About this Journal Submit a Manuscript Table of Contents
Journal of Signal Transduction
Volume 2012 (2012), Article ID 694386, 10 pages
http://dx.doi.org/10.1155/2012/694386
Research Article

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.

Linked References

  1. 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. View at Publisher · View at Google Scholar · View at Scopus
  2. 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. View at Publisher · View at Google Scholar · View at Scopus
  3. 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. View at Publisher · View at Google Scholar · View at Scopus
  4. 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. View at Publisher · View at Google Scholar · View at Scopus
  5. 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. View at Publisher · View at Google Scholar · View at Scopus
  6. 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. View at Publisher · View at Google Scholar
  7. 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. View at Scopus
  8. 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. View at Scopus
  9. 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. View at Publisher · View at Google Scholar · View at Scopus
  10. 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. View at Publisher · View at Google Scholar · View at Scopus
  11. 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. View at Publisher · View at Google Scholar · View at Scopus
  12. 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. View at Publisher · View at Google Scholar · View at Scopus
  13. 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. View at Publisher · View at Google Scholar · View at Scopus
  14. 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. View at Scopus
  15. 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. View at Publisher · View at Google Scholar · View at Scopus
  16. 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. View at Publisher · View at Google Scholar · View at Scopus
  17. 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. View at Publisher · View at Google Scholar · View at Scopus
  18. 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. View at Scopus
  19. 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. View at Scopus
  20. 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. View at Publisher · View at Google Scholar · View at Scopus
  21. 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. View at Publisher · View at Google Scholar · View at Scopus
  22. 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. View at Publisher · View at Google Scholar · View at Scopus
  23. 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. View at Publisher · View at Google Scholar · View at Scopus
  24. 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. View at Publisher · View at Google Scholar · View at Scopus
  25. 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. View at Publisher · View at Google Scholar · View at Scopus
  26. 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. View at Publisher · View at Google Scholar · View at Scopus
  27. 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. View at Scopus
  28. 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. View at Scopus
  29. 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. View at Publisher · View at Google Scholar · View at Scopus