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  • [1]D. Georgess, I. Machuca-Gayet, A. Blangy, P. Jurdic: Podosome organization drives osteoclast-mediated bone resorption. Cell Adh. Migr. 8, 192–204 (2014)

  • [2]G. Seano, G. Chiaverina, P. A. Gagliardi, L. di Blasio, A. Puliafito, C. Bouvard, R. Sessa, G. Tarone, L. Sorokin, D. Helley, R. K. Jain, G. Serini, F. Bussolino, L. Primo: Endothelial podosome rosettes regulate vascular branching in tumour angiogenesis. Nat. Cell Biol. 16, 931–941 (2014)

  • [3]T. David-Pfeuty, S. J. Singer: Altered distributions of the cytoskeletal proteins vinculin and alpha-actinin in cultured fibroblasts transformed by Rous sarcoma virus. Proc. Natl. Acad. Sci. U. S. A. 77, 6687–91 (1980)

  • [4]J. Trotter: The organization of actin in spreading macrophages. Exp. Cell Res. 132, 235–248 (1981)

  • [5]P. C. Marchisio, D. Cirillo, L. Naldini, M. V Primavera, A. Teti: Cell-Substratum Interaction of Cultured Avian Osteoclasts Is Mediated by Specific Adhesion Structures. J Cell Biol. 99, 1696-705 (1984)

  • [6]G. Tarone, D. Cirillo, F. G. Giancotti, P. M. Comoglio, P. C. Marchisio: Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 159, 141–57 (1985)

  • [7]P. C. Marchisio, L. Bergui, G. C. Corbascio, O. Cremona, N. D’Urso, M. Schena, L. Tesio, F. Caligaris-Cappio: Vinculin, talin, and integrins are localized at specific adhesion sites of malignant B lymphocytes. Blood 72, 830–3 (1988)

  • [8]W. T. Chen: Proteolytic activity of specialized surface protrusions formed at rosette contact sites of transformed cells. J. Exp. Zool. 251, 167–85 (1989)

  • [9]S. C. Mueller, W. T. Chen: Cellular invasion into matrix beads: localization of beta 1 integrins and fibronectin to the invadopodia. J. Cell Sci. 99, 213–225 (1991)

  • [10]S. Linder: The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol. 17, 107–117 (2007)

  • [11]D. Murphy, S. Courtneidge: The ‘ins’ and ‘outs’ of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12, 413–426 (2011)

  • [12]S. Burns, A. J. Thrasher, M. P. Blundell, L. M. Machesky, G. E. Jones: Configuration of human dendritic cell cytoskeleton by Rho GTPases, the WAS protein, and differentiation. Blood 98, 1142–1149 (2001)

  • [13]V. Moreau, F. Tatin, C. Varon, E. Génot: Actin can reorganize into podosomes in aortic endothelial cells, a process controlled by Cdc42 and RhoA. Mol. Cell. Biol. 23, 6809–22 (2003)

  • [14]C. Hai: Conventional Protein Kinase C Mediates Phorbol-Dibutyrate-Induced Cytoskeletal Remodeling in A7r5 Smooth Muscle Cells. Exp. Cell Res. 280, 64–74 (2002)

  • [15]E. W. Thompson, S. Paik, N. Brünner, C. L. Sommers, G. Zugmaier, R. Clarke, T. B. Shima, J. Torri, S. Donahue, M. E. Lippman: Association of increased basement membrane invasiveness with absence of estrogen receptor and expression of vimentin in human breast cancer cell lines. J. Cell. Physiol. 150, 534–544 (1992)

  • [16]W. L. Monsky, C. Y. Lin, A. Aoyama, T. Kelly, S. K. Akiyama, S. C. Mueller, W. T. Chen: A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells. Cancer Res. 54, 5702–5710 (1994)

  • [17]R. Del Maestro, R. Shivers, W. McDonald, A. Del Maestro: Dynamics of C6 astrocytoma invasion into three-dimensional collagen gels. J. Neurooncol. 53, 87–98 (2001)

  • [18]Y. S. Hwang, K.-K. Park, W.-Y. Chung: Invadopodia formation in oral squamous cell carcinoma: The role of epidermal growth factor receptor signalling. Arch. Oral Biol. 57, 335–343 (2012)

  • [19]K. Imanishi, M. Yoneyama, S. Hatakeyama, H. Yamamoto, T. Koie, H. Saitoh, K. Yamaya, T. Funyu, T. Nakamura, C. Ohyama, S. Tsuboi: Invadopodia are essential in transurothelial invasion during the muscle invasion of bladder cancer cells. Mol. Med. Rep.2159–2165 (2014)

  • [20]S. Linder: Invadosomes at a glance. J. Cell Sci. 122, 3009–3013 (2009)

  • [21]O. Destaing, M. R. Block, E. Planus, C. Albiges-Rizo: Invadosome regulation by adhesion signaling. Curr. Opin. Cell Biol. 23, 597–606 (2011)

  • [22]F. Saltel, T. Daubon, A. Juin, I. E. Ganuza, V. Veillat, E. Génot: Invadosomes: intriguing structures with promise. Eur. J. Cell Biol. 90, 100–7 (2011)

  • [23]C. Gawden-Bone, Z. Zhou, E. King, A. Prescott, C. Watts, J. Lucocq: Dendritic cell podosomes are protrusive and invade the extracellular matrix using metalloproteinase MMP-14. J. Cell Sci. 123, 1427–1437 (2010)

  • [24]M. V Baranov, M. Ter Beest, I. Reinieren-Beeren, A. Cambi, C. G. Figdor, G. van den Bogaart: Podosomes of dendritic cells facilitate antigen sampling. J. Cell Sci. 127, 1052–64 (2014)

  • [25]K. Clark, M. Langeslag, B. van Leeuwen, L. Ran, A. G. Ryazanov, C. G. Figdor, W. H. Moolenaar, K. Jalink, F. N. van Leeuwen: TRPM7, a novel regulator of actomyosin contractility and cell adhesion. EMBO J. 25, 290–301 (2006)

  • [26]K. M. Branch, D. Hoshino, M. Weaver: Adhesion rings surround invadopodia and promote maturation. Biol. Open 1, 711–722 (2012)

  • [27]O. Y. Revach, A. Weiner, K. Rechav, I. Sabanay, A. Livne, B. Geiger: Mechanical interplay between invadopodia and the nucleus in cultured cancer cells. Sci. Rep.5, 9466 (2015)

  • [28]M. A. Morrissey, E. J. Hagedorn, D. R. Sherwood: Cell invasion through basement membrane: The netrin receptor DCC guides the way. Worm 2, e26169 (2013)

  • [29]M. Santiago-Medina, K. Gregus, R. H. Nichol, S. M. O’Toole, T. M. Gomez: Regulation of ECM degradation and axon guidance by growth cone invadosomes. Development 142, 486–496 (2015)

  • [30]G. Seano, L. Primo: Podosomes and invadopodia: tools to breach vascular basement membrane. Cell cycle 14, 1370–4 (2015)

  • [31]K. van den Dries, S. L. Schwartz, J. Byars, M. B. M. Meddens, M. Bolomini-Vittori, D. S. Lidke, C. G. Figdor, K. a Lidke, A. Cambi: Dual-color superresolution microscopy reveals nanoscale organization of mechanosensory podosomes. Mol. Biol. Cell 24, 2112–23 (2013)

  • [32]M. Pfaff, P. Jurdic: Podosomes in osteoclast-like cells: structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase 2 (Pyk2) and integrin alphaVbeta3. J. Cell Sci. 114, 2775–2786 (2001)

  • [33]A. Chabadel, I. Bañon-Rodríguez, D. Cluet, B. B. Rudkin, B. Wehrle-Haller, E. Genot, P. Jurdic, I. M. Antón, F. SalTel: CD44 and β3 integrin organize two functionally distinct actin-based domains in osteoclasts. Mol. Biol. Cell 18, 4899–4910 (2007)

  • [34]L. L. Lohmer, L. C. Kelley, E. J. Hagedorn, D. R. Sherwood: Invadopodia and basement membrane invasion in vivo. Cell Adh. Migr. 8, 1–10 (2014)

  • [35]O. Destaing, F. Saltel, J.-C. Géminard, P. Jurdic, F. Bard: Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein. Mol. Biol. Cell 14, 407–416 (2003)

  • [36]O. Y. Revach, B. Geiger: The interplay between the proteolytic, invasive, and adhesive domains of invadopodia and their roles in cancer invasion. Cell Adh. Migr. 8, 1–11 (2013)

  • [37]M. B. M. Meddens, K. van den Dries, A. Cambi: Podosomes revealed by advanced bioimaging: what did we learn? Eur. J. Cell Biol. 93, 380–7 (2014)

  • [38]B. T. Beaty, J. Condeelis: Digging a little deeper: The stages of invadopodium formation and maturation. Eur. J. Cell Biol. 93, 438–444 (2014)

  • [39]C. M. Gould, S. a Courtneidge: Regulation of invadopodia by the tumor microenvironment. Cell Adh. Migr. 8, 1–10 (2014)

  • [40]L. C. Kelley, L. L. Lohmer, E. J. Hagedorn, D. R. Sherwood: Traversing the basement membrane in vivo: a diversity of strategies. J. Cell Biol. 204, 291–302 (2014)

  • [41]S. Linder, C. Wiesner: Tools of the trade: podosomes as multipurpose organelles of monocytic cells. Cell. Mol. Life Sci. 72, 121–35 (2015)

  • [42]S. Linder, C. Wiesner, M. Himmel: Degrading Devices: Invadosomes in Proteolytic Cell Invasion. Annu. Rev. Cell Dev. Biol. 27, 185–211 (2011)

  • [43]M. Schoumacher, R. D. Goldman, D. Louvard, D. M. Vignjevic: Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 189, 541–56 (2010)

  • [44]H. Yamaguchi, M. Lorenz, S. Kempiak, C. Sarmiento, S. Coniglio, M. Symons, J. Segall, R. Eddy, H. Miki, T. Takenawa, J. Condeelis: Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J. Cell Biol. 168, 441–52 (2005)

  • [45]I. Kaverina, T. E. B. Stradal, M. Gimona: Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains. J. Cell Sci. 116, 4915–24 (2003)

  • [46]K. G. Campellone, M. D. Welch: A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11, 237–51 (2010)

  • [47]L. Helgeson, B. J. Nolen: Mechanism of synergistic activation of Arp2/3 complex by cortactin and N-WASP. Elife 2, e00884 (2013)

  • [48]S. B. Padrick, L. K. Doolittle, C. a Brautigam, D. S. King, M. K. Rosen: Arp2/3 complex is bound and activated by two WASP proteins. Proc. Natl. Acad. Sci. U. S. A. 108, E472–E479 (2011)

  • [49]T. Uruno, J. Liu, P. Zhang, Fan Yx, C. Egile, R. Li, S. C. Mueller, X. Zhan: Activation of Arp2/3 complex-mediated actin polymerization by cortactin. Nat. Cell Biol. 3, 259–266 (2001)

  • [50]A. M. Weaver, J. E. Heuser, A. V Karginov, W. lih Lee, J. T. Parsons, J. A. Cooper: Interaction of cortactin and N-WASp with Arp2/3 complex. Curr. Biol. 12, 1270–1278 (2002)

  • [51]E. S. Clark, A. S. Whigham, W. G. Yarbrough, A. M. Weaver: Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia. Cancer Res. 67, 4227–35 (2007)

  • [52]B. Gligorijevic, J. Wyckoff, H. Yamaguchi, Y. Wang, E. T. Roussos, J. Condeelis: N-WASP-mediated invadopodium formation is involved in intravasation and lung metastasis of mammary tumors. J. Cell Sci. 125, 724–34 (2012)

  • [53]L. M. Nusblat, A. Dovas, D. Cox: The non-redundant role of N-WASP in podosome-mediated matrix degradation in macrophages. Eur. J. Cell Biol. 90, 205–12 (2011)

  • [54]B. Webb, R. Eves, A. S. Mak: Cortactin regulates podosome formation: roles of the protein interaction domains. Exp. Cell Res. 312, 760–9 (2006)

  • [55]J. B. Marchand, D. a Kaiser, T. D. Pollard, H. N. Higgs: Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex. Nat. Cell Biol. 3, 76–82 (2001)

  • [56]S. Suetsugu: Activation of nucleation promoting factors for directional actin filament elongation: Allosteric regulation and multimerization on the membrane. Semin. Cell Dev. Biol. 24, 267–271 (2013)

  • [57]M. Lorenz, H. Yamaguchi, Y. Wang, R. H. Singer, J. Condeelis: Imaging sites of N-WASP activity in lamellipodia and invadopodia of carcinoma cells. Curr. Biol. 14, 697–703 (2004)

  • [58]N. Khanduja, J. R. Kuhn: Processive acceleration of actin barbed-end assembly by N-WASP. Mol. Biol. Cell 25, 55–65 (2014)

  • [59]K. Lee, J. L. Gallop, K. Rambani, M. W. Kirschner: Self-assembly of filopodia-like structures on supported lipid bilayers. Science 329, 1341–5 (2010)

  • [60]V. Artym, Y. Zhang, F. Seillier-Moiseiwitsch, K. M. Yamada, S. C. Mueller: Dynamic Interactions of Cortactin and Membrane Type 1 Matrix Metalloproteinase at Invadopodia: Defining the Stages of Invadopodia Formation and Function. Cancer Res. 66, 3034–3043 (2006)

  • [61]I. Ayala, M. Baldassarre, G. Giacchetti, G. Caldieri, S. Tetè, A. Luini, R. Buccione: Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. J. Cell Sci. 121, 369–78 (2008)

  • [62]M. Oser, H. Yamaguchi, C. C. Mader, J. J. Bravo-Cordero, M. Arias, X. Chen, V. Desmarais, J. van Rheenen, A. J. Koleske, J. Condeelis: Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. J. Cell Biol. 186, 571–87 (2009)

  • [63]C. C. Mader, M. Oser, M. a O. Magalhaes, J. J. Bravo-Cordero, J. Condeelis, A. J. Koleske, H. Gil-Henn: An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion. Cancer Res. 71, 1730–41 (2011)

  • [64]S. Tehrani, N. Tomasevic, S. Weed, R. Sakowicz, J. Cooper: Src phosphorylation of cortactin enhances actin assembly. Proc. Natl. Acad. Sci. U. S. A. 104, 11933–8 (2007)

  • [65]V. DesMarais, H. Yamaguchi, M. Oser, L. Soon, G. Mouneimne, C. Sarmiento, R. Eddy, J. Condeelis: N-WASP and cortactin are involved in invadopodium-dependent chemotaxis to EGF in breast tumor cells. Cell Motil. Cytoskeleton 66, 303–316 (2009)

  • [66]V. Moreau, F. Frischknecht, I. Reckmann, R. Vincentelli, G. Rabut, D. Stewart, M. Way: A complex of N-WASP and WIP integrates signalling cascades that lead to actin polymerization. Nat. Cell Biol. 2, 441–448 (2000)

  • [67]E. García, L. M. Machesky, G. E. Jones, I. M. Antón: WIP is necessary for matrix invasion by breast cancer cells. Eur. J. Cell Biol. 93, 413–23 (2014)

  • [68]Y. Li, M. Tondravi, J. Liu, E. Smith, C. C. Haudenschild, M. Kaczmarek, X. Zhan: Cortactin potentiates bone metastasis of breast cancer cells. Cancer Res. 61, 6906–11 (2001)

  • [69]N. Martinez-Quiles, R. Rohatgi, I. M. Antón, M. Medina, S. P. Saville, H. Miki, H. Yamaguchi, T. Takenawa, J. H. Hartwig, R. S. Geha, N. Ramesh: WIP regulates N-WASP-mediated actin polymerization and filopodium formation. Nat. Cell Biol. 3, 484–491 (2001)

  • [70]S. K. Donnelly, I. Weisswange, M. Zettl, M. Way: WIP provides an essential link between nck and n-wasp during arp2/3-dependent actin polymerization. Curr. Biol. 23, 999–1006 (2013)

  • [71]A. W. Kinley, S. A. Weed, A. M. Weaver, A. V. Karginov, E. Bissonette, J. A. Cooper, J. T. Parsons: Cortactin Interacts with WIP in Regulating Arp2/3 Activation and Membrane Protrusion. Curr. Biol. 13, 384–393 (2003)

  • [72]U. Ghoshdastider, D. Popp, L. D. Burtnick, R. C. Robinson: The expanding superfamily of gelsolin homology domain proteins. Cytoskeleton 70, 775–795 (2013)

  • [73]M. Chellaiah, N. Kizer, M. Silva, U. Alvarez, D. Kwiatkowski, K. Hruska: Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength. J. Cell Biol. 148, 665–678 (2000)

  • [74]J. L. Crowley, T. C. Smith, Z. Fang, N. Takizawa, E. J. Luna: Supervillin Reorganizes the Actin Cytoskeleton and Increases Invadopodial Efficiency. Mol. Biol. Cell 20, 948–962 (2009)

  • [75]M. Ghosh, X. Song, G. Mouneimne, M. Sidani, D. S. Lawrence, J. S. Condeelis: Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304, 743–746 (2004)

  • [76]T. D. Pollard, G. G. Borisy: Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453–65 (2003)

  • [77]K. Takemoto, T. Matsuda, N. Sakai, D. Fu, M. Noda, S. Uchiyama, I. Kotera, Y. Arai, M. Horiuchi, K. Fukui, T. Ayabe, F. Inagaki, H. Suzuki, T. Nagai: SuperNova, a monomeric photosensitizing fluorescent protein for chromophore-assisted light inactivation. Sci. Rep.3, 2629 (2013)

  • [78]E. J. Hagedorn, J. W. Ziel, M. Morrissey, L. M. Linden, Z. Wang, Q. Chi, S. Johnson, D. R. Sherwood: The netrin receptor DCC focuses invadopodia-driven basement membrane transmigration in vivo. J. Cell Biol. 201, 903–13 (2013)

  • [79]T. Isogai, R. van der Kammen, D. Leyton-Puig, K. M. Kedziora, K. Jalink, M. Innocenti: Initiation of lamellipodia and ruffles involves cooperation between mDia1 and the Arp2/3 complex. J. Cell Sci. 128, 3796–810 (2015)

  • [80]B. T. Beaty, Y. Wang, J. J. Bravo-Cordero, V. P. Sharma, V. Miskolci, L. Hodgson, J. Condeelis: Talin regulates moesin-NHE-1 recruitment to invadopodia and promotes mammary tumor metastasis. J. Cell Biol. 205, 737–751 (2014)

  • [81]M. O. Magalhaes, D. R. Larson, C. C. Mader, J. J. Bravo-Cordero, H. Gil-Henn, M. Oser, X. Chen, A. J. Koleske, J. Condeelis: Cortactin phosphorylation regulates cell invasion through a pH-dependent pathway. J. Cell Biol. 195, 903–20 (2011)

  • [82]C. Frantz, G. Barreiro, L. Dominguez, X. Chen, R. Eddy, J. Condeelis, M. J. S. Kelly, M. P. Jacobson, D. L. Barber: Cofilin is a pH sensor for actin free barbed end formation: role of phosphoinositide binding. J. Cell Biol. 183, 865–879 (2008)

  • [83]K. Mizuno: Signaling mechanisms and functional roles of cofilin phosphorylation and dephosphorylation. Cell. Signal. 25, 457–469 (2013)

  • [84]J. J. Bravo-Cordero, M. Oser, X. Chen, R. Eddy, L. Hodgson, J. Condeelis: A novel spatiotemporal RhoC activation pathway locally regulates cofilin activity at invadopodia. Curr. Biol. 21, 635–44 (2011)

  • [85]B. L. Goode, M. J. Eck: Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76, 593–627 (2007)

  • [86]M. Gardberg, K. Kaipio, L. Lehtinen, P. Mikkonen, V. D. Heuser, K. Talvinen, K. Iljin, C. Kampf, M. Uhlen, R. Grénman, M. Koivisto, O. Carpén: FHOD1, a formin upregulated in epithelial-mesenchymal transition, participates in cancer cell migration and invasion. PLoS One 8, e74923 (2013)

  • [87]Z. Li, Y. Xu, C. Zhang, X. Liu, L. Jiang, F. Chen: Mammalian diaphanous-related formin 1 is required for motility and invadopodia formation in human U87 glioblastoma cells. Int. J. Mol. Med. 33, 383–391 (2014)

  • [88]F. Lizárraga, R. Poincloux, M. Romao, G. Montagnac, G. Le Dez, I. Bonne, G. Rigaill, G. Raposo, P. Chavrier: Diaphanous-related formins are required for invadopodia formation and invasion of breast tumor cells. Cancer Res. 69, 2792–800 (2009)

  • [89]V. Lagal, M. Abrivard, V. Gonzalez, A. Perazzi, S. Popli, E. Verzeroli, I. Tardieux: Spire-1 contributes to the invadosome and its associated invasive properties. J. Cell Sci. 127, 328–40 (2014)

  • [90]J. Choi, Y. S. Jung, J. Y. Kim, H. M. Kim, I. K. Lim: Inhibition of breast cancer invasion by TIS21(/BTG2/Pc3)-Akt1-Sp1-Nox4 pathway targeting actin nucleators, mDia genes. Oncogene 1–11 (2015)

  • [91]C. Baarlink, H. Wang, R. Grosse: Nuclear actin network assembly by formins regulates the SRF coactivator MAL. Science 340, 864–7 (2013)

  • [92]T. Isogai, R. van der Kammen, S. S. Goerdayal, A. J. R. Heck, A. F. M. Altelaar, M. Innocenti: Proteomic analyses uncover a new function and mode of action for mouse homolog of Diaphanous 2 (mDia2) Mol. Cell. proteomics 14, 1064–78 (2015)

  • [93]L. Blanchoin, A. Michelot: Actin cytoskeleton: A team effort during actin assembly. Curr. Biol. 22, 643–645 (2012)

  • [94]S. Pfender, V. Kuznetsov, S. Pleiser, E. Kerkhoff, M. Schuh: Spire-type actin nucleators cooperate with Formin-2 to drive asymmetric oocyte division. Curr. Biol. 21, 955–60 (2011)

  • [95]M. E. Quinlan, S. Hilgert, A. Bedrossian, R. D. Mullins, E. Kerkhoff: Regulatory interactions between two actin nucleators, Spire and Cappuccino. J. Cell Biol. 179, 117–128 (2007)

  • [96]C. Luxenburg, S. Winograd-Katz, L. Addadi, B. Geiger: Involvement of actin polymerization in podosome dynamics. J. Cell Sci. 125, 1666–72 (2012)

  • [97]S. G. Babb, P. Matsudaira, M. Sato, I. Correia, S. S. Lim: Fimbrin in podosomes of monocyte-derived osteoclasts. Cell Motil. Cytoskeleton 37, 308–325 (1997)

  • [98]J. G. Evans, I. Correia, O. Krasavina, N. Watson, P. Matsudaira: Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J. Cell Biol. 161, 697–705 (2003)

  • [99]A. Li, J. C. Dawson, M. Forero-Vargas, H. J. Spence, X. Yu, I. König, K. Anderson, L. M. Machesky: The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr. Biol. 20, 339–45 (2010)

  • [100]M. R. Milone, B. Pucci, K. Bifulco, F. Iannelli, R. Lombardi, C. Ciardiello, F. Bruzzese, M. V. Carriero, A. Budillon: Proteomic analysis of zoledronic-acid resistant prostate cancer cells unveils novel pathways characterizing an invasive phenotype. Oncotarget 6, 5324–41 (2015)

  • [101]I. Van Audenhove, C. Boucherie, L. Pieters, O. Zwaenepoel, B. Vanloo, E. Martens, C. Verbrugge, G. Hassanzadeh-Ghassabeh, J. Vandekerckhove, M. Cornelissen, A. De Ganck, J. Gettemans: Stratifying fascin and cortactin function in invadopodium formation using inhibitory nanobodies and targeted subcellular delocalization. FASEB J. 28, 1805–18 (2014)

  • [102]C. Bachmann, L. Fischer, U. Walter, M. Reinhard: The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation. J. Biol. Chem. 274, 23549–23557 (1999)

  • [103]M. Barzik, T. I. Kotova, H. N. Higgs, L. Hazelwood, D. Hanein, F. B. Gertler, D. A. Schafer: Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins. J. Biol. Chem. 280, 28653–28662 (2005)

  • [104]U. Philippar, E. T. Roussos, M. Oser, H. Yamaguchi, H.-D. Kim, S. Giampieri, Y. Wang, S. Goswami, J. B. Wyckoff, D. a Lauffenburger, E. Sahai, J. S. Condeelis, F. B. Gertler: A Mena invasion isoform potentiates EGF-induced carcinoma cell invasion and metastasis. Dev. Cell 15, 813–28 (2008)

  • [105]P. J. Goldschmidt-Clermont, M. I. Furman, D. Wachsstock, D. Safer, V. T. Nachmias, T. D. Pollard: The control of actin nucleotide exchange by thymosin beta 4 and profilin. A potential regulatory mechanism for actin polymerization in cells. Mol. Biol. Cell 3, 1015–1024 (1992)

  • [106]A. Valenzuela-Iglesias, V. P. Sharma, B. T. Beaty, Z. Ding, L. E. Gutierrez-Millan, P. Roy, J. S. Condeelis, J. J. Bravo-Cordero: Profilin1 regulates invadopodium maturation in human breast cancer cells. Eur. J. Cell Biol. 94, 78–89 (2015)

  • [107]P. J. Lu, W. R. Shieh, S. G. Rhee, H. L. Yin, C. S. Chen: Lipid products of phosphoinositide 3-kinase bind human profilin with high affinity. Biochemistry 35, 14027–34 (1996)

  • [108]J. D. Rotty, C. Wu, E. M. Haynes, C. Suarez, J. D. Winkelman, H. E. Johnson, J. M. Haugh, D. R. Kovar, J. E. Bear: Profilin-1 serves as a gatekeeper for actin assembly by Arp2/3-dependent and -independent pathways. Dev. Cell 32, 54–67 (2015)

  • [109]B. T. Beaty, V. P. Sharma, J. J. Bravo-Cordero, M. a Simpson, R. J. Eddy, A. J. Koleske, J. Condeelis: β1 integrin regulates Arg to promote invadopodial maturation and matrix degradation. Mol. Biol. Cell 24, 1661–75, (2013)

  • [110]S. L. Gupton, D. Riquelme, S. K. Hughes-Alford, J. Tadros, S. S. Rudina, R. O. Hynes, D. Lauffenburger, F. B. Gertler: Mena binds α5 integrin directly and modulates α5β1 function. J. Cell Biol. 198, 657–676 (2012)

  • [111]S. L. Gupton, C. M. Waterman-Storer: Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361–74 (2006)

  • [112]A. Ponti, M. Machacek, S. L. Gupton, C. M. Waterman-Storer, G. Danuser: Two distinct actin networks drive the protrusion of migrating cells. Science (80 -.) 305, 1782–1786 (2004)

  • [113]T. Akisaka, H. Yoshida, R. Suzuki, K. Takama: Adhesion structures and their cytoskeleton-membrane interactions at podosomes of osteoclasts in culture. Cell Tissue Res. 331, 625–641 (2008)

  • [114]K. van den Dries, M. B. M. Meddens, S. de Keijzer, S. C. Shekhar, V. Subramaniam, C. G. Figdor, A. Cambi: Interplay between myosin IIA-mediated contractility and actin network integrity orchestrates podosome composition and oscillations. Nat. Commun. 4, 1412 (2013)

  • [115]F. Margadant, L. L. Chew, X. Hu, H. Yu, N. Bate, X. Zhang, M. Sheetz: Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin. PLoS Biol. 9, (2011)

  • [116]A. T. Mersich, M. R. Miller, H. Chkourko, S. D. Blystone: The formin FRL1 (FMNL1) is an essential component of macrophage podosomes. Cytoskeleton (Hoboken) 67, 573–85 (2010)

  • [117]R. Bhuwania, S. Cornfine, Z. Fang, M. Kruger, E. J. Luna, S. Linder: Supervillin couples myosin-dependent contractility to podosomes and enables their turnover. J. Cell Sci. 125, 2300–2314 (2012)

  • [118]C. Luxenburg, D. Geblinger, E. Klein, K. Anderson, D. Hanein, B. Geiger, L. Addadi: The architecture of the adhesive apparatus of cultured osteoclasts: from podosome formation to sealing zone assembly. PLoS One 2, e179 (2007)

  • [119]K. Wolf, P. Friedl: Extracellular matrix determinants of proteolytic and non-proteolytic cell migration. Trends Cell Biol. 21, 736–44 (2011)

  • [120]M. Sutoh Yoneyama, S. Hatakeyama, T. Habuchi, T. Inoue, T. Nakamura, T. Funyu, G. Wiche, C. Ohyama, S. Tsuboi: Vimentin intermediate filament and plectin provide a scaffold for invadopodia, facilitating cancer cell invasion and extravasation for metastasis. Eur. J. Cell Biol. 93, 157–169 (2014)

  • [121]K. Kikuchi, K. Takahashi: WAVE2-and microtubule-dependent formation of long protrusions and invasion of cancer cells cultured on three-dimensional extracellular matrices. Cancer Sci. 99, 2252–2259 (2008)

  • [122]Y. H. Zhang, C. Q. Zhao, L. S. Jiang, L. Y. Dai: Substrate stiffness regulates apoptosis and the mRNA expression of extracellular matrix regulatory genes in the rat annular cells. Matrix Biol. 30, 135–144 (2011)

  • [123]X. Jiang, P. F. Austin, R. a Niederhoff, S. R. Manson, J. J. Riehm, B. L. Cook, G. Pengue, K. Chitaley, K. Nakayama, K. I. Nakayama, S. J. Weintraub: Mechanoregulation of proliferation. Mol. Cell. Biol. 29, 5104–5114 (2009)

  • [124]M. W. C. Chan, F. Chaudary, W. Lee, J. W. Copeland, C. McCulloch: Force-induced myofibroblast differentiation through collagen receptors is dependent on mammalian diaphanous (mDia) J. Biol. Chem. 285, 9273–9281 (2010)

  • [125]J. R. Lange, B. Fabry: Cell and tissue mechanics in cell migration. Exp. Cell Res. 319, 2418–23 (2013)

  • [126]C. M. Lo, H. B. Wang, M. Dembo, Y. L. Wang: Cell movement is guided by the rigidity of the substrate. Biophys. J. 79, 144–152 (2000)

  • [127]R. Kirmse, H. Otto, T. Ludwig: Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling. J. Cell Sci. 124, 1857–1866 (2011)

  • [128]I. Levental, K. R. Levental, E. Klein, R. Assoian, R. T. Miller, R. G. Wells, P. a Janmey: A simple indentation device for measuring micrometer-scale tissue stiffness. J. Phys. Condens. Matter 22, 194120 (2010)

  • [129]R. G. Wells: Cellular Sources of Extracellular Matrix in Hepatic Fibrosis. Clin. Liver Dis. 12, 759–768 (2008)

  • [130]D. Duprez, J. N. Cohn: Arterial stiffness as a risk factor for coronary atherosclerosis. Curr. Atheroscler. Rep.9, 139–144 (2007)

  • [131]P. P. Provenzano, D. R. Inman, K. W. Eliceiri, J. G. Knittel, L. Yan, C. T. Rueden, J. G. White, P. J. Keely: Collagen density promotes mammary tumor initiation and progression. BMC Med. 6, 11 (2008)

  • [132]T. Kobayashi, M. Sokabe: Sensing substrate rigidity by mechanosensitive ion channels with stress fibers and focal adhesions. Curr. Opin. Cell Biol. 22, 669–676 (2010)

  • [133]M. J. Paszek, N. Zahir, K. R. Johnson, J. N. Lakins, G. I. Rozenberg, A. Gefen, C. Reinhart-King, S. S. Margulies, M. Dembo, D. Boettiger, D. a. Hammer, V. M. Weaver: Tensional homeostasis and the malignant phenotype. Cancer Cell 8, 241–254 (2005)

  • [134]K. Harris, P. Wild, D. Stopak: Silicone rubber substrata: a new wrinkle in the study of cell locomotion. Science (80 ) 208, 177–179 (1980)

  • [135]R. J. Pelham, Y. L. Wang: Cell locomotion and focal adhesions are regulated by the mechanical properties of the substrate. Biol. Bull. 194, 348–350 (1998)

  • [136]E. C. Yusko, C. L. Asbury: Force is a signal that cells cannot ignore. Mol. Biol. Cell 25, 3717–25 (2014)

  • [137]L. Trichet, J. Le Digabel, R. J. Hawkins, S. R. K. Vedula, M. Gupta, C. Ribrault, P. Hersen, R. Voituriez, B. Ladoux: Evidence of a large-scale mechanosensing mechanism for cellular adaptation to substrate stiffness. Proc. Natl. Acad. Sci. 109, 6933–6938 (2012)

  • [138]S. S. Ranade, R. Syeda, A. Patapoutian: Mechanically Activated Ion Channels. Neuron 87, 1162–79 (2015)

  • [139]A. J. Kuipers, J. Middelbeek, F. N. van Leeuwen: Mechanoregulation of cytoskeletal dynamics by TRP channels. Eur. J. Cell Biol. 91, 834–46 (2012)

  • [140]M. Prager-Khoutorsky, A. Lichtenstein, R. Krishnan, K. Rajendran, A. Mayo, Z. Kam, B. Geiger, A. D. Bershadsky: Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing. Nat. Cell Biol. 13, 1457–1465 (2011)

  • [141]M. Chrzanowska-Wodnicka, K. Burridge: Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403–15 (1996)

  • [142]K. van den Dries, S. F. G. van Helden, J. Te Riet, R. Diez-Ahedo, C. Manzo, M. M. Oud, F. N. van Leeuwen, R. Brock, M. F. Garcia-Parajo, A. Cambi, C. G. Figdor: Geometry sensing by dendritic cells dictates spatial organization and PGE2-induced dissolution of podosomes. Cell. Mol. Life Sci. 69, 1889–1901 (2012)

  • [143]C. Yu, N. B. M. Rafiq, A. Krishnasamy, K. L. Hartman, G. E. Jones, A. D. Bershadsky, M. P. Sheetz: Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces. Cell Rep.5, 1456–68 (2013)

  • [144]G. Burgstaller, M. Gimona: Actin cytoskeleton remodelling via local inhibition of contractility at discrete microdomains. J. Cell Sci. 117, 223–31 (2004)

  • [145]M. Dembo, Y. L. Wang: Stresses at the cell-to-substrate interface during locomotion of fibroblasts. Biophys. J. 76, 2307–16 (1999)

  • [146]Y. Cai, N. Biais, G. Giannone, M. Tanase, G. Jiang, J. M. Hofman, C. H. Wiggins, P. Silberzan, A. Buguin, B. Ladoux, M. P. Sheetz: Nonmuscle myosin IIA-dependent force inhibits cell spreading and drives F-actin flow. Biophys. J. 91, 3907–3920 (2006)

  • [147]S. F. G. van Helden, M. M. Oud, B. Joosten, N. Peterse, C. G. Figdor, F. N. van Leeuwen: PGE2-mediated podosome loss in dendritic cells is dependent on actomyosin contraction downstream of the RhoA-Rho-kinase axis. J. Cell Sci. 121, 1096–106 (2008)

  • [148]N. R. Alexander, K. M. Branch, A. Parekh, E. S. Clark, I. C. Iwueke, S. A. Guelcher, A. M. Weaver: Extracellular matrix rigidity promotes invadopodia activity. Curr. Biol. 18, 1295–1299 (2008)

  • [149]R. J. Jerrell, A. Parekh: Cellular traction stresses mediate extracellular matrix degradation by invadopodia. Acta Biomater. 10, 1886–96 (2014)

  • [150]A. Parekh, N. S. Ruppender, K. M. Branch, M. K. Sewell-Loftin, J. Lin, P. D. Boyer, J. E. Candiello, W. D. Merryman, S. a Guelcher, A. M. Weaver: Sensing and modulation of invadopodia across a wide range of rigidities. Biophys. J. 100, 573–82 (2011)

  • [151]C. V Carman, P. T. Sage, T. E. Sciuto, M. a de la Fuente, R. S. Geha, H. D. Ochs, H. F. Dvorak, A. M. Dvorak, T. a Springer: Transcellular diapedesis is initiated by invasive podosomes. Immunity 26, 784–97 (2007)

  • [152]R. Martinelli, M. Kamei, P. T. Sage, R. Massol, L. Varghese, T. Sciuto, M. Toporsian, A. M. Dvorak, T. Kirchhausen, T. a. Springer, C. V. Carman: Release of cellular tension signals self-restorative ventral lamellipodia to heal barrier micro-wounds. J. Cell Biol. 201, 449–465 (2013)

  • [153]A. Schaefer, J. Te Riet, K. Ritz, M. Hoogenboezem, E. C. Anthony, F. P. J. Mul, C. J. de Vries, M. J. Daemen, C. G. Figdor, J. D. van Buul, P. L. Hordijk: Actin-binding proteins differentially regulate endothelial cell stiffness, ICAM-1 function and neutrophil transmigration. J. Cell Sci. 4470–4482 (2014)

  • [154]A. Juin, E. Planus, F. Guillemot, P. Horakova, C. Albiges-Rizo, E. Génot, J. Rosenbaum, V. Moreau, F. SalTel: Extracellular matrix rigidity controls podosome induction in microvascular endothelial cells. Biol. Cell 105, 46–57 (2013)

  • [155]K. Wolf, M. te Lindert, M. Krause, S. Alexander, J. te Riet, A. L. Willis, R. M. Hoffman, C. G. Figdor, S. J. Weiss, P. Friedl: Physical limits of cell migration: Control by ECM space and nuclear deformation and tuning by proteolysis and traction force. J. Cell Biol. 201, 1069–1084 (2013)

  • [156]A. Aung, Y. N. Seo, S. Lu, Y. Wang, C. Jamora, J. C. Del Álamo, S. Varghese: 3D traction stresses activate protease-dependent invasion of cancer cells. Biophys. J. 107, 2528–37 (2014)

  • [157]A. Juin, J. Di Martino, B. Leitinger, E. Henriet, A.-S. Gary, L. Paysan, J. Bomo, G. Baffet, C. Gauthier-Rouvière, J. Rosenbaum, V. Moreau, F. SalTel: Discoidin domain receptor 1 controls linear invadosome formation via a Cdc42-Tuba pathway. J. Cell Biol. 207, 517–33 (2014)

  • [158]A. Juin, C. Billottet, V. Moreau, O. Destaing, C. Albiges-Rizo, J. Rosenbaum, E. Génot, F. SalTel: Physiological type I collagen organization induces the formation of a novel class of linear invadosomes. Mol. Biol. Cell 23, 297–309 (2012)

  • [159]V. V. Artym, S. Swatkoski, K. Matsumoto, C. B. Campbell, R. J. Petrie, E. K. Dimitriadis, X. Li, S. C. Mueller, T. H. Bugge, M. Gucek, K. M. Yamada: Dense fibrillar collagen is a potent inducer of invadopodia via a specific signaling network. J. Cell Biol. 208, 331–350 (2015)

  • [160]P. J. Wipff, D. B. Rifkin, J. J. Meister, B. Hinz: Myofibroblast contraction activates latent TGF-ß1 from the extracellular matrix. J. Cell Biol. 179, 1311–1323 (2007)

  • [161]L. Buscemi, D. Ramonet, F. Klingberg, A. Formey, J. Smith-Clerc, J. J. Meister, B. Hinz: The single-molecule mechanics of the latent TGF-β1 complex. Curr. Biol. 21, 2046–2054 (2011)

  • [162]A. Labernadie, C. Thibault, C. Vieu, I. Maridonneau-Parini, G. M. Charrière: Dynamics of podosome stiffness revealed by atomic force microscopy. Proc. Natl. Acad. Sci. U. S. A. 107, 21016–21021 (2010)

  • [163]A. Labernadie, A. Bouissou, P. Delobelle, S. Balor, R. Voituriez, A. Proag, I. Fourquaux, C. Thibault, C. Vieu, R. Poincloux, G. M. Charrière, I. Maridonneau-Parini: Protrusion force microscopy reveals oscillatory force generation and mechanosensing activity of human macrophage podosomes. Nat. Commun. 5, 5343 (2014)

  • [164]A. Proag, A. Bouissou, T. Mangeat, R. Voituriez, P. Delobelle, C. Thibault, C. Vieu, I. Maridonneau-Parini, R. Poincloux: Working together: spatial synchrony in the force and actin dynamics of podosome first neighbors. ACS Nano 9, 3800–13 (2015)

  • [165]O. Collin, P. Tracqui, A. Stephanou, Y. Usson, J. Clément-Lacroix, E. Planus: Spatiotemporal dynamics of actin-rich adhesion microdomains: influence of substrate flexibility. J. Cell Sci. 119, 1914–25 (2006)

  • [166]O. Collin, S. Na, F. Chowdhury, M. Hong, M. E. Shin, F. Wang, N. Wang: Self-organized podosomes are dynamic mechanosensors. Curr. Biol. 18, 1288–1294 (2008)

  • [167]C. Varon, F. Tatin, V. Moreau, E. Van Obberghen-schilling, S. Fernandez-sauze, E. Reuzeau, I. Kramer, E. Génot: Transforming Growth Factor β Induces Rosettes of Podosomes in Primary Aortic Endothelial Cells. Mol. Cell. Biochem. 26, 3582–3594 (2006)

  • [168]R. L. Berdeaux, B. Díaz, L. Kim, G. S. Martin: Active Rho is localized to podosomes induced by oncogenic Src and is required for their assembly and function. J. Cell Biol. 166, 317–23 (2004)

  • [169]F. Tatin, C. Varon, E. Génot, V. Moreau: A signalling cascade involving PKC, Src and Cdc42 regulates podosome assembly in cultured endothelial cells in response to phorbol ester. J. Cell Sci. 119, 769–81 (2006)

  • [170]Y. R. Pan, C. L. Chen, H. C. Chen: FAK is required for the assembly of podosome rosettes. J. Cell Biol. 195, 113–129 (2011)

  • [171]Y.R. Pan, K.H. Cho, H.H. Lee, Z.F. Chang, H.C. Chen: Protein tyrosine phosphatase SHP2 suppresses podosome rosette formation in Src-transformed fibroblasts. J. Cell Sci. 126, 657–66 (2013)

  • [172]D. Geblinger, C. Zink, N. D. Spencer, L. Addadi, B. Geiger: Effects of surface microtopography on the assembly of the osteoclast resorption apparatus. J. R. Soc. Interface 9, 1599–608 (2012)

  • [173]F. Anderegg, D. Geblinger, P. Horvath, M. Charnley, M. Textor, L. Addadi, B. Geiger: Substrate adhesion regulates sealing zone architecture and dynamics in cultured osteoclasts. PLoS One 6, (2011)

  • [174]E. J. Hagedorn, D. R. Sherwood: Cell invasion through basement membrane: the anchor cell breaches the barrier. Curr. Opin. Cell Biol. 23, 589–96 (2011)

  • [175]C. Seiler, G. Davuluri, J. Abrams, F. J. Byfield, P. Janmey, M. Pack: Smooth Muscle Tension Induces Invasive Remodeling of the Zebrafish Intestine. PLoS Biol. 10, (2012)

  • [176]H. S. Leong, A. E. Robertson, K. Stoletov, S. J. Leith, C. A. Chin, A. E. Chien, M. N. Hague, A. Ablack, K. Carmine-Simmen, V. A. McPherson, C. O. Postenka, E. A. Turley, S. A. Courtneidge, A. F. Chambers, J. D. Lewis: Invadopodia Are Required for Cancer Cell Extravasation and Are a Therapeutic Target for Metastasis. Cell Rep.8, 1558–1570 (2014)

  • [177]J. Condeelis, J. E. Segall: Intravital imaging of cell movement in tumours. Nat. Rev. Cancer 3, 921–930 (2003)

  • [178]E. Beerling, L. Ritsma, N. Vrisekoop, P. W. B. Derksen, J. van Rheenen: Intravital microscopy: new insights into metastasis of tumors. J. Cell Sci. 124, 299–310 (2011)

  • [179]P. Friedl, S. Alexander: Cancer invasion and the microenvironment: Plasticity and reciprocity. Cell 147, 992–1009 (2011)

  • [180]C. Cougoule, V. Le Cabec, R. Poincloux, T. Al Saati, J. L. Mége, G. Tabouret, C. Lowell, N. Laviolette-Malirat, I. Maridonneau-Parini: Three-dimensional migration of macrophages requires Hck for podosome organization and extracellular matrix proteolysis. Blood 115, 1444–1452 (2010)

  • [181]E. Van Goethem, R. Guiet, S. Balor, G. M. Charrière, R. Poincloux, A. Labrousse, I. Maridonneau-Parini, V. Le Cabec: Macrophage podosomes go 3D. Eur. J. Cell Biol. 90, 224–36 (2011)

  • [182]X. Yu, T. Zech, L. McDonald, E. G. Gonzalez, A. Li, I. Macpherson, J. P. Schwarz, H. Spence, K. Futó, P. Timpson, C. Nixon, Y. Ma, I. M. Anton, B. Visegrády, R. H. Insall, K. Oien, K. Blyth, J. C. Norman, L. M. Machesky: N-WASP coordinates the delivery and F-actin-mediated capture of MT1-MMP at invasive pseudopods. J. Cell Biol. 199, 527–44 (2012)

  • [183]K. Wolf, Y. I. Wu, Y. Liu, J. Geiger, E. Tam, C. Overall, M. S. Stack, P. Friedl: Multi-step pericellular proteolysis controls the transition from individual to collective cancer cell invasion. Nat. Cell Biol. 9, 893–904 (2007)

  • [184]O. Tolde, D. Rösel, P. Veselý, P. Folk, J. Brábek: The structure of invadopodia in a complex 3D environment. Eur. J. Cell Biol. 89, 674–680 (2010)

  • [185]K. Stoletov, J. D. Lewis: Invadopodia: a new therapeutic target to block cancer metastasis. Expert Rev. Anticancer Ther 15, 733–735 (2015)

  • [186]E. J. Hagedorn, L. C. Kelley, K. M. Naegeli, Z. Wang, Q. Chi, D. R. Sherwood: ADF/cofilin promotes invadopodial membrane recycling during cell invasion in vivo. J. Cell Biol. 204, 1209–1218 (2014)

  • [187]A. Parekh, A. M. Weaver: Regulation of cancer invasiveness by the physical extracellular matrix environment. Cell Adhes. Migr. 3, 288–292 (2009)

  • [188]A. D. Celiz, J. G. W. Smith, R. Langer, D. G. Anderson, D. A. Winkler, D. A. Barrett, M. C. Davies, L. E. Young, C. Denning, M. R. Alexander: Materials for stem cell factories of the future. Nat. Mater. 13, 570–579 (2014)

  • [189]J. T. Finer, R. M. Simmons, J. Spudich: Single myosin molecule mechanics: piconewton forces and nanometre steps. Nature 368, 113–119 (1994)

  • [190]R. Huang, G.-J. Cao, H. Guo, J. Kordowska, C.L. Albert Wang: Direct interaction between caldesmon and cortactin. Arch. Biochem. Biophys. 456, 175–82 (2006)

  • [191]O. Thoumine, P. Kocian,A. Kottelat, J. J. Meister: Short-term binding of fibroblasts to fibronectin: optical tweezers experiments and probabilistic analysis. Eur. Biophys. J. 29, 398–408 (2000)

  • [192]F. Kong, A. J. García, P. Mould, M. J. Humphries, C. Zhu: Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 185, 1275–1284 (2009)

  • [193]M. Yao, B. T. Goult, H. Chen, P. Cong, M. P. Sheetz, J. Yan: Mechanical activation of vinculin binding to talin locks talin in an unfolded conformation. Sci. Rep.4, 4610 (2014)

  • [194]C. Grashoff, B. D. Hoffman, M. D. Brenner, R. Zhou, M. Parsons, M. T. Yang, M. McLean, S. G. Sligar, C. S. Chen, T. Ha, M. Schwartz: Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics. Nature 466, 263–266 (2010)

  • [195]N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, a Bershadsky, L. Addadi, B. Geiger: Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates. Nat. Cell Biol. 3, 466–472 (2001)

  • [196]J. Fu, Y.-K. Wang, M. T. Yang, R. Desai, X. Yu, Z. Liu, C. S. Chen: Mechanical regulation of cell function with geometrically modulated elastomeric substrates. Nat. Methods 7, 733–736 (2010)

  • [197]A. Aung, Y. N. Seo, S. Lu, Y. Wang, C. Jamora, J. C. Del Álamo, S. Varghese: 3D Traction Stresses Activate Protease-Dependent Invasion of Cancer Cells. Biophys. J. 107, 2528–2537 (2014)

  • [198]J. L. Tan, J. Tien, D. M. Pirone, D. S. Gray, K. Bhadriraju, C. S. Chen: Cells lying on a bed of microneedles: an approach to isolate mechanical force. Proc. Natl. Acad. Sci. U. S. A. 100, 1484–1489 (2003)

  • [199]B. S. Elkin, E. U. Azeloglu, K. D. Costa, B. Morrison: Mechanical heterogeneity of the rat hippocampus measured by atomic force microscope indentation. J. Neurotrauma 24, 812–822 (2007)

  • [200]A. Samani, J. Zubovits, D. Plewes: Elastic moduli of normal and pathological human breast tissues: an inversion-technique-based investigation of 169 samples. Phys. Med. Biol. 52, 1565–1576 (2007)

  • [201]R. M. Lang, B. P. Cholley, C. Korcarz, R. H. Marcus, S. G. Shroff: Measurement of regional elastic properties of the human aorta. A new application of transesophageal echocardiography with automated border detection and calibrated subclavian pulse tracings. Circulation 90, 1875–82 (1994)

  • [202]M. B. Schaffler, D. B. Burr: Stiffness of compact bone: effects of porosity and density. J. Biomech. 21, 13–16 (1988)

  • [203]S. W. Moore, P. Roca-Cusachs, M. P. Sheetz: Stretchy proteins on stretchy substrates: The important elements of integrin-mediated rigidity sensing. Dev. Cell 19, 194–206 (2010)

  • [204]A. J. S. Ribeiro, A. K. Denisin, R. E. Wilson, B. L. Pruitt: For whom the cells pull: Hydrogel and micropost devices for measuring traction forces. Methods (2015)

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Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on imrpress.com as a courtesy and upon agreement with Frontiers in Bioscience.

1 Jun 2016Review
Invadosomes – shaping actin networks to follow mechanical cues
Katarzyna M Kedziora 1, Tadamoto Isogai 2, Kees Jalink 1, Metello Innocenti 2,*
Affiliations
Article Info

1 Division of Cell Biology I, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam, 1066 CX, The Netherlands

2 Division of Molecular Genetics, The Netherlands Cancer Institute, Plesmanlaan 121, Amsterdam, 1066 CX, The Netherlands

Abstract

Invadosomes are actin-based protrusions formed by cells in response to obstacles in their microenvironment, especially basement membranes and dense interstitial matrices. A versatile set of proteins controls assembly and dynamics of the actin networks at invadosomes and adhesive molecules link them with the extracellular matrix. Furthermore, polarized delivery of proteases makes invadosomes degradative. Therefore, invadosomes have been classically viewed as specialized protrusions involved in cell migration and remodeling of the microenvironment. Recent discoveries have considerably broadened this picture by showing that invadosomes respond to traction forces and can self-organize into dynamic arrays capable of following the topography of the substrate. Although these findings suggest that invadosomes may function as mechanosensors, this possibility has not been critically evaluated. In this review, we first summarize the organization and dynamics of actin in invadosomes and their superstructures with emphasis on force-production mechanisms. Next, we outline our current understanding of how mechanical cues impinge on invadosomes and modify their behavior. From this perspective, we provide an outlook of the outstanding open questions and the main challenges in the field.

Keywords

  • Invadosomes
  • Invadopodia
  • Podosomes
  • Actin
  • Mechanobiology
  • Review

References