About this Journal Submit a Manuscript Table of Contents
ISRN Cell Biology
Volume 2012 (2012), Article ID 597876, 7 pages
http://dx.doi.org/10.5402/2012/597876
Review Article

Focus on ADF/Cofilin: Beyond Actin Cytoskeletal Regulation

Department of Biomedical Imaging and Radiological Sciences, School of Biomedical Science and Engineering, National Yang-Ming University, Taipei, Taiwan

Received 8 November 2011; Accepted 8 December 2011

Academic Editors: V. M. Golubovskaya and A. A. Minin

Copyright © 2012 Cheng-Han Tsai and Yi-Jang Lee. 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. O. Bernard, “Lim kinases, regulators of actin dynamics,” International Journal of Biochemistry and Cell Biology, vol. 39, no. 6, pp. 1071–1076, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. J. Toshima, J. Y. Toshima, T. Amano, N. Yang, S. Narumiya, and K. Mizuno, “Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation,” Molecular Biology of the Cell, vol. 12, no. 4, pp. 1131–1145, 2001. View at Scopus
  3. J. Toshima, J. Y. Toshima, K. Takeuchi, R. Mori, and K. Mizuno, “Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular sertoli cells,” Journal of Biological Chemistry, vol. 276, no. 33, pp. 31449–31458, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. M. Kobayashi, M. Nishita, T. Mishima, K. Ohashi, and K. Mizuno, “MAPKAPK-2-mediated LIM-kinase activation is critical for VEGF-induced actin remodeling and cell migration,” EMBO Journal, vol. 25, no. 4, pp. 713–726, 2006. View at Publisher · View at Google Scholar · View at Scopus
  5. T. Takuma, T. Ichida, N. Yokoyama, S. Tamura, and T. Obinata, “Dephosphorylation of cofilin in parotid acinar cells,” Journal of Biochemistry, vol. 120, no. 1, pp. 35–41, 1996. View at Scopus
  6. J. R. Bamburg and B. W. Bernstein, “ADF/cofilin,” Current Biology, vol. 18, no. 7, pp. R273–R275, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. N. Kaji, K. Ohashi, M. Shuin, R. Niwa, T. Uemura, and K. Mizuno, “Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells,” Journal of Biological Chemistry, vol. 278, no. 35, pp. 33450–33455, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. R. M. Warn and R. Magrath, “F-actin distribution during the cellularization of the Drosophila embryo visualized with FL-phalloidin,” Experimental Cell Research, vol. 143, no. 1, pp. 103–114, 1983. View at Scopus
  9. C. H. Tsai, S. J. Chiu, C. C. Liu et al., “Regulated expression of cofilin and the consequent regulation of p27 kip1 are essential for G1 phase progression,” Cell Cycle, vol. 8, no. 15, pp. 2365–2374, 2009. View at Scopus
  10. W. Wang, G. Mouneimne, M. Sidani et al., “The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors,” Journal of Cell Biology, vol. 173, no. 3, pp. 395–404, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. W. Wang, R. Eddy, and J. Condeelis, “The cofilin pathway in breast cancer invasion and metastasis,” Nature Reviews Cancer, vol. 7, no. 6, pp. 429–440, 2007. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Quintela-Fandino, E. Arpaia, D. Brenner et al., “HUNK suppresses metastasis of basal type breast cancers by disrupting the interaction between PP2A and cofilin-1,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 6, pp. 2622–2627, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. Y. J. Lee, D. J. Mazzatti, Z. Yun, and P. C. Keng, “Inhibition of invasiveness of human lung cancer cell line H1299 by over-expression of cofilin,” Cell Biology International, vol. 29, no. 11, pp. 877–883, 2005. View at Publisher · View at Google Scholar · View at Scopus
  14. R. Nagaoka, H. Abe, and T. Obinata, “Site-directed mutagenesis of the phosphorylation site of cofilin: its role in cofilin-actin interaction and cytoplasmic localization,” Cell Motility and the Cytoskeleton, vol. 35, no. 3, pp. 200–209, 1996. View at Publisher · View at Google Scholar · View at Scopus
  15. J. R. Bamburg, B. W. Bernstein, R. C. Davis et al., “ADF/Cofilin-actin rods in neurodegenerative diseases,” Current Alzheimer Research, vol. 7, no. 3, pp. 241–250, 2010. View at Publisher · View at Google Scholar · View at Scopus
  16. K. Berger and M. J. Moeller, “Cofilin-1 in the podocyte: a molecular switch for actin dynamics,” International Urology and Nephrology, vol. 43, no. 1, pp. 273–275, 2011. View at Publisher · View at Google Scholar
  17. M. K. Vartiainen, T. Mustonen, P. K. Mattila et al., “The three mouse actin-depolymerizing factor/cofilins evolved to fulfill cell-type-specific requirements for actin dynamics,” Molecular Biology of the Cell, vol. 13, no. 1, pp. 183–194, 2002. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Blanchoin, T. D. Pollard, and R. D. R. D. Mullins, “Interactions of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks,” Current Biology, vol. 10, no. 20, pp. 1273–1282, 2000. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Van Troys, L. Huyck, S. Leyman, S. Dhaese, J. Vandekerkhove, and C. Ampe, “Ins and outs of ADF/cofilin activity and regulation,” European Journal of Cell Biology, vol. 87, no. 8-9, pp. 649–667, 2008. View at Publisher · View at Google Scholar · View at Scopus
  20. B. W. Bernstein and J. R. Bamburg, “ADF/Cofilin: a functional node in cell biology,” Trends in Cell Biology, vol. 20, no. 4, pp. 187–195, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. M. Oser and J. Condeelis, “The cofilin activity cycle in lamellipodia and invadopodia,” Journal of Cellular Biochemistry, vol. 108, no. 6, pp. 1252–1262, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. S. Kurita, E. Gunji, K. Ohashi, and K. Mizuno, “Actin filaments-stabilizing and -bundling activities of cofilin-phosphatase Slingshot-1,” Genes to Cells, vol. 12, no. 5, pp. 663–676, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. N. Marcoux and K. Vuori, “EGF receptor activity is essential for adhesion-induced stress fiber formation and cofilin phosphorylation,” Cellular Signalling, vol. 17, no. 11, pp. 1449–1455, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. N. S. Bryce, G. Schevzov, V. Ferguson et al., “Specification of actin filament function and molecular composition by tropomyosin isoforms,” Molecular Biology of the Cell, vol. 14, no. 3, pp. 1002–1016, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. P. Gunning, G. O'Neill, and E. Hardeman, “Tropomyosin-based regulation of the actin cytoskeleton in time and space,” Physiological Reviews, vol. 88, no. 1, pp. 1–35, 2008. View at Publisher · View at Google Scholar · View at Scopus
  26. K. Katoh, Y. Kano, M. Amano, K. Kaibuchi, and K. Fujiwara, “Stress fiber organization regulated by MLCK and Rho-kinase in cultured human fibroblasts,” American Journal of Physiology, vol. 280, no. 6, pp. C1669–C1679, 2001. View at Scopus
  27. J. R. Molina and A. A. Adjei, “The Ras/Raf/MAPK pathway,” Journal of Thoracic Oncology, vol. 1, no. 1, pp. 7–9, 2006. View at Publisher · View at Google Scholar · View at Scopus
  28. W. Kolch, “Coordinating ERK/MAPK signalling through scaffolds and inhibitors,” Nature Reviews Molecular Cell Biology, vol. 6, no. 11, pp. 827–837, 2005. View at Publisher · View at Google Scholar · View at Scopus
  29. J. Paez and W. R. Sellers, “PI3K/PTEN/AKT pathway. A critical mediator of oncogenic signaling,” Cancer Treatment and Research, vol. 115, pp. 145–167, 2003. View at Scopus
  30. G. H. Wabnitz, G. Nebl, M. Klemke, A. J. Schröder, and Y. Samstag, “Phosphatidylinositol 3-kinase functions as a Ras effector in the signaling cascade that regulates dephosphorylation of the actin-remodeling protein cofilin after costimulation of untransformed human T lymphocytes,” Journal of Immunology, vol. 176, no. 3, pp. 1668–1674, 2006. View at Scopus
  31. D. T. Denhardt, “Signal-transducing protein phosphorylation cascades mediated by Ras/Rho proteins in the mammalian cell: the potential for multiplex signalling,” Biochemical Journal, vol. 318, no. 3, pp. 729–747, 1996. View at Scopus
  32. S. H. Zigmond, “Signal transduction and actin filament organization,” Current Opinion in Cell Biology, vol. 8, no. 1, pp. 66–73, 1996. View at Publisher · View at Google Scholar · View at Scopus
  33. S. Arber, F. A. Barbayannis, H. Hanser et al., “Regulation of actin dynamics through phosphorylation of cofilin by LIM- kinase,” Nature, vol. 393, no. 6687, pp. 805–809, 1998. View at Publisher · View at Google Scholar · View at Scopus
  34. T. Y. Huang, C. Dermardirossian, and G. M. Bokoch, “Cofilin phosphatases and regulation of actin dynamics,” Current Opinion in Cell Biology, vol. 18, no. 1, pp. 26–31, 2006. View at Publisher · View at Google Scholar · View at Scopus
  35. R. Niwa, K. Nagata-Ohashi, M. Takeichi, K. Mizuno, and T. Uemura, “Control of actin reorganization by slingshot, a family of phosphatases that dephosphorylate ADF/cofilin,” Cell, vol. 108, no. 2, pp. 233–246, 2002. View at Publisher · View at Google Scholar · View at Scopus
  36. Y. Yoo, H. J. Ho, C. Wang, and J. L. Guan, “Tyrosine phosphorylation of cofilin at Y68 by v-Src leads to its degradation through ubiquitin-proteasome pathway,” Oncogene, vol. 29, no. 2, pp. 263–272, 2010. View at Publisher · View at Google Scholar · View at Scopus
  37. M. De Graauw, I. Tijdens, M. B. Smeets, P. J. Hensbergen, A. M. Deelder, and B. Van De Water, “Annexin A2 phosphorylation mediates cell scattering and branching morphogenesis via cofilin activation,” Molecular and Cellular Biology, vol. 28, no. 3, pp. 1029–1040, 2008. View at Publisher · View at Google Scholar · View at Scopus
  38. U. Rescher, C. Ludwig, V. Konietzko, A. Kharitonenkov, and V. Gerke, “Tyrosine phosphorylation of annexin A2 regulates Rho-mediated actin rearrangement and cell adhesion,” Journal of Cell Science, vol. 121, no. 13, pp. 2177–2185, 2008. View at Publisher · View at Google Scholar · View at Scopus
  39. Y. J. Lee and P. C. Keng, “Studying the effects of actin cytoskeletal destabilization on cell cycle by cofilin overexpression,” Molecular Biotechnology, vol. 31, no. 1, pp. 1–10, 2005. View at Scopus
  40. G. C. Bellenchi, C. B. Gurniak, E. Perlas, S. Middei, M. Ammassari-Teule, and W. Witke, “N-cofilin is associated with neuronal migration disorders and cell cycle control in the cerebral cortex,” Genes and Development, vol. 21, no. 18, pp. 2347–2357, 2007. View at Publisher · View at Google Scholar · View at Scopus
  41. M. S. Crane, J. B. Clarke, and D. B. Thomas, “Cell cycle dependent changes in morphology. Studies with a cold sensitive mutant of Chinese hamster ovary cells,” Experimental Cell Research, vol. 107, no. 1, pp. 89–94, 1977. View at Scopus
  42. A. G. Clark and E. Paluch, “Mechanics and regulation of cell shape during the cell cycle,” Results and Problems in Cell Differentiation, vol. 53, pp. 31–73, 2011. View at Publisher · View at Google Scholar
  43. P. K. Hepler, A. Valster, T. Molchan, and J. W. Vos, “Roles for Kinesin and myosin during cytokinesis,” Philosophical Transactions of the Royal Society B, vol. 357, no. 1422, pp. 761–766, 2002. View at Publisher · View at Google Scholar · View at Scopus
  44. M. D. Larrea, F. Hong, S. A. Wander et al., “RSK1 drives p27Kip1 phosphorylation at T198 to promote RhoA inhibition and increase cell motility,” Proceedings of the National Academy of Sciences of the United States of America, vol. 106, no. 23, pp. 9268–9273, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. A. Van Opstal, J. J. M. Bijvelt, C. Margadant, and J. Boonstra, “Role of signal transduction and actin in G1 phase progression,” Advances in Enzyme Regulation, vol. 45, pp. 186–200, 2005. View at Publisher · View at Google Scholar · View at Scopus
  46. N. Kaji, A. Muramoto, and K. Mizuno, “LIM kinase-mediated cofilin phosphorylation during mitosis is required for precise spindle positioning,” Journal of Biological Chemistry, vol. 283, no. 8, pp. 4983–4992, 2008. View at Publisher · View at Google Scholar · View at Scopus
  47. F. F. Hsu, T. Y. Lin, J. Y. Chen, and S. Y. Shieh, “P53-mediated transactivation of LIMK2b links actin dynamics to cell cycle checkpoint control,” Oncogene, vol. 29, no. 19, pp. 2864–2876, 2010. View at Publisher · View at Google Scholar · View at Scopus
  48. M. Davila, D. Jhala, D. Ghosh, W. E. Grizzle, and R. Chakrabarti, “Expression of LIM kinase 1 is associated with reversible G1/S phase arrest, chromosomal instability and prostate cancer,” Molecular Cancer, vol. 6, article 40, 2007. View at Publisher · View at Google Scholar · View at Scopus
  49. A. Amiri, F. Noei, T. Feroz, and J. M. Lee, “Geldanamycin anisimycins activate rho and stimulate rho- and ROCK-dependent actin stress fiber formation,” Molecular Cancer Research, vol. 5, no. 9, pp. 933–942, 2007. View at Publisher · View at Google Scholar · View at Scopus
  50. Y.-P. Ho, C.-W. Kuo, Y.-T. Hsu et al., “β-Actin is a downstream effector of the PI3K/AKT signaling pathway in myeloma cells,” Molecular and Cellular Biochemistry, vol. 348, no. 1-2, pp. 129–139, 2011. View at Publisher · View at Google Scholar
  51. H. Chen, J. Bai, J. Ye et al., “JWA as a functional molecule to regulate cancer cells migration via MAPK cascades and F-actin cytoskeleton,” Cellular Signalling, vol. 19, no. 6, pp. 1315–1327, 2007. View at Publisher · View at Google Scholar · View at Scopus
  52. E. H. J. Danen, P. Sonneveld, A. Sonnenberg, and K. M. Yamada, “Dual stimulation of Ras/Mitogen-activated protein kinase and RhoA by cell adhesion to fibronectin supports growth factor-stimulated cell cycle progression,” Journal of Cell Biology, vol. 151, no. 7, pp. 1413–1422, 2000. View at Publisher · View at Google Scholar · View at Scopus
  53. B. Geiger, A. Bershadsky, R. Pankov, and K. M. Yamada, “Transmembrane extracellular matrix-cytoskeleton crosstalk,” Nature Reviews Molecular Cell Biology, vol. 2, no. 11, pp. 793–805, 2001. View at Publisher · View at Google Scholar · View at Scopus
  54. M. Maekawa, T. Ishizaki, S. Boku et al., “Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase,” Science, vol. 285, no. 5429, pp. 895–898, 1999. View at Publisher · View at Google Scholar · View at Scopus
  55. E. D. Schejter, “Actin organization in the early Drosophila embryo,” Novartis Foundation Symposium, vol. 269, pp. 127–138, 2005. View at Scopus
  56. K. Schwarzerova, Z. Vondrakova, L. Fischer et al., “The role of actin isoforms in somatic embryogenesis in Norway spruce,” BMC Plant Biology, vol. 10, article 89, 2010. View at Publisher · View at Google Scholar · View at Scopus
  57. D. L. Kropf, S. K. Berge, and R. S. Quatrano, “Actin localization during fucus embryogenesis,” Plant Cell, vol. 1, no. 2, pp. 191–200, 1989.
  58. M. Ma, L. Zhou, X. Guo et al., “Decreased cofilin1 expression is important for compaction during early mouse embryo development,” Biochimica et Biophysica Acta, vol. 1793, no. 12, pp. 1804–1810, 2009. View at Publisher · View at Google Scholar · View at Scopus
  59. J. R. Bamburg and G. S. Bloom, “Cytoskeletal pathologies of Alzheimer disease,” Cell Motility and the Cytoskeleton, vol. 66, no. 8, pp. 635–649, 2009. View at Publisher · View at Google Scholar · View at Scopus
  60. R. C. Davis, R. Furukawa, and M. Fechheimer, “A cell culture model for investigation of Hirano bodies,” Acta Neuropathologica, vol. 115, no. 2, pp. 205–217, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. L. S. Minamide, A. M. Striegl, J. A. Boyle, P. J. Meberg, and J. R. Bamburg, “Neurodegenerative stimuli induce persistent ADF/cofilin-actin rods that disrupt distal neurite function,” Nature Cell Biology, vol. 2, no. 9, pp. 628–636, 2000. View at Publisher · View at Google Scholar · View at Scopus
  62. M. E. Velasco, M. A. Smith, S. L. Siedlak, A. Nunomura, and G. Perry, “Striation is the characteristic neuritic abnormality in Alzheimer disease,” Brain Research, vol. 813, no. 2, pp. 329–333, 1998. View at Publisher · View at Google Scholar · View at Scopus
  63. M. T. Maloney and J. R. Bamburg, “Cofilin-mediated neurodegeneration in Alzheimer's disease and other amyloidopathies,” Molecular Neurobiology, vol. 35, no. 1, pp. 21–43, 2007. View at Publisher · View at Google Scholar · View at Scopus
  64. P. Garg, R. Verma, L. Cook et al., “Actin-depolymerizing factor cofilin-1 is necessary in maintaining mature podocyte architecture,” Journal of Biological Chemistry, vol. 285, no. 29, pp. 22676–22688, 2010. View at Publisher · View at Google Scholar · View at Scopus
  65. P. Mundel, J. Reiser, A. Z. M. Borja et al., “Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines,” Experimental Cell Research, vol. 236, no. 1, pp. 248–258, 1997. View at Publisher · View at Google Scholar · View at Scopus
  66. W. E. Smoyer and P. Mundel, “Regulation of podocyte structure during the development of nephrotic syndrome,” Journal of Molecular Medicine, vol. 76, no. 3-4, pp. 172–183, 1998. View at Publisher · View at Google Scholar · View at Scopus
  67. C. Faul, K. Asanuma, E. Yanagida-Asanuma, K. Kim, and P. Mundel, “Actin up: regulation of podocyte structure and function by components of the actin cytoskeleton,” Trends in Cell Biology, vol. 17, no. 9, pp. 428–437, 2007. View at Publisher · View at Google Scholar · View at Scopus
  68. P. Mundel and J. Reiser, “Proteinuria: an enzymatic disease of the podocyte,” Kidney International, vol. 77, no. 7, pp. 571–580, 2010. View at Publisher · View at Google Scholar · View at Scopus
  69. D. Kerjaschki, “Caught flat-footed: podocyte damage and the molecular bases of focal glomerulosclerosis,” Journal of Clinical Investigation, vol. 108, no. 11, pp. 1583–1587, 2001. View at Publisher · View at Google Scholar · View at Scopus
  70. S. Ashworth, B. Teng, J. Kaufeld et al., “Cofilin-1 inactivation leads to proteinuria—studies in zebrafish, mice and humans,” PLoS ONE, vol. 5, no. 9, Article ID e12626, pp. 1–10, 2010. View at Publisher · View at Google Scholar · View at Scopus
  71. J. M. Kaplan, S. H. Kim, K. N. North et al., “Mutations in ACTN4, encoding α-actinin-4, cause familial focal segmental glomerulosclerosis,” Nature Genetics, vol. 24, no. 3, pp. 251–256, 2000. View at Publisher · View at Google Scholar · View at Scopus
  72. M. Kestilä, U. Lenkkeri, M. Männikkö et al., “Positionally cloned gene for a novel glomerular protein—Nephrin—is mutated in congenital nephrotic syndrome,” Molecular Cell, vol. 1, no. 4, pp. 575–582, 1998. View at Scopus
  73. N. Boute, O. Gribouval, S. Roselli et al., “NPHS2, encoding the glomerular protein podocin, is mutated in autosomal recessive steroid-resistant nephrotic syndrome,” Nature Genetics, vol. 24, no. 4, pp. 349–354, 2000. View at Publisher · View at Google Scholar · View at Scopus
  74. J. Y. Rao and N. Li, “Microfilament actin remodeling as a potential target for cancer drug development,” Current Cancer Drug Targets, vol. 4, no. 4, pp. 345–354, 2004. View at Publisher · View at Google Scholar · View at Scopus
  75. T. T. Bonello, J. R. Stehn, and P. W. Gunning, “New approaches to targeting the actin cytoskeleton for chemotherapy,” Future Medicinal Chemistry, vol. 1, no. 7, pp. 1311–1331, 2009. View at Publisher · View at Google Scholar · View at Scopus
  76. D. H. Lee, G. B. Iwanski, and N. H. Thoennissen, “Cucurbitacin: ancient compound shedding new light on cancer treatment,” TheScientificWorldJournal, vol. 10, pp. 413–418, 2010. View at Publisher · View at Google Scholar · View at Scopus
  77. D. A. Knecht, R. A. LaFleur, A. W. Kahsai, C. E. Argueta, A. B. Beshir, and G. Fenteany, “Cucurbitacin I Inhibits cell motility by indirectly interfering with actin dynamics,” PLoS ONE, vol. 5, no. 11, Article ID e14039, 2010. View at Publisher · View at Google Scholar · View at Scopus
  78. T. Tannin-Spitz, S. Grossman, S. Dovrat, H. E. Gottlieb, and M. Bergman, “Growth inhibitory activity of cucurbitacin glucosides isolated from Citrullus colocynthis on human breast cancer cells,” Biochemical Pharmacology, vol. 73, no. 1, pp. 56–67, 2007. View at Publisher · View at Google Scholar · View at Scopus
  79. D. Yin, N. Wakimoto, H. Xing et al., “Cucurbitacin B markedly inhibits growth and rapidly affects the cytoskeleton in glioblastoma multiforme,” International Journal of Cancer, vol. 123, no. 6, pp. 1364–1375, 2008. View at Publisher · View at Google Scholar · View at Scopus
  80. K. L. K. Duncan, M. D. Duncan, M. C. Alley, and E. A. Sausville, “Cucurbitacin E-induced disruption of the actin and vimentin cytoskeleton in prostate carcinoma cells,” Biochemical Pharmacology, vol. 52, no. 10, pp. 1553–1560, 1996. View at Publisher · View at Google Scholar · View at Scopus
  81. K. A. El Sayed, M. A. Khanfar, H. M. Shallal et al., “Latrunculin A and its C-17-O-carbamates inhibit prostate tumor cell invasion and HIF-1 activation in breast tumor cells,” Journal of Natural Products, vol. 71, no. 3, pp. 396–402, 2008. View at Publisher · View at Google Scholar · View at Scopus
  82. J. I. Chao and H. F. Liu, “The blockage of survivin and securin expression increases the cytochalasin B-induced cell death and growth inhibition in human cancer cells,” Molecular Pharmacology, vol. 69, no. 1, pp. 154–164, 2006. View at Publisher · View at Google Scholar · View at Scopus
  83. H. Takeuchi, G. Ara, E. A. Sausville, and B. Teicher, “Jasplakinolide: interaction with radiation and hyperthermia in human prostate carcinoma and Lewis lung carcinoma,” Cancer Chemotherapy and Pharmacology, vol. 42, no. 6, pp. 491–496, 1998. View at Publisher · View at Google Scholar · View at Scopus
  84. K. Nagata-Ohashi, Y. Ohta, K. Goto et al., “A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia,” Journal of Cell Biology, vol. 165, no. 4, pp. 465–471, 2004. View at Publisher · View at Google Scholar · View at Scopus
  85. Y. J. Lee, T. J. Sheu, and P. C. Keng, “Enhancement of radiosensitivity in H1299 cancer cells by actin-associated protein cofilin,” Biochemical and Biophysical Research Communications, vol. 335, no. 2, pp. 286–291, 2005. View at Publisher · View at Google Scholar · View at Scopus
  86. P. Hotulainen, E. Paunola, M. K. Vartiainen, and P. Lappalainen, “Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells,” Molecular Biology of the Cell, vol. 16, no. 2, pp. 649–664, 2005. View at Publisher · View at Google Scholar · View at Scopus
  87. N. Zebda, O. Bernard, M. Bailly, S. Welti, D. S. Lawrence, and J. S. Condeelis, “Phosphorylation of ADF/cofilin abolishes EGF-induced actin nucleation at the leading edge and subsequent lamellipod extension,” Journal of Cell Biology, vol. 151, no. 5, pp. 1119–1127, 2000. View at Publisher · View at Google Scholar · View at Scopus
  88. B. V. McConnell, K. Koto, and A. Gutierrez-Hartmann, “Nuclear and cytoplasmic LIMK1 enhances human breast cancer progression,” Molecular Cancer, vol. 10, article 75, 2011. View at Publisher · View at Google Scholar
  89. D. H. Vlecken and C. P. Bagowski, “LIMK1 and LIMK2 are important for metastatic behavior and tumor cell-induced angiogenesis of pancreatic cancer cells,” Zebrafish, vol. 6, no. 4, pp. 433–439, 2009. View at Publisher · View at Google Scholar · View at Scopus
  90. K. Borensztajn, M. P. Peppelenbosch, and C. A. Spek, “Coagulation Factor Xa inhibits cancer cell migration via LIMK1-mediated cofilin inactivation,” Thrombosis Research, vol. 125, no. 6, pp. e323–e328, 2010. View at Publisher · View at Google Scholar · View at Scopus
  91. T. Ahmed, K. Shea, J. R. W. Masters, G. E. Jones, and C. M. Wells, “A PAK4-LIMK1 pathway drives prostate cancer cell migration downstream of HGF,” Cellular Signalling, vol. 20, no. 7, pp. 1320–1328, 2008. View at Publisher · View at Google Scholar · View at Scopus
  92. C. T. Yap, T. I. Simpson, T. Pratt, D. J. Price, and S. K. Maciver, “The motility of glioblastoma tumour cells is modulated by intracellular cofilin expression in a concentration-dependent manner,” Cell Motility and the Cytoskeleton, vol. 60, no. 3, pp. 153–165, 2005. View at Publisher · View at Google Scholar · View at Scopus
  93. J. Van Rheenen, X. Song, W. Van Roosmalen et al., “EGF-induced PIP2 hydrolysis releases and activates cofilin locally in carcinoma cells,” Journal of Cell Biology, vol. 179, no. 6, pp. 1247–1259, 2007. View at Publisher · View at Google Scholar · View at Scopus