- About this Journal ·
- Abstracting and Indexing ·
- Aims and Scope ·
- Annual Issues ·
- Article Processing Charges ·
- Author Guidelines ·
- Bibliographic Information ·
- Citations to this Journal ·
- Contact Information ·
- Editorial Board ·
- Editorial Workflow ·
- Free eTOC Alerts ·
- Publication Ethics ·
- Recently Accepted Articles ·
- Reviewers Acknowledgment ·
- Submit a Manuscript ·
- Subscription Information ·
- Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 740187, 10 pages
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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- M. Kuijpers and C. C. Hoogenraad, “Centrosomes, microtubules and neuronal development,” Molecular and Cellular Neuroscience, vol. 48, no. 4, pp. 349–358, 2011.
- M. Bornens, “Centrosome composition and microtubule anchoring mechanisms,” Current Opinion in Cell Biology, vol. 14, no. 1, pp. 25–34, 2002.
- 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.
- J. Lüders and T. Stearns, “Microtubule-organizing centers: a reevaluation,” Nature Reviews Molecular Cell Biology, vol. 8, pp. 161–167, 2007.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- 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.
- W. S. Rasband, “ImageJ,” U. S. National Institutes of Health, Bethesda, Md, USA, 1997–2012, http://imagej.nih.gov/ij/.
- 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.
- 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.