-cell phospho-protein analysis by flow cytometry,” Current Protocols in Immunology, vol. 8, unit 8.17, 2007.
- P. O Krutzik and G. P Nolan, “Intracellular phospho-protein staining techniques for flow cytometry: monitoring single cell signaling events,” Cytometry Part A, vol. 55, no. 2, pp. 61–70, 2003.
- I. C Ho, D Lo, and L. H Glimcher, “c-maf Promotes T helper cell type 2 (Th2) and attenuates Th1 differentiation by both interleukin 4-dependent and -independent mechanisms,” Journal of Experimental Medicine, vol. 188, no. 10, pp. 1859–1866, 1998.
- A. T Miller, H. M Wilcox, Z Lai, and L. J Berg, “Signaling through Itk promotes T helper 2 differentiation via negative regulation of T-bet,” Immunity, vol. 21, no. 1, pp. 67–80, 2004.
- H. M Wilcox and L. J Berg, “Itk phosphorylation sites are required for functional activity in primary T cells,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37112–37121, 2003.
- M. I Wahl, A. C Fluckiger, R. M Kato, H Park, O. N Witte, and D. J Rawlings, “Phosphorylation of two regulatory tyrosine residues in the activation of Bruton's tyrosine kinase via alternative receptors,” Proceedings of the National Academy of Sciences of the United States of America, vol. 94, no. 21, pp. 11526–11533, 1997.
- B Poulin, F Sekiya, and S. G Rhee, “Intramolecular interaction between phosphorylated tyrosine-783 and the C-terminal Src homology 2 domain activates phospholipase C-γ1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 12, pp. 4276–4281, 2005.
- A Baguet and M Bix, “Chromatin landscape dynamics of the Il4-Il13 locus during T helper 1 and 2 development,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 31, pp. 11410–11415, 2004.
- Y. H Huang, J. A Grasis, A. T Miller et al., “Positive regulation of Itk PH domain function by soluble IP4,” Science, vol. 316, no. 5826, pp. 886–889, 2007.
- K. A Ching, J. A Grasis, P Tailor, Y Kawakami, T Kawakami, and C. D Tsoukas, “TCR/CD3-induced activation and binding of Emt/Itk to linker of activated T cell complexes: requirement for the Src homology 2 domain,” Journal of Immunology, vol. 165, no. 1, pp. 256–262, 2000.
- D Dombroski, R. A Houghtling, C. M Labno et al., “Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton,” Journal of Immunology, vol. 174, no. 3, pp. 1385–1392, 2005.
- Q Qi, N Sahu, and A August, “Tec kinase Itk forms membrane clusters specifically in the vicinity of recruiting receptors,” Journal of Biological Chemistry, vol. 281, no. 50, pp. 38529–38534, 2006.