메뉴 건너뛰기




Volumn 129, Issue 2, 2016, Pages 298-313

The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes

Author keywords

FHOD1; Formins; INF2; Macrophages; Podosomes

Indexed keywords

ACTIN; PROTEIN DERIVATIVE; PROTEIN FHOD1; PROTEIN INF2; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; FETOPROTEIN; FHOD1 PROTEIN, HUMAN; INF2 PROTEIN, HUMAN; NUCLEAR PROTEIN;

EID: 84957831437     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.177691     Document Type: Article
Times cited : (52)

References (69)
  • 1
    • 39149112463 scopus 로고    scopus 로고
    • Adhesion structures and their cytoskeleton-membrane interactions at podosomes of osteoclasts in culture
    • Akisaka, T., Yoshida, H., Suzuki, R. and Takama, K. (2008). Adhesion structures and their cytoskeleton-membrane interactions at podosomes of osteoclasts in culture. Cell Tissue Res. 331, 625-641.
    • (2008) Cell Tissue Res , vol.331 , pp. 625-641
    • Akisaka, T.1    Yoshida, H.2    Suzuki, R.3    Takama, K.4
  • 2
    • 78650666890 scopus 로고    scopus 로고
    • Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes
    • Andres-Delgado, L., Anton, O. M., Madrid, R., Byrne, J. A. and Alonso, M. A. (2010). Formin INF2 regulates MAL-mediated transport of Lck to the plasma membrane of human T lymphocytes. Blood 116, 5919-5929.
    • (2010) Blood , vol.116 , pp. 5919-5929
    • Andres-Delgado, L.1    Anton, O.M.2    Madrid, R.3    Byrne, J.A.4    Alonso, M.A.5
  • 3
    • 84922265237 scopus 로고    scopus 로고
    • FHOD proteins in actin dynamics-a formin' class of its own
    • Bechtold, M., Schultz, J. and Bogdan, S. (2014). FHOD proteins in actin dynamics-a formin' class of its own. Small GTPases 5, e973765.
    • (2014) Small GTPases , vol.5
    • Bechtold, M.1    Schultz, J.2    Bogdan, S.3
  • 4
    • 84862850308 scopus 로고    scopus 로고
    • Supervillin couples myosin-dependent contractility to podosomes and enables their turnover
    • Bhuwania, R., Cornfine, S., Fang, Z., Kruger, M., Luna, E. J. and Linder, S. (2012). Supervillin couples myosin-dependent contractility to podosomes and enables their turnover. J. Cell Sci. 125, 2300-2314.
    • (2012) J. Cell Sci , vol.125 , pp. 2300-2314
    • Bhuwania, R.1    Cornfine, S.2    Fang, Z.3    Kruger, M.4    Luna, E.J.5    Linder, S.6
  • 7
    • 19344362697 scopus 로고    scopus 로고
    • Podosome-mediated matrix resorption and cell motility in vascular smooth muscle cells
    • Burgstaller, G. and Gimona, M. (2005). Podosome-mediated matrix resorption and cell motility in vascular smooth muscle cells. Am. J. Physiol. Heart Circ. Physiol. 288, H3001-H3005.
    • (2005) Am. J. Physiol. Heart Circ. Physiol , vol.288 , pp. H3001-H3005
    • Burgstaller, G.1    Gimona, M.2
  • 8
    • 84867400931 scopus 로고    scopus 로고
    • Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres
    • Cervero, P., Himmel, M., Krüger, M. and Linder, S. (2012). Proteomic analysis of podosome fractions from macrophages reveals similarities to spreading initiation centres. Eur. J. Cell Biol. 91, 908-922.
    • (2012) Eur. J. Cell Biol , vol.91 , pp. 908-922
    • Cervero, P.1    Himmel, M.2    Krüger, M.3    Linder, S.4
  • 9
    • 84934437503 scopus 로고    scopus 로고
    • Podosome reformation in macrophages: assays and analysis
    • Cervero, P., Panzer, L. and Linder, S. (2013). Podosome reformation in macrophages: assays and analysis. Methods Mol. Biol. 1046, 97-121.
    • (2013) Methods Mol. Biol , vol.1046 , pp. 97-121
    • Cervero, P.1    Panzer, L.2    Linder, S.3
  • 11
    • 0034695921 scopus 로고    scopus 로고
    • Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength
    • Chellaiah, M., Kizer, N., Silva, M., Alvarez, U., Kwiatkowski, D. and Hruska, K. A. (2000). Gelsolin deficiency blocks podosome assembly and produces increased bone mass and strength. J. Cell Biol. 148, 665-678.
    • (2000) J. Cell Biol , vol.148 , pp. 665-678
    • Chellaiah, M.1    Kizer, N.2    Silva, M.3    Alvarez, U.4    Kwiatkowski, D.5    Hruska, K.A.6
  • 12
    • 0009720961 scopus 로고
    • An in vitro cell invasion assay: determination of cell surface proteolytic activity that degrades extracellular matrix
    • Chen, W. T., Yeh, Y., and Nakahara, H. (1994). An in vitro cell invasion assay: determination of cell surface proteolytic activity that degrades extracellular matrix. J. Tissue Culture Meth. 16, 177-181.
    • (1994) J. Tissue Culture Meth , vol.16 , pp. 177-181
    • Chen, W.T.1    Yeh, Y.2    Nakahara, H.3
  • 13
    • 33748745132 scopus 로고    scopus 로고
    • INF2 is a WASP homology 2 motifcontaining formin that severs actin filaments and accelerates both polymerization and depolymerization
    • Chhabra, E. S. and Higgs, H. N. (2006). INF2 is a WASP homology 2 motifcontaining formin that severs actin filaments and accelerates both polymerization and depolymerization. J. Biol. Chem. 281, 26754-26767.
    • (2006) J. Biol. Chem , vol.281 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 14
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra, E. S. and Higgs, H. N. (2007). The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 9, 1110-1121.
    • (2007) Nat. Cell Biol , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 15
    • 67650566835 scopus 로고    scopus 로고
    • INF2 is an endoplasmic reticulum-associated formin protein
    • Chhabra, E. S., Ramabhadran, V., Gerber, S. A. and Higgs, H. N. (2009). INF2 is an endoplasmic reticulum-associated formin protein. J. Cell Sci. 122, 1430-1440.
    • (2009) J. Cell Sci , vol.122 , pp. 1430-1440
    • Chhabra, E.S.1    Ramabhadran, V.2    Gerber, S.A.3    Higgs, H.N.4
  • 17
    • 0037329229 scopus 로고    scopus 로고
    • Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein
    • Destaing, O., Saltel, F., Geminard, J.-C., Jurdic, P. and Bard, F. (2003). Podosomes display actin turnover and dynamic self-organization in osteoclasts expressing actin-green fluorescent protein. Mol. Biol. Cell 14, 407-416.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 407-416
    • Destaing, O.1    Saltel, F.2    Geminard, J.-C.3    Jurdic, P.4    Bard, F.5
  • 18
    • 23744515800 scopus 로고    scopus 로고
    • A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts
    • Destaing, O., Saltel, F., Gilquin, B., Chabadel, A., Khochbin, S., Ory, S. and Jurdic, P. (2005). A novel Rho-mDia2-HDAC6 pathway controls podosome patterning through microtubule acetylation in osteoclasts. J. Cell Sci. 118, 2901-2911.
    • (2005) J. Cell Sci , vol.118 , pp. 2901-2911
    • Destaing, O.1    Saltel, F.2    Gilquin, B.3    Chabadel, A.4    Khochbin, S.5    Ory, S.6    Jurdic, P.7
  • 19
    • 0037512351 scopus 로고    scopus 로고
    • Macrophage podosomes assemble at the leading lamella by growth and fragmentation
    • Evans, J. G., Correia, I., Krasavina, O., Watson, N. and Matsudaira, P. (2003). Macrophage podosomes assemble at the leading lamella by growth and fragmentation. J. Cell Biol. 161, 697-705.
    • (2003) J. Cell Biol , vol.161 , pp. 697-705
    • Evans, J.G.1    Correia, I.2    Krasavina, O.3    Watson, N.4    Matsudaira, P.5
  • 20
    • 77953427107 scopus 로고    scopus 로고
    • The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility
    • Fang, Z., Takizawa, N., Wilson, K. A., Smith, T. C., Delprato, A., Davidson, M.W., Lambright, D. G. and Luna, E. J. (2010). The membrane-associated protein, supervillin, accelerates F-actin-dependent rapid integrin recycling and cell motility. Traffic 11, 782-799.
    • (2010) Traffic , vol.11 , pp. 782-799
    • Fang, Z.1    Takizawa, N.2    Wilson, K.A.3    Smith, T.C.4    Delprato, A.5    Davidson, M.W.6    Lambright, D.G.7    Luna, E.J.8
  • 21
    • 18844404975 scopus 로고    scopus 로고
    • FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation
    • Gasteier, J. E., Schroeder, S., Muranyi, W., Madrid, R., Benichou, S. and Fackler, O. T. (2005). FHOD1 coordinates actin filament and microtubule alignment to mediate cell elongation. Exp. Cell Res. 15, 192-202.
    • (2005) Exp. Cell Res , vol.15 , pp. 192-202
    • Gasteier, J.E.1    Schroeder, S.2    Muranyi, W.3    Madrid, R.4    Benichou, S.5    Fackler, O.T.6
  • 23
    • 84875460283 scopus 로고    scopus 로고
    • Dendritic cell podosome dynamics does not depend on the F-actin regulator SWAP-70
    • Gotz, A. and Jessberger, R. (2013). Dendritic cell podosome dynamics does not depend on the F-actin regulator SWAP-70. PLoS ONE 8, e60642.
    • (2013) PLoS ONE , vol.8
    • Gotz, A.1    Jessberger, R.2
  • 24
    • 33749242977 scopus 로고    scopus 로고
    • PAK4 and alphaPIX determine podosome size and number in macrophages through localized actin regulation
    • Gringel, A., Walz, D., Rosenberger, G., Minden, A., Kutsche, K., Kopp, P. and Linder, S. (2006). PAK4 and alphaPIX determine podosome size and number in macrophages through localized actin regulation. J. Cell Physiol. 209, 568-579.
    • (2006) J. Cell Physiol , vol.209 , pp. 568-579
    • Gringel, A.1    Walz, D.2    Rosenberger, G.3    Minden, A.4    Kutsche, K.5    Kopp, P.6    Linder, S.7
  • 26
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: a domain-based approach
    • Higgs, H. N. (2005). Formin proteins: a domain-based approach. Trends Biochem. Sci. 30, 342-353.
    • (2005) Trends Biochem. Sci , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 27
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes, R. O. (2009). The extracellular matrix: not just pretty fibrils. Science 326, 1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 28
  • 29
    • 0348143126 scopus 로고    scopus 로고
    • Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains
    • Kaverina, I., Stradal, T. E. B. and Gimona, M. (2003). Podosome formation in cultured A7r5 vascular smooth muscle cells requires Arp2/3-dependent de-novo actin polymerization at discrete microdomains. J. Cell Sci. 116, 4915-4924.
    • (2003) J. Cell Sci , vol.116 , pp. 4915-4924
    • Kaverina, I.1    Stradal, T.E.B.2    Gimona, M.3
  • 30
    • 0038325646 scopus 로고    scopus 로고
    • The formin-homology-domain-containing protein FHOD1 enhances cell migration
    • Koka, S., Neudauer, C. L., Li, X., Lewis, R. E., McCarthy, J. B. and Westendorf, J. J. (2003). The formin-homology-domain-containing protein FHOD1 enhances cell migration. J. Cell Sci. 116, 1745-1755.
    • (2003) J. Cell Sci , vol.116 , pp. 1745-1755
    • Koka, S.1    Neudauer, C.L.2    Li, X.3    Lewis, R.E.4    McCarthy, J.B.5    Westendorf, J.J.6
  • 32
    • 84872769447 scopus 로고    scopus 로고
    • An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2
    • Korobova, F., Ramabhadran, V. and Higgs, H. N. (2013). An actin-dependent step in mitochondrial fission mediated by the ER-associated formin INF2. Science 339, 464-467.
    • (2013) Science , vol.339 , pp. 464-467
    • Korobova, F.1    Ramabhadran, V.2    Higgs, H.N.3
  • 33
    • 84894363564 scopus 로고    scopus 로고
    • A role for myosin II in mammalian mitochondrial fission
    • Korobova, F., Gauvin, T. J. and Higgs, H. N. (2014). A role for myosin II in mammalian mitochondrial fission. Curr. Biol. 24, 409-414.
    • (2014) Curr. Biol , vol.24 , pp. 409-414
    • Korobova, F.1    Gauvin, T.J.2    Higgs, H.N.3
  • 34
    • 84903978020 scopus 로고    scopus 로고
    • Formins as effector proteins of Rho GTPases
    • Kuhn, S. and Geyer, M. (2014). Formins as effector proteins of Rho GTPases. Small GTPases 5, e29513.
    • (2014) Small GTPases , vol.5
    • Kuhn, S.1    Geyer, M.2
  • 37
    • 84896871185 scopus 로고    scopus 로고
    • The Drosophila FHOD1-like formin Knittrig acts through Rok to promote stress fiber formation and directed macrophage migration during the cellular immune response
    • Lammel, U., Bechtold, M., Risse, B., Berh, D., Fleige, A., Bunse, I., Jiang, X., Klambt, C. and Bogdan, S. (2014). The Drosophila FHOD1-like formin Knittrig acts through Rok to promote stress fiber formation and directed macrophage migration during the cellular immune response. Development 141, 1366-1380.
    • (2014) Development , vol.141 , pp. 1366-1380
    • Lammel, U.1    Bechtold, M.2    Risse, B.3    Berh, D.4    Fleige, A.5    Bunse, I.6    Jiang, X.7    Klambt, C.8    Bogdan, S.9
  • 38
    • 33847343034 scopus 로고    scopus 로고
    • The matrix corroded: podosomes and invadopodia in extracellular matrix degradation
    • Linder, S. (2007). The matrix corroded: podosomes and invadopodia in extracellular matrix degradation. Trends Cell Biol. 17, 107-117.
    • (2007) Trends Cell Biol , vol.17 , pp. 107-117
    • Linder, S.1
  • 39
    • 0038433238 scopus 로고    scopus 로고
    • Podosomes: adhesion hot-spots of invasive cells
    • Linder, S. and Aepfelbacher, M. (2003). Podosomes: adhesion hot-spots of invasive cells. Trends Cell Biol. 13, 376-385.
    • (2003) Trends Cell Biol , vol.13 , pp. 376-385
    • Linder, S.1    Aepfelbacher, M.2
  • 40
    • 84925229596 scopus 로고    scopus 로고
    • Tools of the trade: podosomes as multipurpose organelles of monocytic cells
    • Linder, S. and Wiesner, C. (2015). Tools of the trade: podosomes as multipurpose organelles of monocytic cells. Cell. Mol. Life Sci. 72, 121-135.
    • (2015) Cell. Mol. Life Sci , vol.72 , pp. 121-135
    • Linder, S.1    Wiesner, C.2
  • 41
    • 0034234559 scopus 로고    scopus 로고
    • The polarization defect of Wiskott-Aldrich syndrome macrophages is linked to dislocalization of the Arp2/3 complex
    • Linder, S., Higgs, H., Hufner, K., Schwarz, K., Pannicke, U. and Aepfelbacher, M. (2000a). The polarization defect of Wiskott-Aldrich syndrome macrophages is linked to dislocalization of the Arp2/3 complex. J. Immunol. 165, 221-225.
    • (2000) J. Immunol , vol.165 , pp. 221-225
    • Linder, S.1    Higgs, H.2    Hufner, K.3    Schwarz, K.4    Pannicke, U.5    Aepfelbacher, M.6
  • 42
    • 0034536206 scopus 로고    scopus 로고
    • Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages
    • Linder, S., Hufner, K., Wintergerst, U. and Aepfelbacher, M. (2000b). Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages. J. Cell Sci. 113, 4165-4176.
    • (2000) J. Cell Sci , vol.113 , pp. 4165-4176
    • Linder, S.1    Hufner, K.2    Wintergerst, U.3    Aepfelbacher, M.4
  • 43
    • 80054031825 scopus 로고    scopus 로고
    • Degrading devices: invadosomes in proteolytic cell invasion
    • Linder, S., Wiesner, C. and Himmel, M. (2011). Degrading devices: invadosomes in proteolytic cell invasion. Annu. Rev. Cell Dev. Biol. 27, 185-211.
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 185-211
    • Linder, S.1    Wiesner, C.2    Himmel, M.3
  • 44
    • 55249119822 scopus 로고    scopus 로고
    • The architecture of the adhesive apparatus of cultured osteoclasts: from podosome formation to sealing zone assembly
    • Luxenburg, C., Geblinger, D., Klein, E., Anderson, K., Hanein, D., Geiger, B. and Addadi, L. (2007). The architecture of the adhesive apparatus of cultured osteoclasts: from podosome formation to sealing zone assembly. PLoS ONE 2, e179.
    • (2007) PLoS ONE , vol.2
    • Luxenburg, C.1    Geblinger, D.2    Klein, E.3    Anderson, K.4    Hanein, D.5    Geiger, B.6    Addadi, L.7
  • 45
    • 84863084225 scopus 로고    scopus 로고
    • Involvement of actin polymerization in podosome dynamics
    • Luxenburg, C., Winograd-Katz, S., Addadi, L. and Geiger, B. (2012). Involvement of actin polymerization in podosome dynamics. J. Cell Sci. 125, 1666-1672.
    • (2012) J. Cell Sci , vol.125 , pp. 1666-1672
    • Luxenburg, C.1    Winograd-Katz, S.2    Addadi, L.3    Geiger, B.4
  • 47
    • 21744445075 scopus 로고    scopus 로고
    • Regulation of myosin II during cytokinesis in higher eukaryotes
    • Matsumura, F. (2005). Regulation of myosin II during cytokinesis in higher eukaryotes. Trends Cell Biol. 15, 371-377.
    • (2005) Trends Cell Biol , vol.15 , pp. 371-377
    • Matsumura, F.1
  • 48
    • 0027999246 scopus 로고
    • Differential localization of myosin-II isozymes in human cultured cells and blood cells
    • Maupin, P., Phillips, C. L., Adelstein, R. S. and Pollard, T. D. (1994). Differential localization of myosin-II isozymes in human cultured cells and blood cells. J. Cell Sci. 107, 3077-3090.
    • (1994) J. Cell Sci , vol.107 , pp. 3077-3090
    • Maupin, P.1    Phillips, C.L.2    Adelstein, R.S.3    Pollard, T.D.4
  • 49
    • 78149299771 scopus 로고    scopus 로고
    • The formin FRL1 (FMNL1) is an essential component of macrophage podosomes
    • Mersich, A. T., Miller, M. R., Chkourko, H. and Blystone, S. D. (2010). The formin FRL1 (FMNL1) is an essential component of macrophage podosomes. Cytoskeleton 67, 573-585.
    • (2010) Cytoskeleton , vol.67 , pp. 573-585
    • Mersich, A.T.1    Miller, M.R.2    Chkourko, H.3    Blystone, S.D.4
  • 50
    • 79959541003 scopus 로고    scopus 로고
    • The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function
    • Murphy, D. A. and Courtneidge, S. A. (2011). The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12, 413-426.
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 413-426
    • Murphy, D.A.1    Courtneidge, S.A.2
  • 52
    • 20444391054 scopus 로고    scopus 로고
    • Subconfluent endothelial cells form podosomes downstream of cytokine and RhoGTPase signaling
    • Osiak, A.-E., Zenner, G. and Linder, S. (2005). Subconfluent endothelial cells form podosomes downstream of cytokine and RhoGTPase signaling. Exp. Cell Res. 307, 342-353.
    • (2005) Exp. Cell Res , vol.307 , pp. 342-353
    • Osiak, A.-E.1    Zenner, G.2    Linder, S.3
  • 53
    • 0034865951 scopus 로고    scopus 로고
    • Podosomes in osteoclast-like cells: structural analysis and cooperative roles of paxillin, proline-rich tyrosine kinase 2 (Pyk2) and integrin alphaVbeta3
    • Pfaff, M. and Jurdic, P. (2001). 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) J. Cell Sci , vol.114 , pp. 2775-2786
    • Pfaff, M.1    Jurdic, P.2
  • 55
    • 84055217451 scopus 로고    scopus 로고
    • Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture
    • Ramabhadran, V., Korobova, F., Rahme, G. J. and Higgs, H. N. (2011). Splice variant-specific cellular function of the formin INF2 in maintenance of Golgi architecture. Mol. Biol. Cell 22, 4822-4833.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4822-4833
    • Ramabhadran, V.1    Korobova, F.2    Rahme, G.J.3    Higgs, H.N.4
  • 56
    • 84867251545 scopus 로고    scopus 로고
    • Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing
    • Ramabhadran, V., Gurel, P. S. and Higgs, H. N. (2012). Mutations to the formin homology 2 domain of INF2 protein have unexpected effects on actin polymerization and severing. J. Biol. Chem. 287, 34234-34245.
    • (2012) J. Biol. Chem , vol.287 , pp. 34234-34245
    • Ramabhadran, V.1    Gurel, P.S.2    Higgs, H.N.3
  • 57
    • 65249155429 scopus 로고    scopus 로고
    • Protease-dependent versus-independent cancer cell invasion programs: three-dimensional amoeboid movement revisited
    • Sabeh, F., Shimizu-Hirota, R. and Weiss, S. J. (2009). Protease-dependent versus-independent cancer cell invasion programs: three-dimensional amoeboid movement revisited. J. Cell Biol. 185, 11-19.
    • (2009) J. Cell Biol , vol.185 , pp. 11-19
    • Sabeh, F.1    Shimizu-Hirota, R.2    Weiss, S.J.3
  • 58
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: a molecular view on the regulation of human formins
    • Schonichen, A. and Geyer, M. (2010). Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim. Biophys. Acta 1803, 152-163.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 152-163
    • Schonichen, A.1    Geyer, M.2
  • 60
    • 84897467341 scopus 로고    scopus 로고
    • FHOD1 regulates stress fiber organization by controlling the dynamics of transverse arcs and dorsal fibers
    • Schulze, N., Graessl, M., Blancke Soares, A., Geyer, M., Dehmelt, L. and Nalbant, P. (2014). FHOD1 regulates stress fiber organization by controlling the dynamics of transverse arcs and dorsal fibers. J. Cell Sci. 127, 1379-1393.
    • (2014) J. Cell Sci , vol.127 , pp. 1379-1393
    • Schulze, N.1    Graessl, M.2    Blancke Soares, A.3    Geyer, M.4    Dehmelt, L.5    Nalbant, P.6
  • 62
    • 33747877557 scopus 로고    scopus 로고
    • The Kindlins: subcellular localization and expression during murine development
    • Ussar, S., Wang, H.-V., Linder, S., Fässler, R. and Moser, M. (2006). The Kindlins: subcellular localization and expression during murine development. Exp. Cell Res. 312, 3142-3151.
    • (2006) Exp. Cell Res , vol.312 , pp. 3142-3151
    • Ussar, S.1    Wang, H.-V.2    Linder, S.3    Fässler, R.4    Moser, M.5
  • 63
    • 84879170343 scopus 로고    scopus 로고
    • Interplay between myosin IIA-mediated contractility and actin network integrity orchestrates podosome composition and oscillations
    • van den Dries, K., Meddens, M. B. M., de Keijzer, S., Shekhar, S., Subramaniam, V., Figdor, C. G. and Cambi, A. (2013a). Interplay between myosin IIA-mediated contractility and actin network integrity orchestrates podosome composition and oscillations. Nat. Commun. 4, 1412.
    • (2013) Nat. Commun , vol.4 , pp. 1412
    • van den Dries, K.1    Meddens, M.B.M.2    de Keijzer, S.3    Shekhar, S.4    Subramaniam, V.5    Figdor, C.G.6    Cambi, A.7
  • 66
    • 0027524780 scopus 로고
    • Non-sarcomeric mode of myosin II organization in the fibroblast lamellum
    • Verkhovsky, A. B. and Borisy, G. G. (1993). Non-sarcomeric mode of myosin II organization in the fibroblast lamellum. J. Cell Biol. 123, 637-652.
    • (1993) J. Cell Biol , vol.123 , pp. 637-652
    • Verkhovsky, A.B.1    Borisy, G.G.2
  • 68
    • 84880662092 scopus 로고    scopus 로고
    • A specific subset of RabGTPases controls cell surface exposure of MT1-MMP, extracellular matrix degradation and three-dimensional invasion of macrophages
    • Wiesner, C., El Azzouzi, K. and Linder, S. (2013). A specific subset of RabGTPases controls cell surface exposure of MT1-MMP, extracellular matrix degradation and three-dimensional invasion of macrophages. J. Cell Sci. 126, 2820-2833.
    • (2013) J. Cell Sci , vol.126 , pp. 2820-2833
    • Wiesner, C.1    El Azzouzi, K.2    Linder, S.3
  • 69
    • 0024324937 scopus 로고
    • Immunocytochemical distribution of extracellular matrix receptors in human osteoclasts: a beta 3 integrin is colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells
    • Zambonin-Zallone, A., Teti, A., Grano, M., Rubinacci, A., Abbadini, M., Gaboli, M. and Marchisio, P. C. (1989). Immunocytochemical distribution of extracellular matrix receptors in human osteoclasts: a beta 3 integrin is colocalized with vinculin and talin in the podosomes of osteoclastoma giant cells. Exp. Cell Res. 182, 645-652.
    • (1989) Exp. Cell Res , vol.182 , pp. 645-652
    • Zambonin-Zallone, A.1    Teti, A.2    Grano, M.3    Rubinacci, A.4    Abbadini, M.5    Gaboli, M.6    Marchisio, P.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.