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BioMed Research International
Volume 2013 (2013), Article ID 740187, 10 pages
http://dx.doi.org/10.1155/2013/740187
Research Article

TrkAIII Promotes Microtubule Nucleation and Assembly at the Centrosome in SH-SY5Y Neuroblastoma Cells, Contributing to an Undifferentiated Anaplastic Phenotype

1Department of Applied Clinical and Biotechnological Sciences, University of L'Aquila, Via Vetoio, Coppito 2, 67100 L’Aquila, Italy
2Department of Experimental Medicine, University of Rome “La Sapienza,” 00185 Rome, Italy

Received 20 March 2013; Accepted 18 May 2013

Academic Editor: Rita de Cassia Stocco

Copyright © 2013 Antonietta R. Farina 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. A. Tacconelli, A. R. Farina, L. Cappabianca et al., “TrkA alternative splicing: a regulated tumor-promoting switch in human neuroblastoma,” Cancer Cell, vol. 6, no. 4, pp. 347–360, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. A. Tacconelli, A. R. Farina, L. Cappabianca et al., “TrkAIII expression in the thymus,” Journal of Neuroimmunology, vol. 183, no. 1-2, pp. 151–161, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. A. R. Farina, A. Tacconelli, L. Cappabianca et al., “The neuroblastoma tumour-suppressor trkAI and its oncogenic alternative trkAIII splice variant exhibit geldanamycin-sensitive interactions with Hsp90 in human neuroblastoma cells,” Oncogene, vol. 28, no. 46, pp. 4075–4094, 2009. View at Publisher · View at Google Scholar · View at Scopus
  4. A. R. Farina, A. Tacconelli, L. Cappabianca et al., “The alternative TrkAIII splice variant targets the centrosome and promotes genetic instability,” Molecular and Cellular Biology, vol. 29, no. 17, pp. 4812–4830, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. A. R. Farina, L. Cappabianca, P. Ruggeri, et al., “Alternative TrkA splicing and neuroblastoma,” in Neuroblastoma Present and Future, H. Shimada, Ed., pp. 111–136, Intech, Croatia, 2012.
  6. J. C. Arevalo, B. Conde, B. L. Hempstead, M. V. Chao, D. Martin-Zanca, and P. Perez, “TrkA Immunoglobulin-like ligand binding domains inhibit spontaneous activation of the receptor,” Molecular and Cellular Biology, vol. 20, no. 16, pp. 5908–5916, 2000. View at Publisher · View at Google Scholar · View at Scopus
  7. F. L. Watson, M. A. Porcionatto, A. Bhattacharyya, C. D. Stiles, and R. A. Segal, “TrkA glycosylation regulates receptor localisation and activity,” Journal of Neurobiology, vol. 39, pp. 323–336, 1999.
  8. E. Lavenius, C. Gestblom, I. Johansson, E. Nånberg, and S. Påhlman, “Transfection of TRK-A into human neuroblastoma cells restores their ability to differentiate in response to nerve growth factor,” Cell Growth and Differentiation, vol. 6, no. 6, pp. 727–736, 1995. View at Scopus
  9. E. Lucarelli, D. Kaplan, and C. J. Thiele, “Activation of trk-A but not trk-B signal transduction pathway inhibits growth of neuroblastoma cells,” European Journal of Cancer, vol. 33, no. 12, pp. 2068–2070, 1997. View at Publisher · View at Google Scholar · View at Scopus
  10. A. M. Simpson, R. Iyer, J. L. Mangino et al., “TrkAIII isoform expression upregulates stem cell markers and correlates with worse outcome in neuroblastomas (NBs),” in Proceedings of the Advances in Neuroblastoma Research, POT055, p. 164, 2012.
  11. M. Kuijpers and C. C. Hoogenraad, “Centrosomes, microtubules and neuronal development,” Molecular and Cellular Neuroscience, vol. 48, no. 4, pp. 349–358, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Bornens, “Centrosome composition and microtubule anchoring mechanisms,” Current Opinion in Cell Biology, vol. 14, no. 1, pp. 25–34, 2002. View at Publisher · View at Google Scholar · View at Scopus
  13. J. Lüders, U. K. Patel, and T. Stearns, “GCP-WD is a γ-tubulin targeting factor required for centrosomal and chromatin-mediated microtubule nucleation,” Nature Cell Biology, vol. 8, no. 2, pp. 137–147, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. J. Lüders and T. Stearns, “Microtubule-organizing centers: a reevaluation,” Nature Reviews Molecular Cell Biology, vol. 8, pp. 161–167, 2007.
  15. K. Katagiri, T. Katagiri, K. Kajiyama, T. Yamamoto, and T. Yoshida, “Tyrosine-phosphorylation of tubulin during monocytic differentiation of HL-60 cells,” Journal of Immunology, vol. 150, no. 2, pp. 585–593, 1993. View at Scopus
  16. Y. A. Komarova, A. S. Akhmanova, S. Kojima, N. Galjart, and G. G. Borisy, “Cytoplasmic linker proteins promote microtubule rescue in vivo,” Journal of Cell Biology, vol. 159, no. 4, pp. 589–599, 2002. View at Scopus
  17. A.-M. Tassin, B. Maro, and M. Bornens, “Fate of microtubule-organizing centers during myogenesis in vitro,” Journal of Cell Biology, vol. 100, no. 1, pp. 35–46, 1985. View at Scopus
  18. A. M. Tassin, M. Paintrand, E. G. Berger, and M. Bornens, “The Golgi apparatus remains associated with microtubule organizing centers during myogenesis,” Journal of Cell Biology, vol. 101, no. 2, pp. 630–638, 1985. View at Scopus
  19. L. Lewis, Y. Barrandon, H. Green, and G. Albrecht-Buehler, “The reorganization of microtubules and microfilaments in differentiating keratinocytes,” Differentiation, vol. 36, no. 3, pp. 228–233, 1987. View at Scopus
  20. K. J. M. Zaal, E. Reid, K. Mousavi et al., “Who needs microtubules? myogenic reorganization of MTOC, golgi complex and er exit sites persists despite lack of normal microtubule tracks,” PLoS ONE, vol. 6, no. 12, Article ID e29057, 2011. View at Publisher · View at Google Scholar · View at Scopus
  21. S. Pryor, G. McCaffrey, L. R. Young, and M. L. Grimes, “NGF causes TrKA to specifically attract microtubules to lipid rafts,” PLoS ONE, vol. 7, no. 4, Article ID e35163, 2012. View at Publisher · View at Google Scholar · View at Scopus
  22. V. Sulimenko, E. Dráberová, T. Sulimenko et al., “Regulation of microtubule formation in activated mast cells by complexes of γ-tubulin with Fyn and Syk kinases,” Journal of Immunology, vol. 176, no. 12, pp. 7243–7253, 2006. View at Scopus
  23. D. Colello, C. G. Reverte, R. Ward et al., “Androgen and Src signaling regulate centrosome activity,” Journal of Cell Science, vol. 123, no. 12, pp. 2094–2102, 2010. View at Publisher · View at Google Scholar · View at Scopus
  24. D. Colello, S. Mathew, R. Ward, K. Pumiglia, and S. E. LaFlamme, “Integrins regulate microtubule nucleating activity of centrosome through mitogen-activated protein kinase/extracellular signal-regulated kinase kinase/extracellular signal-regulated kinase (MEK/ERK) signaling,” Journal of Biological Chemistry, vol. 287, no. 4, pp. 2520–2530, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. C. E. Laurent, F. J. Delfino, H. Y. Cheng, and T. E. Smithgall, “The human c-Fes tyrosine kinase binds tubulin and microtubules through separate domains and promotes microtubule assembly,” Molecular and Cellular Biology, vol. 24, no. 21, pp. 9351–9358, 2004. View at Publisher · View at Google Scholar · View at Scopus
  26. T. Kadowaki, Y. Fujita-Yamaguchi, and E. Nishida, “Phosphorylation of tubulin and microtubule-associated proteins by the purified insulin receptor kinase,” Journal of Biological Chemistry, vol. 260, no. 7, pp. 4016–4020, 1985. View at Scopus
  27. R. Kapeller, A. Toker, L. C. Cantley, and C. L. Carpenter, “Phosphoinositide 3-kinase binds constitutively to α/β-tubulin and binds to γ-tubulin in response to insulin,” Journal of Biological Chemistry, vol. 270, no. 43, pp. 25985–25991, 1995. View at Publisher · View at Google Scholar · View at Scopus
  28. E. L. K. Goh, T. J. Pircher, and P. E. Lobie, “Growth hormone promotion of tubulin polymerization stabilizes the microtubule network and protects against colchicine-induced apoptosis,” Endocrinology, vol. 139, no. 10, pp. 4364–4372, 1998. View at Scopus
  29. D. G. Drubin, S. C. Feinstein, E. M. Shooter, and M. W. Kirschner, “Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors,” Journal of Cell Biology, vol. 101, no. 5 I, pp. 1799–1807, 1985. View at Scopus
  30. F. Zhou, J. Zhou, S. Dedhar, Y. Wu, and W. D. Snider, “NGF-induced axon growth is mediated by localized inactivation of GSK-3β and functions of the microtubule plus end binding protein APC,” Neuron, vol. 42, no. 6, pp. 897–912, 2004. View at Publisher · View at Google Scholar · View at Scopus
  31. G. Morfini, M. C. DiTella, F. Feiguin, N. Carri, and A. Caceres, “Neurotrophin-3 enhances neurite outgrowth in cultured hippocampal pyramidal neurons,” Journal of Neuroscience Research, vol. 39, no. 2, pp. 219–232, 1994. View at Publisher · View at Google Scholar · View at Scopus
  32. Z. Zhang, Y. Yang, A. Gong, C. Wang, Y. Liang, and Y. Chen, “Localization of NGF and TrkA at mitotic apparatus in human glioma cell line U251,” Biochemical and Biophysical Research Communications, vol. 337, no. 1, pp. 68–74, 2005. View at Publisher · View at Google Scholar · View at Scopus
  33. E. J. Jung, S. Y. Lee, and C. W. Kim, “Proteomic analysis of novel targets associated with TrkA-mediated tyrosine phosphorylation signaling pathways in SK-N-MC neuroblastoma cells,” Proteomics, vol. 13, pp. 355–367, 2013.
  34. H. Yano, F. S. Lee, H. Kong et al., “Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor,” The Journal of Neuroscience, vol. 21, no. 3, article RC125, 2001. View at Scopus
  35. A. M. Camoratto, J. P. Jani, T. S. Angeles et al., “CEP-751 inhibits Trk receptor tyrosine kinase activity in vitro and exhibits anti-tumor activity,” International Journal of Cancer, vol. 72, pp. 673–679, 1997.
  36. W. S. Rasband, “ImageJ,” U. S. National Institutes of Health, Bethesda, Md, USA, 1997–2012, http://imagej.nih.gov/ij/.
  37. P. A. Bromann, H. Korkaya, and S. A. Courtneidge, “The interplay between Src family kinases and receptor tyrosine kinases,” Oncogene, vol. 23, no. 48, pp. 7957–7968, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. S. J. Dixon, J. I. S. MacDonald, K. N. Robinson, C. J. Kubu, and S. O. Meakin, “Trk receptor binding and neurotrophin/fibroblast growth factor (FGF)-dependent activation of the FGF receptor substrate (FRS)-3,” Biochimica et Biophysica Acta, vol. 1763, no. 4, pp. 366–380, 2006. View at Publisher · View at Google Scholar · View at Scopus