Advertisement

Targeting cytoskeleton reorganisation as antimetastatic treatment

  • 150 Accesses

  • 12 Citations

Abstract

Metastatic relapse is responsible for 90% of cancer-related deaths. The process of distant spreading is a cascade of events that is regulated in a highly complex manner; one cellular phenomenon underlying all the events is cytoskeletal reorganisation. Despite the fact that the ability to leave the primary site and establish a viable mass in a distant site is a hallmark of cancer, targeting cytoskeletal reorganisation is an emerging field. In this review we describe the key signalling pathways controlling cytoskeletal reorganisation and the current targeted therapies against the “druggable” nodes. Finally, we discuss potential implications of trial design that can play a role in detecting the specific activity of this drug class.

This is a preview of subscription content, log in to check access.

Access options

Buy single article

Instant unlimited access to the full article PDF.

US$ 39.95

Price includes VAT for USA

Subscribe to journal

Immediate online access to all issues from 2019. Subscription will auto renew annually.

US$ 99

This is the net price. Taxes to be calculated in checkout.

References

  1. 1.

    Christofori G (2006) New signals from the invasive front. Nature 441:444–450

  2. 2.

    Llovet JM, Ricci S, Mazzaferro V et al (2008) Sorafenib in advanced hepatocellular carcinoma. N Engl J Med 359:378–390

  3. 3.

    Motzer RJ, Hutson TE, Tomczak P et al (2007) Sunitinib versus interferon alfa in metastatic renal-cell carcinoma. N Engl J Med 356:115–124

  4. 4.

    Miller K, Wang M, Gralow J et al (2007) Paclitaxel plus bevacizumab versus paclitaxel alone for metastatic breast cancer. N Engl J Med 357:2666–2676

  5. 5.

    Lynch TJ, Bell DW, Sordella R et al (2004) Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N Engl J Med 350:2129–2139

  6. 6.

    Druker BJ, Sawyers CL, Kantarjian H et al (2001) Activity of a specific inhibitor of the BCR-ABL tyrosine kinase in the blast crisis of chronic myeloid leukemia and acute lymphoblastic leukemia with the Philadelphia chromosome. N Engl J Med 344:1038–1042

  7. 7.

    Druker BJ, Talpaz M, Resta DJ et al (2001) Efficacy and safety of a specific inhibitor of the BCRABL tyrosine kinase in chronic myeloid leukemia. N Engl J Med 344:1031–1037

  8. 8.

    Chambers AF, Groom AC, MacDonald IC (2002) Dissemination and growth of cancer cells in metastatic sites. Nat Rev Cancer 2:563–572

  9. 9.

    Boyer B, Tucker GC, Valles AM et al (1989) Rearrangements of desmosomal and cytoskeletal proteins during the transition from epithelial to fibroblastoid organization in cultured rat bladder carcinoma cells. J Cell Biol 109:1495–1509

  10. 10.

    Wang W, Eddy R, Condeelis J (2007) The cofilin pathway in breast cancer invasion and metastasis. Nat Rev Cancer 7:429–440

  11. 11.

    Wang W, Wyckoff JB, Goswami S et al (2007) Coordinated regulation of pathways for enhanced cell motility and chemotaxis is conserved in rat and mouse mammary tumors. Cancer Res 67: 3505–3511

  12. 12.

    Wang W, Goswami S, Sahai E et al (2005) Tumor cells caught in the act of invading: their strategy for enhanced cell motility. Trends Cell Biol 15:138–145

  13. 13.

    Ono S (2007) Mechanism of depolymerization and severing of actin filaments and its significance in cytoskeletal dynamics. Int Rev Cytol 258:1–82

  14. 14.

    Maciver SK, Hussey PJ (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3:reviews3007

  15. 15.

    Ghosh M, Song X, Mouneimne G et al (2004) Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304:743–746

  16. 16.

    Hotulainen P, Paunola E, Vartiainen MK et al (2005) Actin-depolymerizing factor and cofilin-1 play overlapping roles in promoting rapid F-actin depolymerization in mammalian nonmuscle cells. Mol Biol Cell 16:649–664

  17. 17.

    Mogilner A, Oster G (2003) Polymer motors: pushing out the front and pulling up the back. Curr Biol 13:R721–733

  18. 18.

    dos Remedios CG, Chhabra D, Kekic M et al (2003) Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol Rev 83:433–473

  19. 19.

    Yamaguchi H, Lorenz M, Kempiak S et al (2005) Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J Cell Biol 168:441–452

  20. 20.

    Wang W, Mouneimne G, Sidani M et al (2006) The activity status of cofilin is directly related to invasion, intravasation, and metastasis of mammary tumors. J Cell Biol 173:395–404

  21. 21.

    Ichetovkin I, Han J, Pang KM et al (2000) Actin filaments are severed by both native and recombinant dictyostelium cofilin but to different extents. Cell Motil Cytoskeleton 45:293–306

  22. 22.

    Ichetovkin I, Grant W, Condeelis J (2002) Cofilin produces newly polymerized actin filaments that are preferred for dendritic nucleation by the Arp2/3 complex. Curr Biol 12:79–84

  23. 23.

    Andrianantoandro E, Pollard TD (2006) Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol Cell 24:13–23

  24. 24.

    Bamburg JR, Wiggan OP (2002) ADF/cofilin and actin dynamics in disease. Trends Cell Biol 12: 598–605

  25. 25.

    Dan C, Kelly A, Bernard O et al (2001) Cytoskeletal changes regulated by the PAK4 serine/threonine kinase are mediated by LIM kinase 1 and cofilin. J Biol Chem 276:32115–32121

  26. 26.

    Okano I, Hiraoka J, Otera H et al (1995) Identification and characterization of a novel family of serine/threonine kinases containing two N-terminal LIM motifs. J Biol Chem 270:31321–31330

  27. 27.

    Yang N, Higuchi O, Ohashi K et al (1998) Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393:809–812

  28. 28.

    Toshima J, Toshima JY, Takeuchi K et al (2001) Cofilin phosphorylation and actin reorganization activities of testicular protein kinase 2 and its predominant expression in testicular Sertoli cells. J Biol Chem 276:31449–31458

  29. 29.

    Toshima J, Toshima JY, Amano T et al (2001) Cofilin phosphorylation by protein kinase testicular protein kinase 1 and its role in integrin-mediated actin reorganization and focal adhesion formation. Mol Biol Cell 12:1131–1145

  30. 30.

    Niwa R, Nagata-Ohashi K, Takeichi M et al (2002) Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin. Cell 108:233–246

  31. 31.

    Meberg PJ, Ono S, Minamide LS et al (1998) Actin depolymerizing factor and cofilin phosphorylation dynamics: response to signals that regulate neurite extension. Cell Motil Cytoskeleton 39: 172–190

  32. 32.

    Ambach A, Saunus J, Konstandin M et al (2000) The serine phosphatases PP1 and PP2A associate with and activate the actin-binding protein cofilin in human T lymphocytes. Eur J Immunol 30:3422–3431

  33. 33.

    Gohla A, Birkenfeld J, Bokoch GM (2005) Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nat Cell Biol 7:21–29

  34. 34.

    Goldberg Y (1999) Protein phosphatase 2A: who shall regulate the regulator? Biochem Pharmacol 57:321–328

  35. 35.

    Janssens V, Goris J (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem J 353:417–439

  36. 36.

    Yonezawa N, Homma Y, Yahara I et al (1991) A short sequence responsible for both phosphoinositide binding and actin binding activities of cofilin. J Biol Chem 266:17218–17221

  37. 37.

    Yonezawa N, Nishida E, Iida K et al (1990) Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 265:8382–8386

  38. 38.

    Mouneimne G, DesMarais V, Sidani M et al (2006) Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr Biol 16:2193–2205

  39. 39.

    Devreotes P, Janetopoulos C (2003) Eukaryotic chemotaxis: distinctions between directional sensing and polarization. J Biol Chem 278:20445–20448

  40. 40.

    Schaller MD (2001) Biochemical signals and biological responses elicited by the focal adhesion kinase. Biochim Biophys Acta 1540:1–21

  41. 41.

    Hsia DA, Lim ST, Bernard-Trifilo JA et al (2005) Integrin alpha4beta1 promotes focal adhesion kinase-independent cell motility via alpha4 cytoplasmic domain-specific activation of c-Src. Mol Cell Biol 25:9700–9712

  42. 42.

    Mitra SK, Hanson DA, Schlaepfer DD (2005) Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6:56–68

  43. 43.

    Angelucci A, Bologna M (2007) Targeting vascular cell migration as a strategy for blocking angiogenesis: the central role of focal adhesion protein tyrosine kinase family. Curr Pharm Des 13:2129–2145

  44. 44.

    Schwock J, Dhani N, Hedley DW (2010) Targeting focal adhesion kinase signaling in tumor growth and metastasis. Expert Opin Ther Targets 14:77–94

  45. 45.

    Avizienyte E, Wyke AW, Jones RJ et al (2002) Src-induced de-regulation of E-cadherin in colon cancer cells requires integrin signalling. Nat Cell Biol 4:632–638

  46. 46.

    Cicchini C, Laudadio I, Citarella F et al (2008) TGFbeta-induced EMT requires focal adhesion kinase (FAK) signaling. Exp Cell Res 314:143–152

  47. 47.

    van Nimwegen MJ, Verkoeijen S, van Buren L et al (2005) Requirement for focal adhesion kinase in the early phase of mammary adenocarcinoma lung metastasis formation. Cancer Res 65:4698–4706

  48. 48.

    Mani SA, Guo W, Liao MJ et al (2008) The epithelial-mesenchymal transition generates cells with properties of stem cells. Cell 133:704–715

  49. 49.

    Luo M, Fan H, Nagy T et al (2009) Mammary epithelial-specific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells. Cancer Res 69:466–474

  50. 50.

    Luo M, Guan JL (2010) Focal adhesion kinase: a prominent determinant in breast cancer initiation, progression and metastasis. Cancer Lett 289:127–139

  51. 51.

    Slack-Davis JK, Martin KH, Tilghman RW et al (2007) Cellular characterization of a novel focal adhesion kinase inhibitor. J Biol Chem 282: 14845–14852

  52. 52.

    Roberts WG, Ung E, Whalen P et al (2008) Antitumor activity and pharmacology of a selective focal adhesion kinase inhibitor, PF-562,271. Cancer Res 68:1935–1944

  53. 53.

    Siu LL, Burris HA, Mileshkin L et al (2007) Phase I study of focal adhesion kinase (FAK) inhibitor PF-00562271 in patients (pts) with advanced solid tumors. J Clin Oncol 2007 ASCO Annual Meeting Proceedings Part I, Vol 25:3527

  54. 54.

    A study of PF-04554878 in patients with advanced non-hematologic malignancies (B0761001). http://clinicaltrials.gov/ct2/show/NCT00787033?term=FAK+inhibitor&rank=3

  55. 55.

    Beierle EA, Trujillo A, Nagaram A et al (2008) TAE226 inhibits human neuroblastoma cell survival. Cancer Invest 26:145–151

  56. 56.

    Golubovskaya VM, Virnig C, Cance WG (2008) TAE226-induced apoptosis in breast cancer cells with overexpressed Src or EGFR. Mol Carcinog 47:222–234

  57. 57.

    Sakurama K, Noma K, Takaoka M et al (2009) Inhibition of focal adhesion kinase as a potential therapeutic strategy for imatinib-resistant gastrointestinal stromal tumor. Mol Cancer Ther 8:127–134

  58. 58.

    Study of a focal adhesion kinase inhibitor in subjects with solid tumors. http://clinicaltrials.gov/ct2/show/NCT01138033?term=FAK+inhibitor&rank=1

  59. 59.

    Sieg DJ, Hauck CR, Ilic D et al (2000) FAK integrates growth-factor and integrin signals to promote cell migration. Nat Cell Biol 2:249–256

  60. 60.

    Carragher NO, Walker SM, Scott Carragher LA et al (2006) Calpain 2 and Src dependence distinguishes mesenchymal and amoeboid modes of tumour cell invasion: a link to integrin function. Oncogene 25:5726–5740

  61. 61.

    Biscardi JS, Tice DA, Parsons SJ (1999) c-Src, receptor tyrosine kinases, and human cancer. Adv Cancer Res 76:61–119

  62. 62.

    Jove R, Hanafusa H (1987) Cell transformation by the viral src oncogene. Annu Rev Cell Biol 3:31–56

  63. 63.

    Wang E, Goldberg AR (1976) Changes in microfilament organization and surface topography upon transformation of chick embryo fibroblasts with Rous sarcoma virus. Proc Natl Acad Sci U S A 73:4065–4069

  64. 64.

    Parsons JT, Weber MJ (1989) Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr Top Microbiol Immunol 147:79–127

  65. 65.

    Bjorge JD, Jakymiw A, Fujita DJ (2000) Selected glimpses into the activation and function of Src kinase. Oncogene 19:5620–5635

  66. 66.

    Laukaitis CM, Webb DJ, Donais K et al (2001) Differential dynamics of alpha 5 integrin, paxillin, and alpha-actinin during formation and disassembly of adhesions in migrating cells. J Cell Biol 153:1427–1440

  67. 67.

    Guarino M (2010) Src signaling in cancer invasion. J Cell Physiol 223:14–26

  68. 68.

    Guarino M (1995) Epithelial-to-mesenchymal change of differentiation. From embryogenetic mechanism to pathological patterns. Histol Histopathol 10:171–184

  69. 69.

    Guarino M (2007) Epithelial-mesenchymal transition and tumour invasion. Int J Biochem Cell Biol 39:2153–2160

  70. 70.

    Guarino M, Rubino B, Ballabio G (2007) The role of epithelial-mesenchymal transition in cancer pathology. Pathology 39:305–318

  71. 71.

    Behrens J, Vakaet L, Friis R et al (1993) Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature-sensitive v-SRC gene. J Cell Biol 120:757–766

  72. 72.

    Niu G, Bowman T, Huang M et al (2002) Roles of activated Src and Stat3 signaling in melanoma tumor cell growth. Oncogene 21:7001–7010

  73. 73.

    Malek RL, Irby RB, Guo QM et al (2002) Identification of Src transformation fingerprint in human colon cancer. Oncogene 21:7256–7265

  74. 74.

    Blake RA, Broome MA, Liu X et al (2000) SU6656, a selective src family kinase inhibitor, used to probe growth factor signaling. Mol Cell Biol 20:9018–9027

  75. 75.

    Sekharam M, Nasir A, Kaiser HE et al (2003) Insulin-like growth factor 1 receptor activates c-SRC and modifies transformation and motility of colon cancer in vitro. Anticancer Res 23:1517–1524

  76. 76.

    Kim LC, Song L, Haura EB (2009) Src kinases as therapeutic targets for cancer. Nat Rev Clin Oncol 6:587–595

  77. 77.

    Talpaz M, Shah NP, Kantarjian H et al (2006) Dasatinib in imatinib-resistant Philadelphia chromosome-positive leukemias. N Engl J Med 354: 2531–2541

  78. 78.

    Shah NP, Tran C, Lee FY et al (2004) Overriding imatinib resistance with a novel ABL kinase inhibitor. Science 305:399–401

  79. 79.

    Lindauer M, Hochhaus A (2010) Dasatinib. Recent Results Cancer Res 184:83–102

  80. 80.

    Trevino JG, Summy JM, Lesslie DP et al (2006) Inhibition of SRC expression and activity inhibits tumor progression and metastasis of human pancreatic adenocarcinoma cells in an orthotopic nude mouse model. Am J Pathol 168:962–972

  81. 81.

    Shor AC, Keschman EA, Lee FY et al (2007) Dasatinib inhibits migration and invasion in diverse human sarcoma cell lines and induces apoptosis in bone sarcoma cells dependent on SRC kinase for survival. Cancer Res 67:2800–2808

  82. 82.

    Tsao AS, He D, Saigal B et al (2007) Inhibition of c-Src expression and activation in malignant pleural mesothelioma tissues leads to apoptosis, cell cycle arrest, and decreased migration and invasion. Mol Cancer Ther 6:1962–1972

  83. 83.

    Timeus F, Crescenzio N, Fandi A et al (2008) In vitro antiproliferative and antimigratory activity of dasatinib in neuroblastoma and Ewing sarcoma cell lines. Oncol Rep 19:353–359

  84. 84.

    Park SI, Zhang J, Phillips KA et al (2008) Targeting SRC family kinases inhibits growth and lymph node metastases of prostate cancer in an orthotopic nude mouse model. Cancer Res 68:3323–3333

  85. 85.

    Pichot CS, Hartig SM, Xia L et al (2009) Dasatinib synergizes with doxorubicin to block growth, migration, and invasion of breast cancer cells. Br J Cancer 101:38–47

  86. 86.

    Choi YL, Bocanegra M, Kwon MJ et al (2010) LYN is a mediator of epithelial-mesenchymal transition and a target of dasatinib in breast cancer. Cancer Res 70:2296–2306

  87. 87.

    Zhang XH, Wang Q, Gerald W et al (2009) Latent bone metastasis in breast cancer tied to Src-dependent survival signals. Cancer Cell 16:67–78

  88. 88.

    Herynk MH, Beyer AR, Cui Y et al (2006) Cooperative action of tamoxifen and c-Src inhibition in preventing the growth of estrogen receptor-positive human breast cancer cells. Mol Cancer Ther 5:3023–3031

  89. 89.

    Golas JM, Lucas J, Etienne C et al (2005) SKI-606, a Src/Abl inhibitor with in vivo activity in colon tumor xenograft models. Cancer Res 65:5358–5364

  90. 90.

    Messersmith WA, Krishnamurthi S, Hewes BA et al (2007) Bosutinib (SKI-606), a dual Src/Abl tyrosine kinase inhibitor: preliminary results from a phase 1 study in patients with advanced malignant solid tumors. J Clin Oncol 2007 ASCO Annual Meeting Proceedings 25(18S):3552

  91. 91.

    Lara PN Jr, Longmate J, Evans CP et al (2009) A phase II trial of the Src-kinase inhibitor AZD0530 in patients with advanced castration-resistant prostate cancer: a California Cancer Consortium study. Anticancer Drugs 20:179–184

  92. 92.

    Haura EB, Tanvetyanon T, Chiappori A et al (2010) Phase I/II study of the Src inhibitor dasatinib in combination with erlotinib in advanced non-small-cell lung cancer. J Clin Oncol 28:1387–94

  93. 93.

    Miller AA, Pang H, Hodgson L et al (2010) A phase II study of dasatinib in patients with chemosensitive relapsed small cell lung cancer (Cancer and Leukemia Group B 30602). J Thorac Oncol 5:380–384

  94. 94.

    Yu EY, Wilding G, Posadas E et al (2009) Phase II study of dasatinib in patients with metastatic castration-resistant prostate cancer. Clin Cancer Res 15:7421–7428

  95. 95.

    Schenone S, Manetti F, Botta M (2007) Synthetic SRC-kinase domain inhibitors and their structural requirements. Anticancer Agents Med Chem 7:660–680

  96. 96.

    Frank C, Burkhardt C, Imhof D et al (2004) Effective dephosphorylation of Src substrates by SHP-1. J Biol Chem 279:11375–11383

  97. 97.

    Ye G, Tiwari R, Parang K (2008) Development of Src tyrosine kinase substrate binding site inhibitors. Curr Opin Investig Drugs 9:605–613

  98. 98.

    Lau GM, Yu GL, Gelman IH et al (2009) Expression of Src and FAK in hepatocellular carcinoma and the effect of Src inhibitors on hepatocellular carcinoma in vitro. Dig Dis Sci 54: 1465–1474

  99. 99.

    KX2-391 in treating patients with advanced solid tumors or lymphoma that did not tespond to treatment. http://clinicaltrials.gov/ct2/show/NCT00646139?term=KX2-391&rank=2

  100. 100.

    Evaluation of KX2-391 in patients with advanced malignancies. http://clinicaltrials.gov/ct2/show/NCT00658970?term=KX2-391&rank=3

  101. 101.

    A safety and efficacy study of KX2-391 in patients with bone-metastatic, castration-resistant prostate cancer who have not received prior chemotherapy. http://clinicaltrials.gov/ct2/show/NCT01074138?term=KX2-391&rank=1

  102. 102.

    Riento K, Ridley AJ (2003) Rocks: multifunctional kinases in cell behaviour. Nat Rev Mol Cell Biol 4:446–456

  103. 103.

    Takayasu M, Suzuki Y, Shibuya M et al (1986) The effects of HA compound calcium antagonists on delayed cerebral vasospasm in dogs. J Neurosurg 65:80–85

  104. 104.

    Ying H, Biroc SL, Li WW et al (2006) The Rho kinase inhibitor fasudil inhibits tumor progression in human and rat tumor models. Mol Cancer Ther 5:2158–2164

  105. 105.

    Yin L, Morishige K, Takahashi T et al (2007) Fasudil inhibits vascular endothelial growth factorinduced angiogenesis in vitro and in vivo. Mol Cancer Ther 6:1517–1525

  106. 106.

    Yang X, Liu Y, Zong Z et al (2010) The Rho kinase inhibitor fasudil inhibits the migratory behaviour of 95-D lung carcinoma cells. Biomed Pharmacother 64:58–62

  107. 107.

    Ogata S, Morishige K, Sawada K et al (2009) Fasudil inhibits lysophosphatidic acid-induced invasiveness of human ovarian cancer cells. Int J Gynecol Cancer 19:1473–1480

  108. 108.

    Deng L, Li G, Li R et al (2010) Rho-kinase inhibitor, fasudil, suppresses glioblastoma cell line progression in vitro and in vivo. Cancer Biol Ther 9:875–884

  109. 109.

    Mahlamaki EH, Kauraniemi P, Monni O et al (2004) High-resolution genomic and expression profiling reveals 105 putative amplification target genes in pancreatic cancer. Neoplasia 6: 432–439

  110. 110.

    Kim JH, Kim HN, Lee KT et al (2008) Gene expression profiles in gallbladder cancer: the close genetic similarity seen for early and advanced gallbladder cancers may explain the poor prognosis. Tumour Biol 29:41–49

  111. 111.

    Wells CM, Abo A, Ridley AJ (2002) PAK4 is activated via PI3K in HGF-stimulated epithelial cells. J Cell Sci 115:3947–3956

  112. 112.

    Eswaran J, Soundararajan M, Knapp S (2009) Targeting group II PAKs in cancer and metastasis. Cancer Metastasis Rev 28:209–217

  113. 113.

    Callow MG, Clairvoyant F, Zhu S et al (2002) Requirement for PAK4 in the anchorage-independent growth of human cancer cell lines. J Biol Chem 277:550–558

  114. 114.

    Murray BW, Guo C, Piraino J et al (2010) Smallmolecule p21-activated kinase inhibitor PF-3758309 is a potent inhibitor of oncogenic signaling and tumor growth. Proc Natl Acad Sci U S A 107:9446–9451

  115. 115.

    This is the first study using escalating doses of PF-03758309, an oral compound, in patients with advanced solid tumors. http://clinicaltrials.gov/ct2/show/NCT00932126?term=PAK4&rank=1

  116. 116.

    Quintela-Fandino M, Arpaia E, Brenner D et al (2010) HUNK suppresses metastasis of basal type breast cancers by disrupting the interaction between PP2A and cofilin-1. Proc Natl Acad Sci U S A 107:2622–2627

Download references

Author information

Correspondence to Miguel Quintela-Fandino.

Rights and permissions

Reprints and Permissions

About this article

Cite this article

Quintela-Fandino, M., González-Martín, A. & Colomer, R. Targeting cytoskeleton reorganisation as antimetastatic treatment. Clin Transl Oncol 12, 662–669 (2010) doi:10.1007/s12094-010-0575-8

Download citation

Keywords

  • Metastasis
  • Cytoskeleton reorganization
  • FAK
  • Src
  • Cofilin
  • Actin polymerization