Table of Contents
Journal of Signal Transduction
Volume 2012 (2012), Article ID 296450, 12 pages
http://dx.doi.org/10.1155/2012/296450
Review Article

Focal Adhesion Kinases in Adhesion Structures and Disease

Department of Oral Biology, Indiana University School of Dentistry, DS241, 1121 W. Michigan Street, Indianapolis, IN 46202, USA

Received 23 March 2012; Revised 25 May 2012; Accepted 31 May 2012

Academic Editor: Donna Webb

Copyright © 2012 Pierre P. Eleniste and Angela Bruzzaniti. 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. E. Hohenester and J. Engel, “Domain structure and organisation in extracellular matrix proteins,” Matrix Biology, vol. 21, no. 2, pp. 115–128, 2002. View at Publisher · View at Google Scholar · View at Scopus
  2. R. O. Hynes, “The extracellular matrix: not just pretty fibrils,” Science, vol. 326, no. 5957, pp. 1216–1219, 2009. View at Publisher · View at Google Scholar · View at Scopus
  3. P. D. Yurchenco and B. L. Patton, “Developmental and pathogenic mechanisms of basement membrane assembly,” Current Pharmaceutical Design, vol. 15, no. 12, pp. 1277–1294, 2009. View at Publisher · View at Google Scholar · View at Scopus
  4. 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
  5. H. C. Slavkin, “Combinatorial process for extracellular matrix influences on gene expression: a hypothesis,” Journal of Craniofacial Genetics and Developmental Biology, vol. 2, no. 2, pp. 179–189, 1982. View at Google Scholar · View at Scopus
  6. K. T. Chan, C. L. Cortesio, and A. Huttenlocher, “Fak alters invadopodia and focal adhesion composition and dynamics to regulate breast cancer invasion,” The Journal of Cell Biology, vol. 185, no. 2, pp. 357–370, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. E. D. Hay, “Extracellular matrix,” The Journal of Cell Biology, vol. 91, no. 3, part 2, pp. 205s–223s, 1981. View at Google Scholar · View at Scopus
  8. C. H. Damsky, “Extracellular matrix-integrin interactions in osteoblast function and tissue remodeling,” Bone, vol. 25, no. 1, pp. 95–96, 1999. View at Publisher · View at Google Scholar · View at Scopus
  9. A. De Arcangelis and E. Georges-Labouesse, “Integrin and ECM functions: roles in vertebrate development,” Trends in Genetics, vol. 16, no. 9, pp. 389–395, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Abercrombie, J. E. M. Heaysman, and S. M. Pegrum, “The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella,” Experimental Cell Research, vol. 67, no. 2, pp. 359–367, 1971. View at Google Scholar · View at Scopus
  11. M. A. Wozniak, K. Modzelewska, L. Kwong, and P. J. Keely, “Focal adhesion regulation of cell behavior,” Biochimica et Biophysica Acta, vol. 1692, no. 2-3, pp. 103–119, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. R. O. Hynes, “Integrins: versatility, modulation, and signaling in cell adhesion,” Cell, vol. 69, no. 1, pp. 11–25, 1992. View at Publisher · View at Google Scholar · View at Scopus
  13. M. A. Schwartz, M. D. Schaller, and M. H. Ginsberg, “Integrins: emerging paradigms of signal transduction,” Annual Review of Cell and Developmental Biology, vol. 11, pp. 549–599, 1995. View at Google Scholar · View at Scopus
  14. L. H. Romer, K. G. Birukov, and J. G. N. Garcia, “Focal adhesions: paradigm for a signaling nexus,” Circulation Research, vol. 98, no. 5, pp. 606–616, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. R. Zaidel-Bar, S. Itzkovitz, A. Ma'ayan, R. Iyengar, and B. Geiger, “Functional atlas of the integrin adhesome,” Nature Cell Biology, vol. 9, no. 8, pp. 858–867, 2007. View at Publisher · View at Google Scholar · View at Scopus
  16. E. Zamir and B. Geiger, “Components of cell-matrix adhesions,” Journal of Cell Science, vol. 114, no. 20, pp. 3577–3579, 2001. View at Google Scholar · View at Scopus
  17. Q. S. Du, X. R. Ren, Y. Xie, Q. Wang, L. Mei, and W. C. Xiong, “Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK,” Journal of Cell Science, vol. 114, no. 16, pp. 2977–2987, 2001. View at Google Scholar · View at Scopus
  18. D. Ilic, Y. Furuta, S. Kanazawa et al., “Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice,” Nature, vol. 377, no. 6549, pp. 539–544, 1995. View at Google Scholar · View at Scopus
  19. H. B. Wang, M. Dembo, S. K. Hanks, and Y. L. Wang, “Focal adhesion kinase is involved in mechanosensing during fibroblast migration,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 20, pp. 11295–11300, 2001. View at Publisher · View at Google Scholar · View at Scopus
  20. D. M. Suter and P. Forscher, “Transmission of growth cone traction force through apCAM-cytoskeletal linkages is regulated by Src family tyrosine kinase activity,” The Journal of Cell Biology, vol. 155, no. 4, pp. 427–438, 2001. View at Google Scholar · View at Scopus
  21. M. C. Frame, V. J. Fincham, N. O. Carragher, and J. A. Wyke, “v-Src's hold over actin and cell adhesions,” Nature Reviews Molecular Cell Biology, vol. 3, no. 4, pp. 233–245, 2002. View at Publisher · View at Google Scholar · View at Scopus
  22. E. Zamir and B. Geiger, “Molecular complexity and dynamics of cell-matrix adhesions,” Journal of Cell Science, vol. 114, no. 20, pp. 3583–3590, 2001. View at Google Scholar · View at Scopus
  23. C. Grashoff, I. Thievessen, K. Lorenz, S. Ussar, and R. Fässler, “Integrin-linked kinase: integrin's mysterious partner,” Current Opinion in Cell Biology, vol. 16, no. 5, pp. 565–571, 2004. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Angers-Loustau, J. F. Côté, A. Charest et al., “Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts,” The Journal of Cell Biology, vol. 144, no. 5, pp. 1019–1031, 1999. View at Publisher · View at Google Scholar · View at Scopus
  25. A. Bourdeau, N. Dubé, and M. L. Tremblay, “Cytoplasmic protein tyrosine phosphatases, regulation and function: the roles of PTP1B and TC-PTP,” Current Opinion in Cell Biology, vol. 17, no. 2, pp. 203–209, 2005. View at Publisher · View at Google Scholar · View at Scopus
  26. C. E. Turner, “Paxillin and focal adhesion signalling,” Nature Cell Biology, vol. 2, no. 12, pp. E231–E236, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. H. Yano, H. Uchida, T. Iwasaki et al., “Paxillin α and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 97, no. 16, pp. 9076–9081, 2000. View at Publisher · View at Google Scholar · View at Scopus
  28. K. A. DeMali, C. A. Barlow, and K. Burridge, “Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion,” The Journal of Cell Biology, vol. 159, no. 5, pp. 881–891, 2002. View at Publisher · View at Google Scholar · View at Scopus
  29. I. D. Campbell and M. H. Ginsberg, “The talin-tail interaction places integrin activation on FERM ground,” Trends in Biochemical Sciences, vol. 29, no. 8, pp. 429–435, 2004. View at Publisher · View at Google Scholar · View at Scopus
  30. D. R. Critchley, “Genetic, biochemical and structural approaches to talin function,” Biochemical Society Transactions, vol. 33, no. 6, pp. 1308–1312, 2005. View at Publisher · View at Google Scholar · View at Scopus
  31. S. H. Lo, “Tensin,” The International Journal of Biochemistry and Cell Biology, vol. 36, no. 1, pp. 31–34, 2004. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Wang, H. Cao, J. Chen, and M. A. McNiven, “A direct interaction between the large GTPase dynamin-2 and FAK regulates focal adhesion dynamics in response to active Src,” Molecular Biology of the Cell, vol. 22, no. 9, pp. 1529–1538, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. C. D. Nobes and A. Hall, “Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia,” Cell, vol. 81, no. 1, pp. 53–62, 1995. View at Google Scholar · View at Scopus
  34. K. Burridge and K. Wennerberg, “Rho and Rac take center stage,” Cell, vol. 116, no. 2, pp. 167–179, 2004. View at Publisher · View at Google Scholar · View at Scopus
  35. L. A. Cary, D. C. Han, T. R. Polte, S. K. Hanks, and J. L. Guan, “Identification of p130(Cas) as a mediator of focal adhesion kinase-promoted cell migration,” The Journal of Cell Biology, vol. 140, no. 1, pp. 211–221, 1998. View at Publisher · View at Google Scholar · View at Scopus
  36. B. Geiger, J. P. Spatz, and A. D. Bershadsky, “Environmental sensing through focal adhesions,” Nature Reviews Molecular Cell Biology, vol. 10, no. 1, pp. 21–33, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. S. K. Mitra, D. A. Hanson, and D. D. Schlaepfer, “Focal adhesion kinase: in command and control of cell motility,” Nature Reviews Molecular Cell Biology, vol. 6, no. 1, pp. 56–68, 2005. View at Publisher · View at Google Scholar · View at Scopus
  38. J. D. Hildebrand, M. D. Schaller, and J. T. Parsons, “Identification of sequences required for the efficient localization of the focal adhesion kinase, pp125(FAK), to cellular focal adhesions,” The Journal of Cell Biology, vol. 123, no. 4, pp. 993–1005, 1993. View at Publisher · View at Google Scholar · View at Scopus
  39. J. W. Thomas, M. A. Cooley, J. M. Broome et al., “The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin,” The Journal of Biological Chemistry, vol. 274, no. 51, pp. 36684–36692, 1999. View at Publisher · View at Google Scholar · View at Scopus
  40. M. D. Schaller, C. A. Otey, J. D. Hildebrand, and J. T. Parsons, “Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains,” The Journal of Cell Biology, vol. 130, no. 5, pp. 1181–1187, 1995. View at Publisher · View at Google Scholar · View at Scopus
  41. I. Eke, Y. Deuse, S. Hehlgans et al., “β(1) Integrin/FAK/cortactin signaling is essential for human head and neck cancer resistance to radiotherapy,” The Journal of Clinical Investigation, vol. 122, no. 4, pp. 1529–1540, 2012. View at Publisher · View at Google Scholar
  42. M. G. Yeo, M. A. Partridge, E. J. Ezratty, Q. Shen, G. G. Gundersen, and E. E. Marcantonio, “Src SH2 arginine 175 is required for cell motility: specific focal adhesion kinase targeting and focal adhesion assembly function,” Molecular and Cellular Biology, vol. 26, no. 12, pp. 4399–4409, 2006. View at Publisher · View at Google Scholar · View at Scopus
  43. E. J. Ezratty, M. A. Partridge, and G. G. Gundersen, “Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase,” Nature Cell Biology, vol. 7, no. 6, pp. 581–590, 2005. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Bruzzaniti, L. Neff, A. Sanjay, W. C. Horne, P. De Camilli, and R. Baron, “Dynamin forms a Src kinase-sensitive complex with Cbl and regulates podosomes and osteoclast activity,” Molecular Biology of the Cell, vol. 16, no. 7, pp. 3301–3313, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. A. Bruzzaniti, L. Neff, A. Sandoval, L. Du, W. C. Horne, and R. Baron, “Dynamin reduces Pyk2 Y402 phosphorylation and Src binding in osteoclasts,” Molecular and Cellular Biology, vol. 29, no. 13, pp. 3644–3656, 2009. View at Publisher · View at Google Scholar · View at Scopus
  46. P. A. Amato, E. R. Unanue, and D. L. Taylor, “Distribution of actin in spreading macrophages: a comparative study on living and fixed cells,” The Journal of Cell Biology, vol. 96, no. 3, pp. 750–761, 1983. View at Google Scholar · View at Scopus
  47. P. C. Marchisio, D. Cirillo, L. Naldini, M. V. Primavera, A. Teti, and A. Zambonin-Zallone, “Cell-substratum interaction of cultured avian osteoclasts is mediated by specific adhesion structures,” The Journal of Cell Biology, vol. 99, no. 5, pp. 1696–1705, 1984. View at Google Scholar · View at Scopus
  48. J. Wang, Y. Taba, J. Pang, G. Yin, C. Yan, and B. C. Berk, “GIT1 mediates vegf-induced podosome formation in endothelial cells. Critical role for PLCγ,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 29, no. 2, pp. 202–208, 2009. View at Publisher · View at Google Scholar · View at Scopus
  49. S. Linder, K. Hufner, U. Wintergerst, and M. Aefelbacher, “Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages,” Journal of Cell Science, vol. 113, no. 23, pp. 4165–4176, 2000. View at Google Scholar · View at Scopus
  50. O. Destaing, F. Saltel, J. C. Géminard, P. Jurdic, and F. Bard, “Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein,” Molecular Biology of the Cell, vol. 14, no. 2, pp. 407–416, 2003. View at Publisher · View at Google Scholar · View at Scopus
  51. K. Mizutani, H. Miki, H. He, H. Maruta, and T. Takenawa, “Essential role of neural Wiskott-Aldrich syndrome protein in podosome formation and degradation of extracellular matrix in Src-transformed fibroblasts,” Cancer Research, vol. 62, no. 3, pp. 669–674, 2002. View at Google Scholar · View at Scopus
  52. H. M. Kocher, J. Sandle, T. A. Mirza, N. F. Li, and I. R. Hart, “Ezrin interacts with cortactin to form podosomal rosettes in pancreatic cancer cells,” Gut, vol. 58, no. 2, pp. 271–284, 2009. View at Publisher · View at Google Scholar · View at Scopus
  53. W. T. Chen, “Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells,” Journal of Experimental Zoology, vol. 251, no. 2, pp. 167–185, 1989. View at Google Scholar · View at Scopus
  54. G. Tarone, D. Cirillo, and F. G. Giancotti, “Rous-sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes,” Experimental Cell Research, vol. 159, no. 1, pp. 141–157, 1985. View at Google Scholar · View at Scopus
  55. V. V. Artym, Y. Zhang, F. Seillier-Moiseiwitsch, K. M. Yamada, and S. C. Mueller, “Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function,” Cancer Research, vol. 66, no. 6, pp. 3034–3043, 2006. View at Publisher · View at Google Scholar · View at Scopus
  56. E. S. Clark, A. S. Whigham, W. G. Yarbrough, and A. M. Weaver, “Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia,” Cancer Research, vol. 67, no. 9, pp. 4227–4235, 2007. View at Publisher · View at Google Scholar · View at Scopus
  57. S. Linder and P. Kopp, “Podosomes at a glance,” Journal of Cell Science, vol. 118, no. 10, pp. 2079–2082, 2005. View at Publisher · View at Google Scholar · View at Scopus
  58. M. Gimona, R. Buccione, S. A. Courtneidge, and S. Linder, “Assembly and biological role of podosomes and invadopodia,” Current Opinion in Cell Biology, vol. 20, no. 2, pp. 235–241, 2008. View at Publisher · View at Google Scholar · View at Scopus
  59. D. A. Murphy and S. A. Courtneidge, “The “ins” and “outs” of podosomes and invadopodia: characteristics, formation and function,” Nature Reviews Molecular Cell Biology, vol. 12, no. 7, pp. 413–426, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. M. R. Block, C. Badowski, A. Millon-Fremillon et al., “Podosome-type adhesions and focal adhesions, so alike yet so different,” European Journal of Cell Biology, vol. 87, no. 8-9, pp. 491–506, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. P. Jurdic, F. Saltel, A. Chabadel, and O. Destaing, “Podosome and sealing zone: specificity of the osteoclast model,” European Journal of Cell Biology, vol. 85, no. 3-4, pp. 195–202, 2006. View at Publisher · View at Google Scholar · View at Scopus
  62. R. Buccione, J. D. Orth, and M. A. McNiven, “Foot and mouth: podosomes, invadopodia and circular dorsal ruffles,” Nature Reviews Molecular Cell Biology, vol. 5, no. 8, pp. 647–657, 2004. View at Publisher · View at Google Scholar · View at Scopus
  63. M. A. McNiven, M. Baldassarre, and R. Buccione, “The role of dynamin in the assembly and function of podosomes and invadopodia,” Frontiers in Bioscience, vol. 9, pp. 1944–1953, 2004. View at Google Scholar · View at Scopus
  64. H. Gil-Henn, O. Destaing, N. A. Sims et al., “Defective microtubule-dependent podosome organization in osteoclasts leads to increased bone density in Pyk2-/- mice,” The Journal of Cell Biology, vol. 178, no. 6, pp. 1053–1064, 2007. View at Publisher · View at Google Scholar · View at Scopus
  65. Y. Furuta, D. Ilic, S. Kanazawa, N. Takeda, T. Yamamoto, and S. Aizawa, “Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK,” Oncogene, vol. 11, no. 10, pp. 1989–1995, 1995. View at Google Scholar · View at Scopus
  66. M. Pfaff and P. Jurdic, “Podosomes in osteoclast-like cells: structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase 2 (Pyk2) and integrin αVβ3,” Journal of Cell Science, vol. 114, no. 15, pp. 2775–2786, 2001. View at Google Scholar · View at Scopus
  67. V. Betapudi, “Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading,” PLoS ONE, vol. 5, no. 1, Article ID e8560, 2010. View at Publisher · View at Google Scholar · View at Scopus
  68. T. Sato, M. D. C. Ovejero, P. Hou et al., “Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts,” Journal of Cell Science, vol. 110, no. 5, pp. 589–596, 1997. View at Google Scholar · View at Scopus
  69. S. Burns, A. J. Thrasher, M. P. Blundell, L. Machesky, and G. E. Jones, “Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation,” Blood, vol. 98, no. 4, pp. 1142–1149, 2001. View at Publisher · View at Google Scholar · View at Scopus
  70. C. Itzstein, F. P. Coxon, and M. J. Rogers, “The regulation of osteoclast function and bone resorption by small GTPases,” Small GTPases, vol. 2, no. 3, pp. 117–130, 2011. View at Google Scholar · View at Scopus
  71. S. F. G. van Helden and P. L. Hordijk, “Podosome regulation by Rho GTPases in myeloid cells,” European Journal of Cell Biology, vol. 90, no. 2-3, pp. 189–197, 2011. View at Publisher · View at Google Scholar · View at Scopus
  72. S. Ory, H. Brazier, G. Pawlak, and A. Blangy, “Rho GTPases in osteoclasts: orchestrators of podosome arrangement,” European Journal of Cell Biology, vol. 87, no. 8-9, pp. 469–477, 2008. View at Publisher · View at Google Scholar · View at Scopus
  73. G. Giannone, G. Jiang, D. H. Sutton, D. R. Critchley, and M. P. Sheetz, “Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation,” The Journal of Cell Biology, vol. 163, no. 2, pp. 409–419, 2003. View at Publisher · View at Google Scholar · View at Scopus
  74. V. V. Artym, K. M. Yamada, and S. C. Mueller, “ECM degradation assays for analyzing local cell invasion,” Methods in Molecular Biology, vol. 522, pp. 211–219, 2009. View at Google Scholar · View at Scopus
  75. J. M. Delaissé, M. T. Engsig, V. Everts et al., “Proteinases in bone resorption: obvious and less obvious roles,” Clinica Chimica Acta, vol. 291, no. 2, pp. 223–234, 2000. View at Publisher · View at Google Scholar · View at Scopus
  76. S. Linder and M. Aepfelbacher, “Podosomes: adhesion hot-spots of invasive cells,” Trends in Cell Biology, vol. 13, no. 7, pp. 376–385, 2003. View at Publisher · View at Google Scholar · View at Scopus
  77. S. Hu, E. Planus, D. Georgess et al., “Podosome rings generate forces that drive saltatory osteoclast migration,” Molecular Biology of the Cell, vol. 22, no. 17, pp. 3120–3126, 2011. View at Publisher · View at Google Scholar
  78. I. Dikic, G. Tokiwa, S. Lev, S. A. Courtneidge, and J. Schlessinger, “A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation,” Nature, vol. 383, no. 6600, pp. 547–550, 1996. View at Publisher · View at Google Scholar · View at Scopus
  79. H. Avraham, S. Y. Park, K. Schinkmann, and S. Avraham, “RAFTK/Pyk2-mediated cellular signalling,” Cellular Signalling, vol. 12, no. 3, pp. 123–133, 2000. View at Publisher · View at Google Scholar · View at Scopus
  80. D. Davidson and A. Veillette, “PTP-PEST, a scaffold protein tyrosine phosphatase, negatively regulates lymphocyte activation by targeting a unique set of substrates,” The EMBO Journal, vol. 20, no. 13, pp. 3414–3426, 2001. View at Publisher · View at Google Scholar · View at Scopus
  81. Y. Shen, G. Schneider, J. F. Cloutier, A. Veillette, and M. D. Schaller, “Direct association of protein-tyrosine phosphatase PTP-PEST with paxillin,” The Journal of Biological Chemistry, vol. 273, no. 11, pp. 6474–6481, 1998. View at Publisher · View at Google Scholar · View at Scopus
  82. C. E. Turner, “Paxillin interactions,” Journal of Cell Science, vol. 113, no. 23, pp. 4139–4140, 2000. View at Google Scholar · View at Scopus
  83. S. Avraham, R. London, Y. Fu et al., “Identification and characterization of a novel related adhesion focal tyrosine kinase (RAFTK) from megakaryocytes and brain,” The Journal of Biological Chemistry, vol. 270, no. 46, pp. 27742–27751, 1995. View at Publisher · View at Google Scholar · View at Scopus
  84. L. Buckbinder, D. T. Crawford, H. Qi et al., “Proline-rich tyrosine kinase 2 regulates osteoprogenitor cells and bone formation, and offers an anabolic treatment approach for osteoporosis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 25, pp. 10619–10624, 2007. View at Publisher · View at Google Scholar · View at Scopus
  85. M. A. Kacena, P. P. Eleniste, Y. H. Cheng et al., “Megakaryocytes regulate expression of Pyk2 isoforms and caspase-mediated cleavage of actin in osteoblasts,” The Journal of Biological Chemistry, vol. 287, no. 21, pp. 17257–17268, 2012. View at Google Scholar
  86. L. T. Duong, P. T. Lakkakorpi, I. Nakamura, M. Machwate, R. M. Nagy, and G. A. Rodan, “PYK2 in osteoclasts is an adhesion kinase, localized in the sealing zone, activated by ligation of α(v)β3 integrin, and phosphorylated by Src kinase,” Journal of Clinical Investigation, vol. 102, no. 5, pp. 881–892, 1998. View at Google Scholar · View at Scopus
  87. A. Sanjay, A. Houghton, L. Neff et al., “Cbl associates with Pyk2 and Src to regulate Src kinase activity, αvβ3 integrin-mediated signaling, cell adhesion, and osteoclast motility,” The Journal of Cell Biology, vol. 152, no. 1, pp. 181–195, 2001. View at Publisher · View at Google Scholar · View at Scopus
  88. O. Destaing, A. Sanjay, C. Itzstein et al., “The tyrosine kinase activity of c-Src regulates actin dynamics and organization of podosomes in osteoclasts,” Molecular Biology of the Cell, vol. 19, no. 1, pp. 394–404, 2008. View at Publisher · View at Google Scholar · View at Scopus
  89. A. Gupta, B. S. Lee, M. A. Khadeer et al., “Leupaxin is a critical adaptor protein in the adhesion zone of the osteoclast,” Journal of Bone and Mineral Research, vol. 18, no. 4, pp. 669–685, 2003. View at Google Scholar · View at Scopus
  90. S. N. Sahu, M. A. Khadeer, B. W. Robertson, S. M. Núñez, G. Bai, and A. Gupta, “Association of leupaxin with Src in osteoclasts,” American Journal of Physiology, vol. 292, no. 1, pp. C581–C590, 2007. View at Publisher · View at Google Scholar · View at Scopus
  91. S. N. Sahu, S. Nunez, G. Bai, and A. Gupta, “Interaction of Pyk2 and PTP-PEST with leupaxin in prostate cancer cells,” American Journal of Physiology, vol. 292, no. 6, pp. C2288–C2296, 2007. View at Publisher · View at Google Scholar · View at Scopus
  92. G. C. Ochoa, V. I. Slepnev, L. Neff et al., “A functional link between dynamin and the actin cytoskeleton at podosomes,” The Journal of Cell Biology, vol. 150, no. 2, pp. 377–389, 2000. View at Publisher · View at Google Scholar · View at Scopus
  93. S. Han, A. Mistry, J. S. Chang et al., “Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design,” The Journal of Biological Chemistry, vol. 284, no. 19, pp. 13193–13201, 2009. View at Publisher · View at Google Scholar · View at Scopus
  94. A. H. Chishti, A. C. Kim, S. M. Marfatia et al., “The FERM domain: a unique module involved in the linkage of cytoplasmic proteins to the membrane,” Trends in Biochemical Sciences, vol. 23, no. 8, pp. 281–282, 1998. View at Publisher · View at Google Scholar · View at Scopus
  95. K. Hamada, T. Shimizu, T. Matsui, S. Tsukita, S. Tsukita, and T. Hakoshima, “Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain,” The EMBO Journal, vol. 19, no. 17, pp. 4449–4462, 2000. View at Google Scholar · View at Scopus
  96. Y. R. Pan, C. L. Chen, and H. C. Chen, “FAK is required for the assembly of podosome rosettes,” The Journal of Cell Biology, vol. 195, no. 1, pp. 113–129, 2011. View at Google Scholar
  97. I. Ayala, M. Baldassarre, G. Caldieri, and R. Buccione, “Invadopodia: a guided tour,” European Journal of Cell Biology, vol. 85, no. 3-4, pp. 159–164, 2006. View at Publisher · View at Google Scholar · View at Scopus
  98. S. Linder, “The matrix corroded: podosomes and invadopodia in extracellular matrix degradation,” Trends in Cell Biology, vol. 17, no. 3, pp. 107–117, 2007. View at Publisher · View at Google Scholar · View at Scopus
  99. S. Linder, “Invadosomes at a glance,” Journal of Cell Science, vol. 122, no. 17, pp. 3009–3013, 2009. View at Publisher · View at Google Scholar · View at Scopus
  100. M. Vicente-Manzanares and A. R. Horwitz, “Cell migration: an overview,” Methods in Molecular Biology, vol. 769, pp. 1–24, 2011. View at Publisher · View at Google Scholar · View at Scopus
  101. I. Ayala, M. Baldassarre, G. Giacchetti et al., “Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation,” Journal of Cell Science, vol. 121, no. 3, pp. 369–378, 2008. View at Publisher · View at Google Scholar · View at Scopus
  102. S. Tehrani, N. Tomasevic, S. Weed, R. Sakowicz, and J. A. Cooper, “Src phosphorylation of cortactin enhances actin assembly,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 29, pp. 11933–11938, 2007. View at Publisher · View at Google Scholar · View at Scopus
  103. M. Marzia, R. Chiusaroli, L. Neff et al., “Calpain is required for normal osteoclast function and is down-regulated by calcitonin,” The Journal of Biological Chemistry, vol. 281, no. 14, pp. 9745–9754, 2006. View at Publisher · View at Google Scholar · View at Scopus
  104. S. S. Stylli, T. T. I. Stacey, A. M. Verhagen et al., “Nck adaptor proteins link Tks5 to invadopodia actin regulation and ECM degradation,” Journal of Cell Science, vol. 122, no. 15, pp. 2727–2740, 2009. View at Publisher · View at Google Scholar · View at Scopus
  105. C. C. Mader, M. Oser, M. A. O. Magalhaes et al., “An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion,” Cancer Research, vol. 71, no. 5, pp. 1730–1741, 2011. View at Publisher · View at Google Scholar · View at Scopus
  106. T. Uruno, J. Liu, P. Zhang et al., “Activation of Arp2/3 complex-mediated actin polymerization by cortactin,” Nature Cell Biology, vol. 3, no. 3, pp. 259–266, 2001. View at Publisher · View at Google Scholar · View at Scopus
  107. M. Baldassarre, A. Pompeo, G. Beznoussenko et al., “Dynamin participates in focal extracellular matrix degradation by invasive cells,” Molecular Biology of the Cell, vol. 14, no. 3, pp. 1074–1084, 2003. View at Publisher · View at Google Scholar · View at Scopus
  108. S. Linder, C. Wiesner, and M. Himmel, “Degrading devices: invadosomes in proteolytic cell invasion,” Annual Review of Cell and Developmental Biology, vol. 27, pp. 185–211, 2011. View at Google Scholar
  109. F. Kimura, K. Iwaya, T. Kawaguchi et al., “Epidermal growth factor-dependent enhancement of invasiveness of squamous cell carcinoma of the breast,” Cancer Science, vol. 101, no. 5, pp. 1133–1140, 2010. View at Publisher · View at Google Scholar · View at Scopus
  110. M. Schoumacher, R. D. Goldman, D. Louvard, and D. M. Vignjevic, “Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia,” The Journal of Cell Biology, vol. 189, no. 3, pp. 541–556, 2010. View at Publisher · View at Google Scholar · View at Scopus
  111. C. S. Pichot, C. Arvanitis, S. M. Hartig et al., “Cdc42-interacting protein 4 promotes breast cancer cell invasion and formation of invadopodia through activation of N-WASp,” Cancer Research, vol. 70, no. 21, pp. 8347–8356, 2010. View at Publisher · View at Google Scholar · View at Scopus
  112. R. Buccione, G. Caldieri, and I. Ayala, “Invadopodia: specialized tumor cell structures for the focal degradation of the extracellular matrix,” Cancer and Metastasis Reviews, vol. 28, no. 1-2, pp. 137–149, 2009. View at Publisher · View at Google Scholar · View at Scopus
  113. C. Albiges-Rizo, O. Destaing, B. Fourcade, E. Planus, and M. R. Block, “Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions,” Journal of Cell Science, vol. 122, no. 17, pp. 3037–3049, 2009. View at Publisher · View at Google Scholar · View at Scopus
  114. U. Philippar, E. T. Roussos, M. Oser et al., “A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis,” Developmental Cell, vol. 15, no. 6, pp. 813–828, 2008. View at Publisher · View at Google Scholar · View at Scopus
  115. D. A. Schafer, “Regulating actin dynamics at membranes: a focus on dynamin,” Traffic, vol. 5, no. 7, pp. 463–469, 2004. View at Publisher · View at Google Scholar · View at Scopus
  116. G. Eitzen, “Actin remodeling to facilitate membrane fusion,” Biochimica et Biophysica Acta, vol. 1641, no. 2-3, pp. 175–181, 2003. View at Publisher · View at Google Scholar · View at Scopus
  117. M. Egeblad and Z. Werb, “New functions for the matrix metalloproteinases in cancer progression,” Nature Reviews Cancer, vol. 2, no. 3, pp. 161–174, 2002. View at Google Scholar · View at Scopus
  118. M. Seiki, “Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion,” Cancer Letters, vol. 194, no. 1, pp. 1–11, 2003. View at Publisher · View at Google Scholar · View at Scopus
  119. F. Saltel, T. Daubon, A. Juin, I. E. Ganuza, V. Veillat, and E. Génot, “Invadosomes: intriguing structures with promise,” European Journal of Cell Biology, vol. 90, no. 2-3, pp. 100–107, 2011. View at Publisher · View at Google Scholar · View at Scopus
  120. M. A. Eckert and J. Yang, “Targeting invadopodia to block breast cancer metastasis,” Oncotarget, vol. 2, no. 7, pp. 562–568, 2011. View at Google Scholar
  121. C. Badowski, G. Pawlak, A. Grichine et al., “Paxillin phosphorylation controls invadopodia/podosomes spatiotemporal organization,” Molecular Biology of the Cell, vol. 19, no. 2, pp. 633–645, 2008. View at Publisher · View at Google Scholar · View at Scopus
  122. C. L. Cortesio, K. T. Chan, B. J. Perrin et al., “Calpain 2 and PTP1B function in a novel pathway with Src to regulate invadopodia dynamics and breast cancer cell invasion,” The Journal of Cell Biology, vol. 180, no. 5, pp. 957–971, 2008. View at Publisher · View at Google Scholar · View at Scopus
  123. L. C. Kelley, A. G. Ammer, K. E. Hayes et al., “Oncogenic Src requires a wild-type counterpart to regulate invadopodia maturation,” Journal of Cell Science, vol. 123, no. 22, pp. 3923–3932, 2010. View at Publisher · View at Google Scholar · View at Scopus
  124. L. Li, M. Okura, and A. Imamoto, “Focal adhesions require catalytic activity of Src family kinases to mediate integrin-matrix adhesion,” Molecular and Cellular Biology, vol. 22, no. 4, pp. 1203–1217, 2002. View at Publisher · View at Google Scholar · View at Scopus
  125. S. Granot-Attas, C. Luxenburg, E. Finkelshtein, and A. Elson, “Protein tyrosine phosphatase epsilon regulates integrin-mediated podosome stability in osteoclasts by activating Src,” Molecular Biology of the Cell, vol. 20, no. 20, pp. 4324–4334, 2009. View at Publisher · View at Google Scholar · View at Scopus
  126. D. J. Webb, K. Donais, L. A. Whitmore et al., “FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly,” Nature Cell Biology, vol. 6, no. 2, pp. 154–161, 2004. View at Publisher · View at Google Scholar · View at Scopus
  127. H. Sasaki, K. Nagura, M. Ishino, H. Tobioka, K. Kotani, and T. Sasaki, “Cloning and characterization of cell adhesion kinase β, a novel protein- tyrosine kinase of the focal adhesion kinase subfamily,” The Journal of Biological Chemistry, vol. 270, no. 36, pp. 21206–21219, 1995. View at Publisher · View at Google Scholar · View at Scopus
  128. R. Baron, “Molecular mechanisms of bone resorption: therapeutic implications,” Revue du Rhumatisme (English Edition), vol. 63, no. 10, pp. 633–638, 1996. View at Google Scholar · View at Scopus
  129. T. Miyazaki, A. Sanjay, L. Neff, S. Tanaka, W. C. Horne, and R. Baron, “Src kinase activity is essential for osteoclast function,” The Journal of Biological Chemistry, vol. 279, no. 17, pp. 17660–17666, 2004. View at Publisher · View at Google Scholar · View at Scopus
  130. J. W. Triplett and F. M. Pavalko, “Disruption of α-actinin-integrin interactions at focal adhesions renders osteoblasts susceptible to apoptosis,” American Journal of Physiology, vol. 291, no. 5, pp. C909–C921, 2006. View at Publisher · View at Google Scholar · View at Scopus
  131. S. A. Courtneidge, “Cell migration and invasion in human disease: the Tks adaptor proteins,” Biochemical Society Transactions, vol. 40, no. 1, pp. 129–132, 2012. View at Google Scholar
  132. B. Blouw, D. F. Seals, I. Pass, B. Diaz, and S. A. Courtneidge, “A role for the podosome/invadopodia scaffold protein Tks5 in tumor growth in vivo,” European Journal of Cell Biology, vol. 87, no. 8-9, pp. 555–567, 2008. View at Publisher · View at Google Scholar · View at Scopus
  133. I. Ayala, G. Giacchetti, G. Caldieri et al., “Faciogenital dysplasia protein Fgd1 regulates invadopodia biogenesis and extracellular matrix degradation and is up-regulated in prostate and breast cancer,” Cancer Research, vol. 69, no. 3, pp. 747–752, 2009. View at Publisher · View at Google Scholar · View at Scopus
  134. G. W. McLean, N. O. Carragher, E. Avizienyte, J. Evans, V. G. Brunton, and M. C. Frame, “The role of focal-adhesion kinase in cancer—a new therapeutic opportunity,” Nature Reviews Cancer, vol. 5, no. 7, pp. 505–515, 2005. View at Publisher · View at Google Scholar · View at Scopus
  135. V. G. Brunton and M. C. Frame, “Src and focal adhesion kinase as therapeutic targets in cancer,” Current Opinion in Pharmacology, vol. 8, no. 4, pp. 427–432, 2008. View at Publisher · View at Google Scholar · View at Scopus
  136. H. Lahlou, V. Sanguin-Gendreau, D. Zuo et al., “Mammary epithelial-specific disruption of the focal adhesion kinase blocks mammary tumor progression,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 51, pp. 20302–20307, 2007. View at Publisher · View at Google Scholar · View at Scopus
  137. M. Luo, H. Fan, T. Nagy et al., “Mammary epithelial-specific ablation of the focal adhesion kinase suppresses mammary tumorigenesis by affecting mammary cancer stem/progenitor cells,” Cancer Research, vol. 69, no. 2, pp. 466–474, 2009. View at Publisher · View at Google Scholar · View at Scopus
  138. B. Tavora, S. Batista, L. E. Reynolds et al., “Endothelial FAK is required for tumour angiogenesis,” EMBO Molecular Medicine, vol. 2, no. 12, pp. 516–528, 2010. View at Publisher · View at Google Scholar · View at Scopus
  139. N. Koon, R. Schneider-Stock, M. Sarlomo-Rikala et al., “Molecular targets for tumour progression in gastrointestinal stromal tumours,” Gut, vol. 53, no. 2, pp. 235–240, 2004. View at Publisher · View at Google Scholar · View at Scopus
  140. T. Miyazaki, H. Kato, M. Nakajima et al., “FAK overexpression is correlated with tumour invasiveness and lymph node metastasis in oesophageal squamous cell carcinoma,” British Journal of Cancer, vol. 89, no. 1, pp. 140–145, 2003. View at Publisher · View at Google Scholar · View at Scopus
  141. C. R. Hauck, D. A. Hsia, X. S. Puente, D. A. Cheresh, and D. D. Schlaepfer, “FRNK blocks v-Src-stimulated invasion and experimental metastases without effects on cell motility or growth,” The EMBO Journal, vol. 21, no. 23, pp. 6289–6302, 2002. View at Publisher · View at Google Scholar · View at Scopus
  142. C. R. Hauck, D. A. Hsia, D. Ilic, and D. D. Schlaepfer, “v-Src SH3-enhanced interaction with focal adhesion kinase at β1 integrin-containing invadopodia promotes cell invasion,” The Journal of Biological Chemistry, vol. 277, no. 15, pp. 12487–12490, 2002. View at Publisher · View at Google Scholar · View at Scopus
  143. C. Annerén, C. A. Cowan, and D. A. Melton, “The Src family of tyrosine kinases is important for embryonic stem cell self-renewal,” The Journal of Biological Chemistry, vol. 279, no. 30, pp. 31590–31598, 2004. View at Publisher · View at Google Scholar · View at Scopus
  144. S. J. Parsons and J. T. Parsons, “Src family kinases, key regulators of signal transduction,” Oncogene, vol. 23, no. 48, pp. 7906–7909, 2004. View at Publisher · View at Google Scholar · View at Scopus
  145. J. M. Su, L. Gui, Y. P. Zhou, and X. L. Zha, “Expression of focal adhesion kinase and α5 and β1 integrins in carcinomas and its clinical significance,” World Journal of Gastroenterology, vol. 8, no. 4, pp. 613–618, 2002. View at Google Scholar · View at Scopus
  146. I. Tanjoni, C. Walsh, S. Uryu et al., “PND-1186 FAK inhibitor selectively promotes tumor cell apoptosis in three-dimensional environments,” Cancer Biology and Therapy, vol. 9, no. 10, pp. 764–777, 2010. View at Google Scholar · View at Scopus
  147. S. Roelle, R. Grosse, T. Buech, V. Chubanov, and T. Gudermann, “Essential role of Pyk2 and Src kinase activation in neuropeptide-induced proliferation of small cell lung cancer cells,” Oncogene, vol. 27, no. 12, pp. 1737–1748, 2008. View at Publisher · View at Google Scholar · View at Scopus
  148. S. Zhang, X. Qiu, Y. Gu, and E. Wang, “Up-regulation of proline-rich tyrosine kinase 2 in non-small cell lung cancer,” Lung Cancer, vol. 62, no. 3, pp. 295–301, 2008. View at Publisher · View at Google Scholar · View at Scopus
  149. M. J. van Nimwegen, S. Verkoeijen, L. van Buren, D. Burg, and B. van de Water, “Requirement for focal adhesion kinase in the early phase of mammary adenocarcinoma lung metastasis formation,” Cancer Research, vol. 65, no. 11, pp. 4698–4706, 2005. View at Publisher · View at Google Scholar · View at Scopus
  150. L. Tremblay, W. Hauck, A. G. Aprikian, L. R. Begin, A. Chapdelaine, and S. Chevalier, “Focal adhesion kinase (pp125FAK) expression, activation and association with paxillin and p50CSK in human metastatic prostate carcinoma,” International Journal of Cancer, vol. 68, no. 2, pp. 164–171, 1996. View at Google Scholar
  151. H. Sun, S. Pisle, E. R. Gardner, and W. D. Figg, “Bioluminescent imaging study: FAK inhibitor, PF-562,271, preclinical study in PC3M-luc-C6 local implant and metastasis xenograft models,” Cancer Biology and Therapy, vol. 10, no. 1, pp. 38–43, 2010. View at Google Scholar · View at Scopus
  152. P. P. Eleniste, L. Du, M. Shivanna, and A. Bruzzaniti, “Dynamin and PTP-PEST cooperatively regulate Pyk2 dephosphorylation in osteoclasts,” The International Journal of Biochemistry & Cell Biology, vol. 44, no. 5, pp. 790–800, 2012. View at Google Scholar
  153. B. Desai, T. Ma, and M. A. Chellaiah, “Invadopodia and matrix degradation, a new property of prostate cancer cells during migration and invasion,” The Journal of Biological Chemistry, vol. 283, no. 20, pp. 13856–13866, 2008. View at Publisher · View at Google Scholar · View at Scopus
  154. A. Gutenberg, W. Brück, M. Buchfelder, and H. C. Ludwig, “Expression of tyrosine kinases FAK and Pyk2 in 331 human astrocytomas,” Acta Neuropathologica, vol. 108, no. 3, pp. 224–230, 2004. View at Google Scholar · View at Scopus
  155. Z. Li, X. Yuan, Z. Wu, Z. Guo, P. Jiang, and Z. Wen, “Expressions of FAK and Pyk2 in human astrocytic tumors and their relationship with angiogenesis,” Chinese-German Journal of Clinical Oncology, vol. 7, no. 11, pp. 658–660, 2008. View at Publisher · View at Google Scholar · View at Scopus
  156. T. P. Hecker, J. R. Grammer, G. Y. Gillespie, J. Stewart Jr., and C. L. Gladson, “Focal adhesion kinase enhances signaling through the Shc/extracellular signal-regulated kinase pathway in anaplastic astrocytoma tumor biopsy samples,” Cancer Research, vol. 62, no. 9, pp. 2699–2707, 2002. View at Google Scholar · View at Scopus
  157. Q. Shi, A. B. Hjelmeland, S. T. Keir et al., “A novel low-molecular weight inhibitor of focal adhesion kinase, TAE226, inhibits glioma growth,” Molecular Carcinogenesis, vol. 46, no. 6, pp. 488–496, 2007. View at Publisher · View at Google Scholar · View at Scopus
  158. A. H. Sikkema, S. H. Diks, W. F. A. den Dunnen et al., “Kinome profiling in pediatric brain tumors as a new approach for target discovery,” Cancer Research, vol. 69, no. 14, pp. 5987–5995, 2009. View at Publisher · View at Google Scholar · View at Scopus
  159. S. M. Weis, S. T. Lim, K. M. Lutu-Fuga et al., “Compensatory role for Pyk2 during angiogenesis in adult mice lacking endothelial cell FAK,” The Journal of Cell Biology, vol. 181, no. 1, pp. 43–50, 2008. View at Publisher · View at Google Scholar · View at Scopus
  160. Y. Duan, J. Learoyd, A. Y. Meliton, B. S. Clay, A. R. Leff, and X. Zhu, “Inhibition of Pyk2 blocks airway inflammation and hyperresponsiveness in a mouse model of asthma,” American Journal of Respiratory Cell and Molecular Biology, vol. 42, no. 4, pp. 491–497, 2010. View at Publisher · View at Google Scholar · View at Scopus
  161. Y. Yu, S. A. Ross, A. E. Halseth et al., “Role of PYK2 in the development of obesity and insulin resistance,” Biochemical and Biophysical Research Communications, vol. 334, no. 4, pp. 1085–1091, 2005. View at Publisher · View at Google Scholar · View at Scopus
  162. M. Okigaki, C. Davis, M. Falascat et al., “Pyk2 regulates multiple signaling events crucial for macrophage morphology and migration,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 19, pp. 10740–10745, 2003. View at Publisher · View at Google Scholar · View at Scopus
  163. D. Lang, A. V. Glukhov, T. Efimova, and I. R. Efimov, “Role of Pyk2 in cardiac arrhythmogenesis,” American Journal of Physiology Heart and Circulatory Physiology, vol. 301, no. 3, pp. H975–H983, 2011. View at Google Scholar
  164. G. M. Fabrizi, M. Ferrarini, T. Cavallaro et al., “Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease,” Neurology, vol. 69, no. 3, pp. 291–295, 2007. View at Publisher · View at Google Scholar · View at Scopus
  165. J. Böhm, V. Biancalana, E. T. Dechene et al., “Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy,” Human Mutation, vol. 33, no. 6, pp. 949–959, 2012. View at Publisher · View at Google Scholar · View at Scopus
  166. P. N. M. Sidiropoulos, M. Miehe, T. Bock et al., “Dynamin 2 mutations in Charcot-Marie-Tooth neuropathy highlight the importance of clathrin-mediated endocytosis in myelination,” Brain, vol. 135, no. 5, pp. 1395–1411, 2012. View at Publisher · View at Google Scholar · View at Scopus