메뉴 건너뛰기




Volumn 6, Issue , 2015, Pages

A resilient formin-derived cortical actin meshwork in the rear drives actomyosin-based motility in 2D confinement

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FORMIN A; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; MYOSIN ADENOSINE TRIPHOSPHATASE; PHOSPHATIDYLINOSITIDE; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG; ACTIN BINDING PROTEIN; CTXA PROTEIN, DICTYOSTELIUM DISCOIDEUM; CTXB PROTEIN, DICTYOSTELIUM DISCOIDEUM; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; MYOSIN II; PHOSPHATIDYLINOSITOL;

EID: 84942771786     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9496     Document Type: Article
Times cited : (31)

References (66)
  • 1
    • 75749146306 scopus 로고    scopus 로고
    • Plasticity of cell migration: A multiscale tuning model
    • Friedl, P. & Wolf, K. Plasticity of cell migration: a multiscale tuning model. J. Cell Biol. 188, 11-19 (2010).
    • (2010) J. Cell Biol , vol.188 , pp. 11-19
    • Friedl, P.1    Wolf, K.2
  • 3
    • 84869471944 scopus 로고    scopus 로고
    • Common mechanisms regulating cell cortex properties during cell division and cell migration
    • Roubinet, C., Tran, P. T. & Piel, M. Common mechanisms regulating cell cortex properties during cell division and cell migration. Cytoskeleton 69, 957-972 (2012).
    • (2012) Cytoskeleton , vol.69 , pp. 957-972
    • Roubinet, C.1    Tran, P.T.2    Piel, M.3
  • 4
    • 84903751503 scopus 로고    scopus 로고
    • Directed migration of mesenchymal cells: Where signaling and the cytoskeleton meet
    • Bear, J. E. & Haugh, J. M. Directed migration of mesenchymal cells: where signaling and the cytoskeleton meet. Curr. Opin. Cell Biol. 30, 74-82 (2014).
    • (2014) Curr. Opin. Cell Biol , vol.30 , pp. 74-82
    • Bear, J.E.1    Haugh, J.M.2
  • 5
    • 70349314647 scopus 로고    scopus 로고
    • Mechanical modes of 'amoeboid' cell migration
    • Lammermann, T. & Sixt, M. Mechanical modes of 'amoeboid' cell migration. Curr. Opin. Cell Biol. 21, 636-644 (2009).
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 636-644
    • Lammermann, T.1    Sixt, M.2
  • 7
    • 77954240254 scopus 로고    scopus 로고
    • Forming the cell rear first: Breaking cell symmetry to trigger directed cell migration
    • Cramer, L. P. Forming the cell rear first: breaking cell symmetry to trigger directed cell migration. Nat. Cell Biol. 12, 628-632 (2010).
    • (2010) Nat. Cell Biol , vol.12 , pp. 628-632
    • Cramer, L.P.1
  • 8
    • 34748878938 scopus 로고    scopus 로고
    • Actin-myosin network reorganization breaks symmetry at the cell rear to spontaneously initiate polarized cell motility
    • Yam, P. T. et al. Actin-myosin network reorganization breaks symmetry at the cell rear to spontaneously initiate polarized cell motility. J. Cell Biol. 178, 1207-1221 (2007).
    • (2007) J. Cell Biol , vol.178 , pp. 1207-1221
    • Yam, P.T.1
  • 9
    • 0032901710 scopus 로고    scopus 로고
    • Self-polarization and directional motility of cytoplasm
    • Verkhovsky, A. B., Svitkina, T. M. & Borisy, G. G. Self-polarization and directional motility of cytoplasm. Curr. Biol. 9, 11-20 (1999).
    • (1999) Curr. Biol , vol.9 , pp. 11-20
    • Verkhovsky, A.B.1    Svitkina, T.M.2    Borisy, G.G.3
  • 10
    • 77952911072 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis: A network of signaling pathways controls motility, directional sensing, and polarity
    • Swaney, K. F., Huang, C. H. & Devreotes, P. N. Eukaryotic chemotaxis: a network of signaling pathways controls motility, directional sensing, and polarity. Annu. Rev. Biophys. 39, 265-289 (2010).
    • (2010) Annu. Rev. Biophys , vol.39 , pp. 265-289
    • Swaney, K.F.1    Huang, C.H.2    Devreotes, P.N.3
  • 11
    • 84866882608 scopus 로고    scopus 로고
    • Actin cortex mechanics and cellular morphogenesis
    • Salbreux, G., Charras, G. & Paluch, E. Actin cortex mechanics and cellular morphogenesis. Trends Cell Biol. 22, 536-545 (2012).
    • (2012) Trends Cell Biol , vol.22 , pp. 536-545
    • Salbreux, G.1    Charras, G.2    Paluch, E.3
  • 12
    • 0033894411 scopus 로고    scopus 로고
    • A micromechanic study of cell polarity and plasma membrane cell body coupling in Dictyostelium
    • Merkel, R. et al. A micromechanic study of cell polarity and plasma membrane cell body coupling in Dictyostelium. Biophys. J. 79, 707-719 (2000).
    • (2000) Biophys. J , vol.79 , pp. 707-719
    • Merkel, R.1
  • 13
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares, M. et al. Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J. Cell Biol. 193, 381-396 (2011).
    • (2011) J. Cell Biol , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1
  • 14
    • 0025720725 scopus 로고
    • Microfilament structure and function in the cortical cytoskeleton
    • Bretscher, A. Microfilament structure and function in the cortical cytoskeleton. Ann. Rev. Cell Biol 7, 337-374 (1991).
    • (1991) Ann. Rev. Cell Biol , vol.7 , pp. 337-374
    • Bretscher, A.1
  • 15
    • 78651388574 scopus 로고    scopus 로고
    • Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding
    • Stewart, M. P. et al. Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding. Nature 469, 226-230 (2011).
    • (2011) Nature , vol.469 , pp. 226-230
    • Stewart, M.P.1
  • 16
    • 84899631548 scopus 로고    scopus 로고
    • Actomyosin networks and tissue morphogenesis
    • Munjal, A. & Lecuit, T. Actomyosin networks and tissue morphogenesis. Development 141, 1789-1793 (2014).
    • (2014) Development , vol.141 , pp. 1789-1793
    • Munjal, A.1    Lecuit, T.2
  • 17
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard, T. D. Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451-477 (2007).
    • (2007) Annu. Rev. Biophys. Biomol. Struct , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 18
    • 84859420307 scopus 로고    scopus 로고
    • Actin branching in the initiation and maintenance of lamellipodia
    • Vinzenz, M. et al. Actin branching in the initiation and maintenance of lamellipodia. J Cell Sci. 125, 2775-2785 (2012).
    • (2012) J Cell Sci , vol.125 , pp. 2775-2785
    • Vinzenz, M.1
  • 19
    • 33947666586 scopus 로고    scopus 로고
    • Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex
    • Eisenmann, K. M. et al. Dia-interacting protein modulates formin-mediated actin assembly at the cell cortex. Curr. Biol. 17, 579-591 (2007).
    • (2007) Curr. Biol , vol.17 , pp. 579-591
    • Eisenmann, K.M.1
  • 20
    • 55549131537 scopus 로고    scopus 로고
    • The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing
    • Hannemann, S. et al. The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. J. Biol. Chem. 283, 27891-27903 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 27891-27903
    • Hannemann, S.1
  • 21
    • 77951587879 scopus 로고    scopus 로고
    • Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC
    • Kitzing, T. M., Wang, Y., Pertz, O., Copeland, J. W. & Grosse, R. Formin-like 2 drives amoeboid invasive cell motility downstream of RhoC. Oncogene 29, 2441-2448 (2010).
    • (2010) Oncogene , vol.29 , pp. 2441-2448
    • Kitzing, T.M.1    Wang, Y.2    Pertz, O.3    Copeland, J.W.4    Grosse, R.5
  • 22
    • 84859420488 scopus 로고    scopus 로고
    • Differing and isoform-specific roles for the formin DIAPH3 in plasma membrane blebbing and filopodia formation
    • Stastna, J. et al. Differing and isoform-specific roles for the formin DIAPH3 in plasma membrane blebbing and filopodia formation. Cell Res. 22, 728-745 (2012).
    • (2012) Cell Res , vol.22 , pp. 728-745
    • Stastna, J.1
  • 23
    • 84904968718 scopus 로고    scopus 로고
    • Cellular control of cortical actin nucleation
    • Bovellan, M. et al. Cellular control of cortical actin nucleation. Curr. Biol. 24, 1628-1635 (2014).
    • (2014) Curr. Biol , vol.24 , pp. 1628-1635
    • Bovellan, M.1
  • 24
    • 0023924075 scopus 로고
    • Cell motility and chemotaxis in Dictyostelium amoebae lacking myosin heavy chain
    • Wessels, D. et al. Cell motility and chemotaxis in Dictyostelium amoebae lacking myosin heavy chain. Dev. Biol. 128, 164-177 (1988).
    • (1988) Dev. Biol , vol.128 , pp. 164-177
    • Wessels, D.1
  • 26
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP-And ADP-Actin by formins and profilin
    • Kovar, D. R., Harris, E. S., Mahaffy, R., Higgs, H. N. & Pollard, T. D. Control of the assembly of ATP-And ADP-Actin by formins and profilin. Cell 124, 423-435 (2006).
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 27
    • 0033932762 scopus 로고    scopus 로고
    • Rac1 GTPases control filopodia formation, cell motility, endocytosis, cytokinesis and development in Dictyostelium
    • Dumontier, M., Hocht, P., Mintert, U. & Faix, J. Rac1 GTPases control filopodia formation, cell motility, endocytosis, cytokinesis and development in Dictyostelium. J. Cell Sci. 113, 2253-2265 (2000).
    • (2000) J. Cell Sci , vol.113 , pp. 2253-2265
    • Dumontier, M.1    Hocht, P.2    Mintert, U.3    Faix, J.4
  • 28
    • 16044367114 scopus 로고    scopus 로고
    • Cortexillins, major determinants of cell shape and size, are actinbundling proteins with a parallel coiled-coil tail
    • Faix, J. et al. Cortexillins, major determinants of cell shape and size, are actinbundling proteins with a parallel coiled-coil tail. Cell 86, 631-642 (1996).
    • (1996) Cell , vol.86 , pp. 631-642
    • Faix, J.1
  • 29
    • 0033081026 scopus 로고    scopus 로고
    • Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow
    • Weber, I. et al. Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow. EMBO J. 18, 586-594 (1999).
    • (1999) EMBO J , vol.18 , pp. 586-594
    • Weber, I.1
  • 30
    • 0035898686 scopus 로고    scopus 로고
    • Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins
    • Faix, J. et al. Recruitment of cortexillin into the cleavage furrow is controlled by Rac1 and IQGAP-related proteins. EMBO J. 20, 3705-3715 (2001).
    • (2001) EMBO J , vol.20 , pp. 3705-3715
    • Faix, J.1
  • 31
    • 78649752769 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton by an interaction of IQGAP related protein GAPA with filamin and cortexillin i
    • Mondal, S. et al. Regulation of the actin cytoskeleton by an interaction of IQGAP related protein GAPA with filamin and cortexillin I. PLoS ONE 5, e15440 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e15440
    • Mondal, S.1
  • 32
    • 0031982879 scopus 로고    scopus 로고
    • Membrane bending modulus and adhesion energy of wild-type and mutant cells of Dictyostelium lacking talin or cortexillins
    • Simson, R. et al. Membrane bending modulus and adhesion energy of wild-type and mutant cells of Dictyostelium lacking talin or cortexillins. Biophys. J. 74, 514-522 (1998).
    • (1998) Biophys. J , vol.74 , pp. 514-522
    • Simson, R.1
  • 33
    • 84859709754 scopus 로고    scopus 로고
    • A mechanosensory system governs myosin II accumulation in dividing cells
    • Kee, Y. S. et al. A mechanosensory system governs myosin II accumulation in dividing cells. Mol. Biol. Cell 23, 1510-1523 (2012).
    • (2012) Mol. Biol. Cell , vol.23 , pp. 1510-1523
    • Kee, Y.S.1
  • 34
    • 84895542705 scopus 로고    scopus 로고
    • Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers
    • Burke, T. A. et al. Homeostatic actin cytoskeleton networks are regulated by assembly factor competition for monomers. Curr. Biol. 24, 579-585 (2014).
    • (2014) Curr. Biol , vol.24 , pp. 579-585
    • Burke, T.A.1
  • 35
    • 0031408781 scopus 로고    scopus 로고
    • Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells
    • Neujahr, R. et al. Three-dimensional patterns and redistribution of myosin II and actin in mitotic Dictyostelium cells. J. Cell Biol. 139, 1793-1804 (1997).
    • (1997) J. Cell Biol , vol.139 , pp. 1793-1804
    • Neujahr, R.1
  • 36
    • 50149095564 scopus 로고    scopus 로고
    • Blebs lead the way: How to migrate without lamellipodia
    • Charras, G. & Paluch, E. Blebs lead the way: how to migrate without lamellipodia. Nat. Rev. Mol. Cell Biol. 9, 730-736 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 730-736
    • Charras, G.1    Paluch, E.2
  • 37
    • 0032568662 scopus 로고    scopus 로고
    • C2-domains, structure and function of a universal Ca2+-binding domain
    • Rizo, J. & Sudhof, T. C. C2-domains, structure and function of a universal Ca2+-binding domain. J. Biol. Chem. 273, 15879-15882 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 15879-15882
    • Rizo, J.1    Sudhof, T.C.2
  • 38
    • 0033215305 scopus 로고    scopus 로고
    • Domain analysis of cortexillin I: Actin-bundling PIP2-binding and the rescue of cytokinesis
    • Stock, A. et al. Domain analysis of cortexillin I: actin-bundling, PIP2-binding and the rescue of cytokinesis. EMBO J. 18, 5274-5384 (1999).
    • (1999) EMBO J , vol.18 , pp. 5274-5384
    • Stock, A.1
  • 39
    • 84858148138 scopus 로고    scopus 로고
    • A dual role for Rac1 GTPases in the regulation of cell motility
    • Filic, V., Marinovic, M., Faix, J. & Weber, I. A dual role for Rac1 GTPases in the regulation of cell motility. J. Cell Sci. 125, 387-398 (2012).
    • (2012) J. Cell Sci , vol.125 , pp. 387-398
    • Filic, V.1    Marinovic, M.2    Faix, J.3    Weber, I.4
  • 40
    • 84885454469 scopus 로고    scopus 로고
    • Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation
    • Steffen, A. et al. Rac function is crucial for cell migration but is not required for spreading and focal adhesion formation. J. Cell Sci. 126, 4572-4588 (2013).
    • (2013) J. Cell Sci , vol.126 , pp. 4572-4588
    • Steffen, A.1
  • 41
    • 77952925797 scopus 로고    scopus 로고
    • Involvement of the cytoskeleton in controlling leading-edge function during chemotaxis
    • Lee, S., Shen, Z., Robinson, D. N., Briggs, S. & Firtel, R. A. Involvement of the cytoskeleton in controlling leading-edge function during chemotaxis. Mol. Biol. Cell 21, 1810-1824 (2010).
    • (2011) Mol. Biol. Cell , vol.21 , pp. 1810-1824
    • Lee, S.1    Shen, Z.2    Robinson, D.N.3    Briggs, S.4    Firtel, R.A.5
  • 42
    • 0031768407 scopus 로고    scopus 로고
    • The IQGAP-related protein DGAP1 interacts with Rac and is involved in the modulation of the F-Actin cytoskeleton and control of cell motility
    • Faix, J. et al. The IQGAP-related protein DGAP1 interacts with Rac and is involved in the modulation of the F-Actin cytoskeleton and control of cell motility. J. Cell Sci. 111, 3059-3071 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 3059-3071
    • Faix, J.1
  • 43
    • 0030929148 scopus 로고    scopus 로고
    • IQGAP1, a Rac-And Cdc42-binding protein, directly binds and cross-links microfilaments
    • Bashour, A. M., Fullerton, A. T., Hart, M. J. & Bloom, G. S. IQGAP1, a Rac-And Cdc42-binding protein, directly binds and cross-links microfilaments. J. Cell Biol. 137, 1555-1566 (1997).
    • (1997) J. Cell Biol , vol.137 , pp. 1555-1566
    • Bashour, A.M.1    Fullerton, A.T.2    Hart, M.J.3    Bloom, G.S.4
  • 44
    • 84885177444 scopus 로고    scopus 로고
    • IQGAP1 is a novel phosphatidylinositol 4,5 bisphosphate effector in regulation of directional cell migration
    • Choi, S. et al. IQGAP1 is a novel phosphatidylinositol 4,5 bisphosphate effector in regulation of directional cell migration. EMBO J. 32, 2617-2630 (2013).
    • (2013) EMBO J , vol.32 , pp. 2617-2630
    • Choi, S.1
  • 46
    • 27144552768 scopus 로고    scopus 로고
    • Self-Association of IQGAP1: Characterization and functional sequelae
    • Ren, J. G., Li, Z., Crimmins, D. L. & Sacks, D. B. Self-Association of IQGAP1: characterization and functional sequelae. J. Biol. Chem. 280, 34548-34557 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 34548-34557
    • Ren, J.G.1    Li, Z.2    Crimmins, D.L.3    Sacks, D.B.4
  • 47
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe, N., Kato, T., Fujita, A., Ishizaki, T. & Narumiya, S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1, 136-143 (1999).
    • (1999) Nat. Cell Biol , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 49
    • 79952150245 scopus 로고    scopus 로고
    • Contractility of the cell rear drives invasion of breast tumor cells in 3D Matrigel
    • Poincloux, R. et al. Contractility of the cell rear drives invasion of breast tumor cells in 3D Matrigel. Proc. Natl Acad. Sci. USA 108, 1943-1948 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 1943-1948
    • Poincloux, R.1
  • 50
    • 33750320965 scopus 로고    scopus 로고
    • Dissection of amoeboid movement into two mechanically distinct modes
    • Yoshida, K. & Soldati, T. Dissection of amoeboid movement into two mechanically distinct modes. J Cell Sci. 119, 3833-3844 (2006).
    • (2006) J Cell Sci , vol.119 , pp. 3833-3844
    • Yoshida, K.1    Soldati, T.2
  • 51
    • 84904278338 scopus 로고    scopus 로고
    • The IQGAP-related protein DGAP1 mediates signaling to the actin cytoskeleton as an effector and a sequestrator of Rac1 GTPases
    • Filic, V., Marinovic, M., Faix, J. & Weber, I. The IQGAP-related protein DGAP1 mediates signaling to the actin cytoskeleton as an effector and a sequestrator of Rac1 GTPases. Cell. Mol. Life Sci. 71, 2775-2785 (2014).
    • (2014) Cell. Mol. Life Sci , vol.71 , pp. 2775-2785
    • Filic, V.1    Marinovic, M.2    Faix, J.3    Weber, I.4
  • 52
    • 84939937425 scopus 로고    scopus 로고
    • Actin flows mediate a universal coupling between cell speed and cell persistence
    • Maiuri, P. et al. Actin flows mediate a universal coupling between cell speed and cell persistence. Cell 161, 374-386 (2015).
    • (2015) Cell , vol.161 , pp. 374-386
    • Maiuri, P.1
  • 53
    • 84882844733 scopus 로고    scopus 로고
    • Ezrin/radixin/moesin proteins and flotillins cooperate to promote uropod formation in T cells
    • Martinelli, S. et al. Ezrin/radixin/moesin proteins and flotillins cooperate to promote uropod formation in T cells. Front. Immunol. 8, 84 (2013).
    • (2013) Front. Immunol , vol.8 , pp. 84
    • Martinelli, S.1
  • 54
    • 0031670169 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium
    • Fukui, Y., Kitanishi-Yumura, T. & Yumura, S. Spatiotemporal dynamics of actin concentration during cytokinesis and locomotion in Dictyostelium. J. Cell Sci. 111, 2097-2108 (1998).
    • (1998) J. Cell Sci , vol.111 , pp. 2097-2108
    • Fukui, Y.1    Kitanishi-Yumura, T.2    Yumura, S.3
  • 55
    • 34548258389 scopus 로고    scopus 로고
    • PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis
    • Wessels, D., Lusche, D. F., Kuhl, S., Heid, P. & Soll, D. R. PTEN plays a role in the suppression of lateral pseudopod formation during Dictyostelium motility and chemotaxis. J. Cell Sci. 120, 2517-2531 (2007).
    • (2007) J. Cell Sci , vol.120 , pp. 2517-2531
    • Wessels, D.1    Lusche, D.F.2    Kuhl, S.3    Heid, P.4    Soll, D.R.5
  • 56
    • 77955927654 scopus 로고    scopus 로고
    • Phospholipids regulate localization and activity of mDia1 formin
    • Ramalingam, N. et al. Phospholipids regulate localization and activity of mDia1 formin. Eur. J. Cell Biol. 89, 723-732 (2010).
    • (2010) Eur. J. Cell Biol , vol.89 , pp. 723-732
    • Ramalingam, N.1
  • 57
    • 33748123994 scopus 로고    scopus 로고
    • Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1
    • Seth, A., Otomo, C. & Rosen, M. K. Autoinhibition regulates cellular localization and actin assembly activity of the diaphanous-related formins FRLalpha and mDia1. J. Cell Biol. 174, 701-713 (2006).
    • (2006) J. Cell Biol , vol.174 , pp. 701-713
    • Seth, A.1    Otomo, C.2    Rosen, M.K.3
  • 58
    • 84884731000 scopus 로고    scopus 로고
    • Wnt5a directs polarized calcium gradients by recruiting cortical endoplasmic reticulum to the cell trailing edge
    • Witze, E. S. et al. Wnt5a directs polarized calcium gradients by recruiting cortical endoplasmic reticulum to the cell trailing edge. Dev. Cell 26, 645-657 (2013).
    • (2013) Dev. Cell , vol.26 , pp. 645-657
    • Witze, E.S.1
  • 59
    • 84892490270 scopus 로고    scopus 로고
    • ERM proteins in cancer progression
    • Clucas, J. & Valderrama, F. ERM proteins in cancer progression. J. Cell Sci. 127, 267-275 (2014).
    • (2014) J. Cell Sci , vol.127 , pp. 267-275
    • Clucas, J.1    Valderrama, F.2
  • 60
    • 84904437909 scopus 로고    scopus 로고
    • G-protein-coupled receptor signaling and polarized actin dynamics drive cell-in-cell invasion
    • Purvanov, V., Holst, M., Khan, J., Baarlink, C. & Grosse, R. G-protein-coupled receptor signaling and polarized actin dynamics drive cell-in-cell invasion. Elife 20, 3 (2014).
    • (2014) Elife , vol.20 , pp. 3
    • Purvanov, V.1    Holst, M.2    Khan, J.3    Baarlink, C.4    Grosse, R.5
  • 61
    • 65449139489 scopus 로고    scopus 로고
    • The mDial formin is required for neutrophil polarization, migration, and activation of the LARG/RhoA/ROCK signaling axis during chemotaxis
    • Shi, Y. et al. The mDial formin is required for neutrophil polarization, migration, and activation of the LARG/RhoA/ROCK signaling axis during chemotaxis. J. Immunol. 182, 3837-3845 (2009).
    • (2009) J. Immunol , vol.182 , pp. 3837-3845
    • Shi, Y.1
  • 62
    • 19644390035 scopus 로고    scopus 로고
    • A rapid and efficient method to generate multiple gene disruptions in Dictyostelium discoideum using a single selectable marker and the Cre-loxP system
    • Faix, J., Kreppel, L., Shaulsky, G., Schleicher, M. & Kimmel, A. R. A rapid and efficient method to generate multiple gene disruptions in Dictyostelium discoideum using a single selectable marker and the Cre-loxP system. Nucleic Acids Res. 32, e143 (2004).
    • (2004) Nucleic Acids Res , vol.32 , pp. e143
    • Faix, J.1    Kreppel, L.2    Shaulsky, G.3    Schleicher, M.4    Kimmel, A.R.5
  • 64
    • 0023002546 scopus 로고
    • Monoclonal antibodies binding to the tail of Dictyostelium discoideum myosin: Their effects on antiparallel and parallel assembly and actin-Activated ATPase activity
    • Pagh, K. & Gerisch, G. Monoclonal antibodies binding to the tail of Dictyostelium discoideum myosin: their effects on antiparallel and parallel assembly and actin-Activated ATPase activity. J. Cell Biol. 103, 1527-1538 (1986).
    • (1986) J. Cell Biol , vol.103 , pp. 1527-1538
    • Pagh, K.1    Gerisch, G.2
  • 65
    • 0026722990 scopus 로고
    • Purification, functional characterization, and cDNA sequencing of mitochondrial porin from Dictyostelium discoideum
    • Troll, H. et al. Purification, functional characterization, and cDNA sequencing of mitochondrial porin from Dictyostelium discoideum. J. Biol. Chem. 267, 21072-21079 (1992).
    • (1992) J. Biol. Chem , vol.267 , pp. 21072-21079
    • Troll, H.1
  • 66
    • 61449230736 scopus 로고    scopus 로고
    • Analysis of cell movement by simultaneous quantification of local membrane displacement and fluorescent intensities using Quimp2
    • Bosgraaf, L., van Haastert, P. J. & Bretschneider, T. Analysis of cell movement by simultaneous quantification of local membrane displacement and fluorescent intensities using Quimp2. Cell Motil. Cytoskeleton. 66, 156-165 (2009).
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 156-165
    • Bosgraaf, L.1    Van Haastert, P.J.2    Bretschneider, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.