메뉴 건너뛰기




Volumn 7, Issue 6, 2005, Pages 619-625

The Diaphanous-related formin dDia2 is required for the formation and maintenance of filopodia

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CELL PROTEIN; PROFILIN; RAC PROTEIN;

EID: 20444426470     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1266     Document Type: Article
Times cited : (211)

References (35)
  • 1
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • Evangelista, M., Zigmond, S. & Boone, C. Formins: signaling effectors for assembly and polarization of actin filaments. J. Cell Sci. 116, 2603-2611 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 2
    • 0041758426 scopus 로고    scopus 로고
    • The formins: Active scaffolds that remodel the cytoskeleton
    • Wallar, B. J. & Alberts, A. S. The formins: active scaffolds that remodel the cytoskeleton. Trends Cell Biol. 13, 435-446 (2003).
    • (2003) Trends Cell Biol. , vol.13 , pp. 435-446
    • Wallar, B.J.1    Alberts, A.S.2
  • 3
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • Zigmond, S. H. Formin-induced nucleation of actin filaments. Curr. Opin. Cell Biol. 16, 99-105 (2004).
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1
  • 4
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation
    • Petersen, J., Nielsen, O., Egel, R. & Hagan, I. M. FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J. Cell Biol. 141, 1217-1228 (1998).
    • (1998) J. Cell Biol. , vol.141 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 5
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts, A. S. Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 6
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • Shimada, A. et al. The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Mol. Cell 13, 511-522 (2004).
    • (2004) Mol. Cell. , vol.13 , pp. 511-522
    • Shimada, A.1
  • 7
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • Xu, Y. et al. Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723 (2004).
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1
  • 8
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, et al. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122 (1997).
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista1
  • 9
    • 0030911424 scopus 로고    scopus 로고
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N. et al. p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 10
    • 0029981652 scopus 로고    scopus 로고
    • Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains
    • Chan, D. C., Bedford, M. T. & Leder, P. Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1045-1054
    • Chan, D.C.1    Bedford, M.T.2    Leder, P.3
  • 12
    • 0037780973 scopus 로고    scopus 로고
    • The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin
    • Kovar, D. R., Kuhn, J. R., Tichy, A. L. & Pollard, T. D. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161, 875-887 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 875-887
    • Kovar, D.R.1    Kuhn, J.R.2    Tichy, A.L.3    Pollard, T.D.4
  • 13
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., Pruyne, D., Amberg, D. C., Boone, C. & Bretscher, A. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nature Cell Biol. 4, 32-41 (2002).
    • (2002) Nature Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 14
    • 0037382160 scopus 로고    scopus 로고
    • Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42
    • Peng, J., Wallar, B. J., Flanders, A., Swiatek, P. J. & Alberts, A. S. Disruption of the Diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr. Biol. 13, 534-545 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 534-545
    • Peng, J.1    Wallar, B.J.2    Flanders, A.3    Swiatek, P.J.4    Alberts, A.S.5
  • 15
    • 12544253725 scopus 로고    scopus 로고
    • The Rho family GTPase Rif induces filopodia through mDia2
    • Pellegrin, S. & Mellor, H. The Rho family GTPase Rif induces filopodia through mDia2. Curr. Biol. 15, 129-133 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 129-133
    • Pellegrin, S.1    Mellor, H.2
  • 16
    • 0032786906 scopus 로고    scopus 로고
    • Membrane tether formation from blebbing cells
    • Dai, J. & Sheetz, M. P. Membrane tether formation from blebbing cells. Biophys. J. 77, 3363-3370 (1999).
    • (1999) Biophys. J. , vol.77 , pp. 3363-3370
    • Dai, J.1    Sheetz, M.P.2
  • 17
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero, S. et al. Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429 (2004).
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1
  • 18
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar, D. R. & Pollard, T. D. Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl Acad. Sci. USA 101, 14725-14730 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 19
    • 18344395923 scopus 로고    scopus 로고
    • The genome of the social amoeba Dictyostelium discoideum
    • Eichinger, L. et al. The genome of the social amoeba Dictyostelium discoideum. Nature 435, 43-57 (2005).
    • (2005) Nature , vol.435 , pp. 43-57
    • Eichinger, L.1
  • 20
    • 0037442388 scopus 로고    scopus 로고
    • ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum
    • Kitayama, C. & Uyeda, T. Q. ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium discoideum. J. Cell Sci. 116, 711-723 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 711-723
    • Kitayama, C.1    Uyeda, T.Q.2
  • 21
    • 0028004565 scopus 로고
    • Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz, M., Noegel, A. A., Karakesisoglou, J. & Schleicher, M. Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79, 303-314 (1994).
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 22
    • 0035282887 scopus 로고    scopus 로고
    • The Dictyostelium discoideum family of Rho-related proteins
    • Rivero, F., Dislich, H., Glöckner, G. & Noegel, A. A. The Dictyostelium discoideum family of Rho-related proteins. Nucleic Acids Res. 29, 1068-1079 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1068-1079
    • Rivero, F.1    Dislich, H.2    Glöckner, G.3    Noegel, A.A.4
  • 23
    • 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
  • 24
    • 0033932762 scopus 로고    scopus 로고
    • Rac1 GTPases control filopodia formation, cell motility, endocytosis, cytokinesis and development in Dictyostelium
    • Dumontier, M., Höcht, 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    Höcht, P.2    Mintert, U.3    Faix, J.4
  • 26
    • 0037147305 scopus 로고    scopus 로고
    • Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in Dictyostelium
    • Han, Y. H. et al. Requirement of a vasodilator-stimulated phosphoprotein family member for cell adhesion, the formation of filopodia, and chemotaxis in Dictyostelium. J. Biol. Chem. 277, 49877-49887 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 49877-49887
    • Han, Y.H.1
  • 27
    • 0037415574 scopus 로고    scopus 로고
    • Mechanism of filopodia initiation by reorganization of a dendritic network
    • Svitkina, T. M. et al. Mechanism of filopodia initiation by reorganization of a dendritic network. J. Cell Biol. 160, 409-421 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 409-421
    • Svitkina, T.M.1
  • 28
    • 1842453175 scopus 로고    scopus 로고
    • Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of Netrin-1
    • Lebrand, C. et al. Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of Netrin-1. Neuron 42, 37-49 (2004).
    • (2004) Neuron , vol.42 , pp. 37-49
    • Lebrand, C.1
  • 29
    • 0029065328 scopus 로고
    • Capping protein levels influence actin assembly and cell motility in Dictyostelium
    • Hug, C. et al. Capping protein levels influence actin assembly and cell motility in Dictyostelium. Cell 81, 591-600 (1995).
    • (1995) Cell , vol.81 , pp. 591-600
    • Hug, C.1
  • 30
    • 0031768407 scopus 로고    scopus 로고
    • The IQGAP-related protein DGAPI 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 DGAPI 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
  • 31
    • 0027217068 scopus 로고
    • A transformation vector for Dictyostelium discoideum with a new selectable marker bsr
    • Sutoh, K. A transformation vector for Dictyostelium discoideum with a new selectable marker bsr. Plasmid 2, 150-154 (1993).
    • (1993) Plasmid , vol.2 , pp. 150-154
    • Sutoh, K.1
  • 33
    • 0030574044 scopus 로고    scopus 로고
    • DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum
    • Faix, J. & Dittrich, W. DGAP1, a homologue of rasGTPase activating proteins that controls growth, cytokinesis, and development in Dictyostelium discoideum. FEBS Lett. 394, 251-257 (1996).
    • (1996) FEBS Lett. , vol.394 , pp. 251-257
    • Faix, J.1    Dittrich, W.2
  • 34
    • 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
  • 35
    • 0026638337 scopus 로고
    • 2+-dependent F-actin fragmenting protein
    • 2+-dependent F-actin fragmenting protein. Biochemistry 31, 4779-4787 (1992).
    • (1992) Biochemistry , vol.31 , pp. 4779-4787
    • Eichinger, L.1    Schleicher, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.