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Volumn 13, Issue 8, 2003, Pages 435-446

The formins: Active scaffolds that remodel the cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; FORMIN PROTEIN; GUANOSINE TRIPHOSPHATASE; PROTEIN; RHO FACTOR; UNCLASSIFIED DRUG;

EID: 0041758426     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(03)00153-3     Document Type: Review
Times cited : (319)

References (119)
  • 1
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon D.H., Wasserman S.A. Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development. 120:1994;3367-3377.
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 2
    • 0032031388 scopus 로고    scopus 로고
    • FH proteins as cytoskeletal organizers
    • Wasserman S. FH proteins as cytoskeletal organizers. Trends Cell Biol. 8:1998;111-115.
    • (1998) Trends Cell Biol. , vol.8 , pp. 111-115
    • Wasserman, S.1
  • 3
    • 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., et al. FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J. Cell Biol. 141:1998;1217-1228.
    • (1998) J. Cell Biol. , vol.141 , pp. 1217-1228
    • Petersen, J.1
  • 4
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias M.J., et al. WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett. 513:2002;30-37.
    • (2002) FEBS Lett. , vol.513 , pp. 30-37
    • Macias, M.J.1
  • 5
    • 0037442388 scopus 로고    scopus 로고
    • ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium
    • Kitayama C., Uyeda T.Q. ForC, a novel type of formin family protein lacking an FH1 domain, is involved in multicellular development in Dictyostelium. J. Cell Sci. 116:2003;711-723.
    • (2003) J. Cell Sci. , vol.116 , pp. 711-723
    • Kitayama, C.1    Uyeda, T.Q.2
  • 6
    • 0036203534 scopus 로고    scopus 로고
    • Nir2, a novel regulator of cell morphogenesis
    • Tian D., et al. Nir2, a novel regulator of cell morphogenesis. Mol. Cell. Biol. 22:2002;2650-2662.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2650-2662
    • Tian, D.1
  • 7
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed end association
    • Pruyne D., et al. Role of formins in actin assembly: nucleation and barbed end association. Science. 297:2002;612-615.
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1
  • 8
    • 0036835889 scopus 로고    scopus 로고
    • Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization
    • Deeks M.J., et al. Formins: intermediates in signal-transduction cascades that affect cytoskeletal reorganization. Trends Plant Sci. 7:2002;492-498.
    • (2002) Trends Plant Sci. , vol.7 , pp. 492-498
    • Deeks, M.J.1
  • 9
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells
    • Kato T., et al. Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J. Cell Sci. 114:2001;775-784.
    • (2001) J. Cell Sci. , vol.114 , pp. 775-784
    • Kato, T.1
  • 10
    • 0033620658 scopus 로고    scopus 로고
    • Identification and characterization of a protein containing formin homology (FH1/FH2) domains
    • Westendorf J.J., et al. Identification and characterization of a protein containing formin homology (FH1/FH2) domains. Gene. 232:1999;173-182.
    • (1999) Gene , vol.232 , pp. 173-182
    • Westendorf, J.J.1
  • 11
    • 0030004228 scopus 로고    scopus 로고
    • Prediction and analysis of coiled-coil structures
    • Lupas A. Prediction and analysis of coiled-coil structures. Methods Enzymol. 266:1996;513-525.
    • (1996) Methods Enzymol. , vol.266 , pp. 513-525
    • Lupas, A.1
  • 12
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I., et al. Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4:2002;42-50.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1
  • 13
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N., et al. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1:1999;136-143.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1
  • 14
    • 0032784388 scopus 로고    scopus 로고
    • Distinct actions and cooperative roles of ROCK and mDia in Rho Small G protein-induced reorganization of the actin cytoskeleton in madin-darby canine kidney cells
    • Nakano K., et al. Distinct actions and cooperative roles of ROCK and mDia in Rho Small G protein-induced reorganization of the actin cytoskeleton in madin-darby canine kidney cells. Mol. Biol. Cell. 10:1999;2481-2491.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2481-2491
    • Nakano, K.1
  • 15
    • 0032537023 scopus 로고    scopus 로고
    • Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: Implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Umikawa M., et al. Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae. Oncogene. 16:1998;2011-2016.
    • (1998) Oncogene , vol.16 , pp. 2011-2016
    • Umikawa, M.1
  • 16
    • 0036175770 scopus 로고    scopus 로고
    • Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: Implications for anchoring mRNA in cell protrusions
    • Liu G., et al. Interactions of elongation factor 1alpha with F-actin and beta-actin mRNA: implications for anchoring mRNA in cell protrusions. Mol. Biol. Cell. 13:2002;579-592.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 579-592
    • Liu, G.1
  • 17
    • 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. 16:1997;3044-3056.
    • (1997) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 18
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7
    • Alberts A.S., et al. Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J. Biol. Chem. 273:1998;8616-8622.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1
  • 19
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista M., et al. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science. 276:1997;118-122.
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1
  • 20
    • 10544228528 scopus 로고    scopus 로고
    • Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae
    • Kohno H., et al. Bni1p implicated in cytoskeletal control is a putative target of Rho1p small GTP binding protein in Saccharomyces cerevisiae. EMBO J. 15:1996;6060-6068.
    • (1996) EMBO J. , vol.15 , pp. 6060-6068
    • Kohno, H.1
  • 21
    • 0033816998 scopus 로고    scopus 로고
    • FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages
    • Yayoshi-Yamamoto S., et al. FRL, a novel formin-related protein, binds to Rac and regulates cell motility and survival of macrophages. Mol. Cell. Biol. 20:2000;6872-6881.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6872-6881
    • Yayoshi-Yamamoto, S.1
  • 22
    • 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., et al. Disruption of the diaphanous-related formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr. Biol. 13:2003;534-545.
    • (2003) Curr. Biol. , vol.13 , pp. 534-545
    • Peng, J.1
  • 23
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo P.D., et al. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:1995;29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1
  • 24
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • Gasman S., et al. RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat. Cell Biol. 5:2003;195-204.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 195-204
    • Gasman, S.1
  • 25
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxy-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts A.S. Identification of a carboxy-terminal diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276:2001;2824-2830.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 26
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard T.D., Borisy G.G. Cellular motility driven by assembly and disassembly of actin filaments. Cell. 112:2003;453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 27
    • 0036049615 scopus 로고    scopus 로고
    • An actin nucleation mechanism mediated by Bni1 and Profilin
    • Sagot I., et al. An actin nucleation mechanism mediated by Bni1 and Profilin. Nat. Cell Biol. 4:2002;626-631.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 626-631
    • Sagot, I.1
  • 28
    • 0037458002 scopus 로고    scopus 로고
    • Mechanism of formin-induced nucleation of actin filaments
    • Pring M., et al. Mechanism of formin-induced nucleation of actin filaments. Biochemistry. 42:2003;486-496.
    • (2003) Biochemistry , vol.42 , pp. 486-496
    • Pring, M.1
  • 29
    • 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., et al. The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161:2003;875-887.
    • (2003) J. Cell Biol. , vol.161 , pp. 875-887
    • Kovar, D.R.1
  • 30
    • 0036273491 scopus 로고    scopus 로고
    • Evolutionary conservation of microtubule-capture mechanisms
    • Gundersen G.G. Evolutionary conservation of microtubule-capture mechanisms. Nat. Rev. Mol. Cell Biol. 3:2002;296-304.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 296-304
    • Gundersen, G.G.1
  • 31
    • 0037451174 scopus 로고    scopus 로고
    • Polarized growth and organelle segregation in yeast: The tracks, motors, and receptors
    • Bretscher A. Polarized growth and organelle segregation in yeast: the tracks, motors, and receptors. J. Cell Biol. 160:2003;811-816.
    • (2003) J. Cell Biol. , vol.160 , pp. 811-816
    • Bretscher, A.1
  • 32
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M., et al. Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4:2002;32-41.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1
  • 33
    • 0036854328 scopus 로고    scopus 로고
    • The Diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • Copeland J.W., Treisman R. The Diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol. Biol. Cell. 13:2002;4088-4099.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 34
    • 0012644537 scopus 로고    scopus 로고
    • Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling
    • Tominaga T., et al. Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling. Mol. Cell. 5:2000;13-25.
    • (2000) Mol. Cell , vol.5 , pp. 13-25
    • Tominaga, T.1
  • 35
    • 0035816691 scopus 로고    scopus 로고
    • Differential usage of signal transduction pathways defines two types of serum response factor target gene
    • Gineitis D., Treisman R. Differential usage of signal transduction pathways defines two types of serum response factor target gene. J. Biol. Chem. 276:2001;24531-24539.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24531-24539
    • Gineitis, D.1    Treisman, R.2
  • 36
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill C.S., et al. The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell. 81:1995;1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1
  • 37
    • 0033597825 scopus 로고    scopus 로고
    • Signal-regulated activation of serum response factor is mediated by changes in actin dynamics
    • Sotiropoulos A., et al. Signal-regulated activation of serum response factor is mediated by changes in actin dynamics. Cell. 98:1999;159-169.
    • (1999) Cell , vol.98 , pp. 159-169
    • Sotiropoulos, A.1
  • 38
    • 0036788748 scopus 로고    scopus 로고
    • Interaction of serum response factor (SRF) with the Elk-1 B box inhibits RhoA-actin signaling to SRF and potentiates transcriptional activation by Elk-1
    • Murai K., Treisman R. Interaction of serum response factor (SRF) with the Elk-1 B box inhibits RhoA-actin signaling to SRF and potentiates transcriptional activation by Elk-1. Mol. Cell. Biol. 22:2002;7083-7092.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 7083-7092
    • Murai, K.1    Treisman, R.2
  • 39
    • 0037182585 scopus 로고    scopus 로고
    • LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics
    • Geneste O., et al. LIM kinase and Diaphanous cooperate to regulate serum response factor and actin dynamics. J. Cell Biol. 157:2002;831-838.
    • (2002) J. Cell Biol. , vol.157 , pp. 831-838
    • Geneste, O.1
  • 40
    • 85031130314 scopus 로고    scopus 로고
    • Mutant actins demonstrate a role for unpolymerised actin in controld of transcription by Serum Response Factor
    • in press
    • Posern, G. et al. Mutant actins demonstrate a role for unpolymerised actin in controld of transcription by Serum Response Factor. Mol. Biol. Cell (in press).
    • Mol. Biol. Cell
    • Posern, G.1
  • 41
    • 0035967868 scopus 로고    scopus 로고
    • Activation of cardiac gene expression by myocardin, a transcriptional cofactor for serum response factor
    • Wang D., et al. Activation of cardiac gene expression by myocardin, a transcriptional cofactor for serum response factor. Cell. 105:2001;851-862.
    • (2001) Cell , vol.105 , pp. 851-862
    • Wang, D.1
  • 42
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles F., et al. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell. 113:2003;329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1
  • 43
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach B., Chang F. Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11:2001;1656-1665.
    • (2001) Curr. Biol. , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 44
    • 0030958087 scopus 로고    scopus 로고
    • Cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin
    • Chang F., et al. cdc12p, a protein required for cytokinesis in fission yeast, is a component of the cell division ring and interacts with profilin. J. Cell Biol. 137:1997;169-182.
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, F.1
  • 45
    • 0033615081 scopus 로고    scopus 로고
    • Movement of a cytokinesis factor cdc12p to the site of cell division
    • Chang F. Movement of a cytokinesis factor cdc12p to the site of cell division. Curr. Biol. 9:1999;849-852.
    • (1999) Curr. Biol. , vol.9 , pp. 849-852
    • Chang, F.1
  • 46
    • 0037195254 scopus 로고    scopus 로고
    • Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis
    • Tolliday N., et al. Rho1 directs formin-mediated actin ring assembly during budding yeast cytokinesis. Curr. Biol. 12:2002;1864-1870.
    • (2002) Curr. Biol. , vol.12 , pp. 1864-1870
    • Tolliday, N.1
  • 47
    • 0035137208 scopus 로고    scopus 로고
    • Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae
    • Ozaki-Kuroda K., et al. Dynamic localization and function of Bni1p at the sites of directed growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 21:2001;827-839.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 827-839
    • Ozaki-Kuroda, K.1
  • 48
    • 0033846845 scopus 로고    scopus 로고
    • Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p)
    • Jaquenoud M., Peter M. Gic2p may link activated Cdc42p to components involved in actin polarization, including Bni1p and Bud6p (Aip3p). Mol. Cell. Biol. 20:2000;6244-6258.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6244-6258
    • Jaquenoud, M.1    Peter, M.2
  • 50
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin H., et al. Myosin V orientates the mitotic spindle in yeast. Nature. 406:2000;1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1
  • 51
    • 0033506707 scopus 로고    scopus 로고
    • Bni1p regulates microtubule-dependent nuclear migration through the actin cytoskeleton in Saccharomyces cerevisiae
    • Fujiwara T., et al. Bni1p regulates microtubule-dependent nuclear migration through the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Cell. Biol. 19:1999;8016-8027.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8016-8027
    • Fujiwara, T.1
  • 52
    • 0033535351 scopus 로고    scopus 로고
    • Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p
    • Lee L., et al. Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p. J. Cell Biol. 144:1999;947-961.
    • (1999) J. Cell Biol. , vol.144 , pp. 947-961
    • Lee, L.1
  • 53
    • 0037459058 scopus 로고    scopus 로고
    • Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment
    • Liakopoulos D., et al. Asymmetric loading of Kar9 onto spindle poles and microtubules ensures proper spindle alignment. Cell. 112:2003;561-574.
    • (2003) Cell , vol.112 , pp. 561-574
    • Liakopoulos, D.1
  • 54
    • 0036904735 scopus 로고    scopus 로고
    • Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes
    • Leader B., et al. Formin-2, polyploidy, hypofertility and positioning of the meiotic spindle in mouse oocytes. Nat. Cell Biol. 4:2002;921-928.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 921-928
    • Leader, B.1
  • 55
    • 0030040263 scopus 로고    scopus 로고
    • Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring
    • Chang F., et al. Isolation and characterization of fission yeast mutants defective in the assembly and placement of the contractile actin ring. J. Cell Sci. 109:1996;131-142.
    • (1996) J. Cell Sci. , vol.109 , pp. 131-142
    • Chang, F.1
  • 56
    • 0034907213 scopus 로고    scopus 로고
    • MDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo A., et al. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3:2001;723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.1
  • 57
    • 0035141074 scopus 로고    scopus 로고
    • Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1
    • Ishizaki T., et al. Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nat. Cell Biol. 3:2001;8-14.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 8-14
    • Ishizaki, T.1
  • 58
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A., Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:2002;1587-1609.
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 59
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S., Hall A. Rho GTPases in cell biology. Nature. 420:2002;629-635.
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 60
    • 0032938745 scopus 로고    scopus 로고
    • Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70
    • Robinson N.G., et al. Rho3 of Saccharomyces cerevisiae, which regulates the actin cytoskeleton and exocytosis, is a GTPase which interacts with Myo2 and Exo70. Mol. Cell. Biol. 19:1999;3580-3587.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 3580-3587
    • Robinson, N.G.1
  • 61
    • 0030927327 scopus 로고    scopus 로고
    • Bni1p and Bnr1p: Downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae
    • Imamura H., et al. Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. EMBO J. 16:1997;2745-2755.
    • (1997) EMBO J. , vol.16 , pp. 2745-2755
    • Imamura, H.1
  • 62
    • 0037695052 scopus 로고    scopus 로고
    • GTPase signalling: New functions for diaphanous-related formins
    • Olson M.F. GTPase signalling: new functions for diaphanous-related formins. Curr. Biol. 13:2003;R360-R362.
    • (2003) Curr. Biol. , vol.13
    • Olson, M.F.1
  • 63
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 64
    • 0035824618 scopus 로고    scopus 로고
    • The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element
    • Westendorf J.J. The formin/diaphanous-related protein, FHOS, interacts with Rac1 and activates transcription from the serum response element. J. Biol. Chem. 276:2001;46453-46459.
    • (2001) J. Biol. Chem. , vol.276 , pp. 46453-46459
    • Westendorf, J.J.1
  • 65
    • 0038392871 scopus 로고    scopus 로고
    • Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP
    • Torres E., Rosen M.K. Contingent phosphorylation/dephosphorylation provides a mechanism of molecular memory in WASP. Mol. Cell. 11:2003;1215-1227.
    • (2003) Mol. Cell , vol.11 , pp. 1215-1227
    • Torres, E.1    Rosen, M.K.2
  • 66
    • 0038392873 scopus 로고    scopus 로고
    • Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP
    • Cory G.O., et al. Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol. Cell. 11:2003;1229-1239.
    • (2003) Mol. Cell , vol.11 , pp. 1229-1239
    • Cory, G.O.1
  • 67
    • 0030707797 scopus 로고    scopus 로고
    • Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous
    • Lynch E.D., et al. Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science. 278:1997;1315-1318.
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1
  • 68
    • 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. 160:2003;409-421.
    • (2003) J. Cell Biol. , vol.160 , pp. 409-421
    • Svitkina, T.M.1
  • 69
    • 0025998618 scopus 로고
    • Actin dynamics in growth cones
    • Okabe S., Hirokawa N. Actin dynamics in growth cones. J. Neurosci. 11:1991;1918-1929.
    • (1991) J. Neurosci. , vol.11 , pp. 1918-1929
    • Okabe, S.1    Hirokawa, N.2
  • 70
    • 0035479910 scopus 로고    scopus 로고
    • Assembly and mechanosensory function of focal contacts
    • Geiger B., Bershadsky A. Assembly and mechanosensory function of focal contacts. Curr. Opin. Cell Biol. 13:2001;584-592.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 584-592
    • Geiger, B.1    Bershadsky, A.2
  • 71
    • 0033546275 scopus 로고    scopus 로고
    • The Cdc42p GTPase is involved in a G2/M morphogenetic checkpoint regulating the apical-isotropic switch and nuclear division in yeast
    • Richman T.J., et al. The Cdc42p GTPase is involved in a G2/M morphogenetic checkpoint regulating the apical-isotropic switch and nuclear division in yeast. J. Biol. Chem. 274:1999;16861-16870.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16861-16870
    • Richman, T.J.1
  • 72
    • 0036469912 scopus 로고    scopus 로고
    • Delphilin: A novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor delta 2 subunit
    • Miyagi Y., et al. Delphilin: a novel PDZ and formin homology domain-containing protein that synaptically colocalizes and interacts with glutamate receptor delta 2 subunit. J. Neurosci. 22:2002;803-814.
    • (2002) J. Neurosci. , vol.22 , pp. 803-814
    • Miyagi, Y.1
  • 73
    • 0036606515 scopus 로고    scopus 로고
    • Axon guidance: Receptor complexes and signaling mechanisms
    • Grunwald I.C., Klein R. Axon guidance: receptor complexes and signaling mechanisms. Curr. Opin. Neurobiol. 12:2002;250-259.
    • (2002) Curr. Opin. Neurobiol. , vol.12 , pp. 250-259
    • Grunwald, I.C.1    Klein, R.2
  • 74
    • 0036702196 scopus 로고    scopus 로고
    • Regulating the actin cytoskeleton during vesicular transport
    • Stamnes M. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14:2002;428-433.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 428-433
    • Stamnes, M.1
  • 75
    • 0030460431 scopus 로고    scopus 로고
    • Molecular interaction between limb deformity proteins (formins) and Src family kinases
    • Uetz P., et al. Molecular interaction between limb deformity proteins (formins) and Src family kinases. J. Biol. Chem. 271:1996;33525-33530.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33525-33530
    • Uetz, P.1
  • 76
    • 0032481313 scopus 로고    scopus 로고
    • In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly
    • Witke W., et al. In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly. EMBO J. 17:1998;967-976.
    • (1998) EMBO J. , vol.17 , pp. 967-976
    • Witke, W.1
  • 77
    • 0034685631 scopus 로고    scopus 로고
    • Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2
    • Fujiwara T., et al. Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2. Biochem. Biophys. Res. Commun. 271:2000;626-629.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 626-629
    • Fujiwara, T.1
  • 78
    • 0035914408 scopus 로고    scopus 로고
    • MDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation
    • Satoh S., Tominaga T. mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation. J. Biol. Chem. 276:2001;39290-39294.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39290-39294
    • Satoh, S.1    Tominaga, T.2
  • 79
    • 0031194074 scopus 로고    scopus 로고
    • Actin cytoskeleton: Are FH proteins local organizers?
    • Frazier J.A., Field C.M. Actin cytoskeleton: are FH proteins local organizers? Curr. Biol. 7:1997;R414-R417.
    • (1997) Curr. Biol. , vol.7
    • Frazier, J.A.1    Field, C.M.2
  • 80
    • 0348087045 scopus 로고    scopus 로고
    • A formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans
    • Severson A.F., et al. A formin homology protein and a profilin are required for cytokinesis and Arp2/3-independent assembly of cortical microfilaments in C. elegans. Curr. Biol. 12:2002;2066-2075.
    • (2002) Curr. Biol. , vol.12 , pp. 2066-2075
    • Severson, A.F.1
  • 81
    • 0032829333 scopus 로고    scopus 로고
    • Distinct roles of profilin in cell morphological changes: Microspikes, membrane ruffles, stress fibers, and cytokinesis
    • Suetsugu S., et al. Distinct roles of profilin in cell morphological changes: microspikes, membrane ruffles, stress fibers, and cytokinesis. FEBS Lett. 457:1999;470-474.
    • (1999) FEBS Lett. , vol.457 , pp. 470-474
    • Suetsugu, S.1
  • 82
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of profilin in the assembly of actin for microspike formation
    • Suetsugu S., et al. The essential role of profilin in the assembly of actin for microspike formation. EMBO J. 17:1998;6516-6526.
    • (1998) EMBO J. , vol.17 , pp. 6516-6526
    • Suetsugu, S.1
  • 83
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization
    • Machesky L.M., Hall A. Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization. J. Cell Biol. 138:1997;913-926.
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 84
    • 0026611047 scopus 로고
    • Association of p60c-src with endosomal membranes in mammalian fibroblasts
    • Kaplan K.B., et al. Association of p60c-src with endosomal membranes in mammalian fibroblasts. J. Cell Biol. 118:1992;321-333.
    • (1992) J. Cell Biol. , vol.118 , pp. 321-333
    • Kaplan, K.B.1
  • 85
    • 0035960717 scopus 로고    scopus 로고
    • Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity
    • Timpson P., et al. Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity. Curr. Biol. 11:2001;1836-1846.
    • (2001) Curr. Biol. , vol.11 , pp. 1836-1846
    • Timpson, P.1
  • 86
    • 0024296405 scopus 로고
    • Altered phosphorylation and activation of pp60c-src during fibroblast mitosis
    • Chackalaparampil I., Shalloway D. Altered phosphorylation and activation of pp60c-src during fibroblast mitosis. Cell. 52:1988;801-810.
    • (1988) Cell , vol.52 , pp. 801-810
    • Chackalaparampil, I.1    Shalloway, D.2
  • 87
    • 0030979676 scopus 로고    scopus 로고
    • Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis
    • Resnick R.J., et al. Phosphorylation of the Src substrate Sam68 by Cdc2 during mitosis. Oncogene. 15:1997;1247-1253.
    • (1997) Oncogene , vol.15 , pp. 1247-1253
    • Resnick, R.J.1
  • 88
    • 0025605786 scopus 로고
    • Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells
    • David-Pfeuty T., Nouvian-Dooghe Y. Immunolocalization of the cellular src protein in interphase and mitotic NIH c-src overexpresser cells. J. Cell Biol. 111:1990;3097-3116.
    • (1990) J. Cell Biol. , vol.111 , pp. 3097-3116
    • David-Pfeuty, T.1    Nouvian-Dooghe, Y.2
  • 89
    • 0028988998 scopus 로고
    • Elongation factor 1 alpha, translation and the cytoskeleton
    • Condeelis J. Elongation factor 1 alpha, translation and the cytoskeleton. Trends Biochem. Sci. 20:1995;169-170.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 169-170
    • Condeelis, J.1
  • 90
    • 0034638596 scopus 로고    scopus 로고
    • Elongation factor-1 alpha is a novel substrate of rho-associated kinase
    • Izawa T., et al. Elongation factor-1 alpha is a novel substrate of rho-associated kinase. Biochem. Biophys. Res. Commun. 278:2000;72-78.
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 72-78
    • Izawa, T.1
  • 91
    • 0036635310 scopus 로고    scopus 로고
    • Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer
    • Anand N., et al. Protein elongation factor EEF1A2 is a putative oncogene in ovarian cancer. Nat. Genet. 31:2002;301-305.
    • (2002) Nat. Genet. , vol.31 , pp. 301-305
    • Anand, N.1
  • 92
    • 0029981258 scopus 로고    scopus 로고
    • Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins
    • Jansen R.P., et al. Mother cell-specific HO expression in budding yeast depends on the unconventional myosin myo4p and other cytoplasmic proteins. Cell. 84:1996;687-697.
    • (1996) Cell , vol.84 , pp. 687-697
    • Jansen, R.P.1
  • 93
    • 0030471363 scopus 로고    scopus 로고
    • Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends
    • Murray J.W., et al. Bundling of actin filaments by elongation factor 1 alpha inhibits polymerization at filament ends. J. Cell Biol. 135:1996;1309-1321.
    • (1996) J. Cell Biol. , vol.135 , pp. 1309-1321
    • Murray, J.W.1
  • 94
    • 0035838320 scopus 로고    scopus 로고
    • A Rho-dependent signaling pathway operating through myosin localizes beta-actin mRNA in fibroblasts
    • Latham V.M., et al. A Rho-dependent signaling pathway operating through myosin localizes beta-actin mRNA in fibroblasts. Curr. Biol. 11:2001;1010-1016.
    • (2001) Curr. Biol. , vol.11 , pp. 1010-1016
    • Latham, V.M.1
  • 95
    • 0033519623 scopus 로고    scopus 로고
    • Localization and anchoring of mRNA in budding yeast
    • Beach D.L., et al. Localization and anchoring of mRNA in budding yeast. Curr. Biol. 9:1999;569-578.
    • (1999) Curr. Biol. , vol.9 , pp. 569-578
    • Beach, D.L.1
  • 96
    • 0034877024 scopus 로고    scopus 로고
    • Structure of AF3p21, a new member of mixed lineage leukemia (MLL) fusion partner proteins-implication for MLL-induced leukemogenesis
    • Sano K. Structure of AF3p21, a new member of mixed lineage leukemia (MLL) fusion partner proteins-implication for MLL-induced leukemogenesis. Leuk. Lymphoma. 42:2001;595-602.
    • (2001) Leuk. Lymphoma , vol.42 , pp. 595-602
    • Sano, K.1
  • 97
    • 0035918136 scopus 로고    scopus 로고
    • SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation
    • Lim C.S., et al. SPIN90 (SH3 protein interacting with Nck, 90 kDa), an adaptor protein that is developmentally regulated during cardiac myocyte differentiation. J. Biol. Chem. 276:2001;12871-12878.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12871-12878
    • Lim, C.S.1
  • 98
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (n-wasp) binding protein, wish, induces arp2/3 complex activation independent of cdc42
    • Fukuoka M., et al. A novel neural Wiskott-Aldrich syndrome protein (n-wasp) binding protein, wish, induces arp2/3 complex activation independent of cdc42. J. Cell Biol. 152:2001;471-482.
    • (2001) J. Cell Biol. , vol.152 , pp. 471-482
    • Fukuoka, M.1
  • 99
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: A new generation of protein database search programs
    • Altschul S.F., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25:1997;3389-3402.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3389-3402
    • Altschul, S.F.1
  • 100
    • 0021984210 scopus 로고
    • Effect of capping protein on the kinetics of actin polymerization
    • Cooper J.A., Pollard T.D. Effect of capping protein on the kinetics of actin polymerization. Biochemistry. 24:1985;793-799.
    • (1985) Biochemistry , vol.24 , pp. 793-799
    • Cooper, J.A.1    Pollard, T.D.2
  • 101
    • 0035204484 scopus 로고    scopus 로고
    • The social life of actin and microtubules: Interaction versus cooperation
    • Yarm F., et al. The social life of actin and microtubules: interaction versus cooperation. Curr. Opin. Microbiol. 4:2001;696-702.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 696-702
    • Yarm, F.1
  • 102
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: Externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK- independent mechanism
    • Riveline D., et al. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK- independent mechanism. J. Cell Biol. 153:2001;1175-1186.
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1
  • 103
    • 0036305635 scopus 로고    scopus 로고
    • ROCK and Dia have opposing effects on adherens junctions downstream of Rho
    • Sahai E., Marshall C.J. ROCK and Dia have opposing effects on adherens junctions downstream of Rho. Nat. Cell Biol. 4:2002;408-415.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 408-415
    • Sahai, E.1    Marshall, C.J.2
  • 104
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim A.S., et al. Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature. 404:2000;151-158.
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1
  • 105
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42- dependent signals to actin assembly
    • Rohatgi R., et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42- dependent signals to actin assembly. Cell. 97:1999;221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1
  • 106
    • 0034705317 scopus 로고    scopus 로고
    • Negative regulation of fibroblast motility by Ena/VASP proteins
    • Bear J.E., et al. Negative regulation of fibroblast motility by Ena/VASP proteins. Cell. 101:2000;717-728.
    • (2000) Cell , vol.101 , pp. 717-728
    • Bear, J.E.1
  • 107
    • 17344369363 scopus 로고    scopus 로고
    • A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: Evidence for conserved function in oogenesis and implications for human sterility
    • Bione S., et al. A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: evidence for conserved function in oogenesis and implications for human sterility. Am. J. Hum. Genet. 62:1998;533-541.
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 533-541
    • Bione, S.1
  • 108
    • 0029666043 scopus 로고    scopus 로고
    • The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes
    • Sen-Gupta M., et al. The sequence of a 24,152 bp segment from the left arm of chromosome XIV from Saccharomyces cerevisiae between the BNI1 and the POL2 genes. Yeast. 12:1996;505-514.
    • (1996) Yeast , vol.12 , pp. 505-514
    • Sen-Gupta, M.1
  • 109
    • 0028973402 scopus 로고
    • Cappuccino, a Drosophila maternal effect gene required for polarity of the egg and embryo, is related to the vertebrate limb deformity locus
    • Emmons S., et al. Cappuccino, a Drosophila maternal effect gene required for polarity of the egg and embryo, is related to the vertebrate limb deformity locus. Genes Dev. 9:1995;2482-2494.
    • (1995) Genes Dev. , vol.9 , pp. 2482-2494
    • Emmons, S.1
  • 110
    • 0030927282 scopus 로고    scopus 로고
    • The Aspergillus nidulans sepA gene encodes an FH1/2 protein involved in cytokinesis and the maintenance of cellular polarity
    • Harris S.D., et al. The Aspergillus nidulans sepA gene encodes an FH1/2 protein involved in cytokinesis and the maintenance of cellular polarity. EMBO J. 16:1997;3474-3483.
    • (1997) EMBO J. , vol.16 , pp. 3474-3483
    • Harris, S.D.1
  • 111
    • 0026533152 scopus 로고
    • The chicken limb deformity gene encodes nuclear proteins expressed in specific cell types during morphogenesis
    • Trumpp A., et al. The chicken limb deformity gene encodes nuclear proteins expressed in specific cell types during morphogenesis. Genes Dev. 6:1992;14-28.
    • (1992) Genes Dev. , vol.6 , pp. 14-28
    • Trumpp, A.1
  • 112
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik R.P., et al. 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature. 346:1990;850-853.
    • (1990) Nature , vol.346 , pp. 850-853
    • Woychik, R.P.1
  • 113
    • 0026575833 scopus 로고
    • A variant limb deformity transcript expressed in the embryonic mouse limb defines a novel formin
    • Jackson-Grusby L., et al. A variant limb deformity transcript expressed in the embryonic mouse limb defines a novel formin. Genes Dev. 6:1992;29-37.
    • (1992) Genes Dev. , vol.6 , pp. 29-37
    • Jackson-Grusby, L.1
  • 114
    • 0034191965 scopus 로고    scopus 로고
    • Formin-2, a novel formin homology protein of the cappuccino subfamily, is highly expressed in the developing and adult central nervous system
    • Leader B., Leder P. Formin-2, a novel formin homology protein of the cappuccino subfamily, is highly expressed in the developing and adult central nervous system. Mech. Dev. 93:2000;221-231.
    • (2000) Mech. Dev. , vol.93 , pp. 221-231
    • Leader, B.1    Leder, P.2
  • 115
    • 0029019950 scopus 로고
    • Characterization of Fus1 of Schizosaccharomyces pombe: A developmentally controlled function needed for conjugation
    • Petersen J., et al. Characterization of Fus1 of Schizosaccharomyces pombe: a developmentally controlled function needed for conjugation. Mol. Cell. Biol. 15:1995;3697-3707.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3697-3707
    • Petersen, J.1
  • 116
    • 0031818091 scopus 로고    scopus 로고
    • Cyk-1: A C. elegans FH gene required for a late step in embryonic cytokinesis
    • Swan K.A., et al. cyk-1: a C. elegans FH gene required for a late step in embryonic cytokinesis. J. Cell Sci. 111:1998;2017-2027.
    • (1998) J. Cell Sci. , vol.111 , pp. 2017-2027
    • Swan, K.A.1
  • 117
    • 0035966322 scopus 로고    scopus 로고
    • Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1
    • Habas R., et al. Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1. Cell. 107:2001;843-854.
    • (2001) Cell , vol.107 , pp. 843-854
    • Habas, R.1
  • 118
    • 0032981482 scopus 로고    scopus 로고
    • Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein
    • Lev S., et al. Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol. Cell. Biol. 19:1999;2278-2288.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2278-2288
    • Lev, S.1
  • 119
    • 85031138181 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by auto-inhibition
    • in press
    • Li, F. and Higgs, H.N. The mouse formin mDia1 is a potent actin nucleation factor regulated by auto-inhibition. Curr. Biol. (in press).
    • Curr. Biol.
    • Li, F.1    Higgs, H.N.2


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