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Volumn 7, Issue 11, 2002, Pages 492-498

Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; ARABIDOPSIS; FUNGI;

EID: 0036835889     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1360-1385(02)02341-5     Document Type: Review
Times cited : (130)

References (68)
  • 3
    • 0032007313 scopus 로고    scopus 로고
    • In vivo functions of actin binding proteins
    • Asycough, K.R. (1998) In vivo functions of actin binding proteins. Curr. Opin. Cell Biol. 10, 102-111
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 102-111
    • Asycough, K.R.1
  • 4
    • 0032475981 scopus 로고    scopus 로고
    • Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover
    • Didry, D. et al. (1998) Synergy between actin depolymerizing factor/cofilin and profilin in increasing actin filament turnover. J. Biol. Chem. 273, 25602-25611
    • (1998) J. Biol. Chem. , vol.273 , pp. 25602-25611
    • Didry, D.1
  • 5
    • 0035145686 scopus 로고    scopus 로고
    • Interaction of pollen-specific actin-depolymerizing factor with actin
    • Smertenko, A.P. et al. (2001) Interaction of pollen-specific actin-depolymerizing factor with actin. Plant J. 25, 203-212
    • (2001) Plant J. , vol.25 , pp. 203-212
    • Smertenko, A.P.1
  • 6
    • 0030006089 scopus 로고    scopus 로고
    • Pollen specific expression of maize genes encoding actin depolymerizing factor-like proteins
    • Lopez, I. et al. (1996) Pollen specific expression of maize genes encoding actin depolymerizing factor-like proteins. Proc. Natl. Acad. Sci. U. S. A. 93, 7415-7420
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 7415-7420
    • Lopez, I.1
  • 7
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J.R. (1999) Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 8
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang, F. et al. (1999) Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J. Biol. Chem. 274, 36963-36972
    • (1999) J. Biol. Chem. , vol.274 , pp. 36963-36972
    • Kang, F.1
  • 9
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • Kovar, D.R. et al. (2000) Maize profilin isoforms are functionally distinct. Plant Cell 12, 583-598
    • (2000) Plant Cell , vol.12 , pp. 583-598
    • Kovar, D.R.1
  • 10
    • 0033653820 scopus 로고    scopus 로고
    • Intracellular pH modulation of ADF/cofilin proteins
    • Bernstein, B.W. et al. (2000) Intracellular pH modulation of ADF/cofilin proteins. Cell Motil. Cytoskeleton 47, 319-336
    • (2000) Cell Motil. Cytoskeleton , vol.47 , pp. 319-336
    • Bernstein, B.W.1
  • 11
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa, N. et al. (1985) pH control of actin polymerization by cofilin. J. Biol. Chem. 260, 14410-14412
    • (1985) J. Biol. Chem. , vol.260 , pp. 14410-14412
    • Yonezawa, N.1
  • 12
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins, M. et al. (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32, 9985-9993
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1
  • 13
    • 0032565962 scopus 로고    scopus 로고
    • Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase
    • Arber, S. et al. (1998) Regulation of actin dynamics through phosphorylation of cofilin by LIM-kinase. Nature 393, 805-809
    • (1998) Nature , vol.393 , pp. 805-809
    • Arber, S.1
  • 14
    • 0032053115 scopus 로고    scopus 로고
    • Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity
    • Smertenko, A.P. et al. (1998) Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity. Plant J. 14, 187-193
    • (1998) Plant J. , vol.14 , pp. 187-193
    • Smertenko, A.P.1
  • 15
    • 0035876055 scopus 로고    scopus 로고
    • Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase
    • Allwood, E.G. et al. (2001) Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase. FEBS Lett. 499, 97-100
    • (2001) FEBS Lett. , vol.499 , pp. 97-100
    • Allwood, E.G.1
  • 16
    • 0032443967 scopus 로고    scopus 로고
    • Interaction of maize actin-depolymerising factor with actin and phosphoinositides and its inhibition of plant phospholipase C
    • Gungabissoon, R.A. et al. (1998) Interaction of maize actin-depolymerising factor with actin and phosphoinositides and its inhibition of plant phospholipase C. Plant J. 16, 689-696
    • (1998) Plant J. , vol.16 , pp. 689-696
    • Gungabissoon, R.A.1
  • 17
    • 0023940928 scopus 로고
    • Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex
    • Lassing, I. and Lindberg, U. (1988) Specificity of the interaction between phosphatidylinositol 4,5-bisphosphate and the profilin:actin complex. J. Cell Biol. 37, 255-267
    • (1988) J. Cell Biol. , vol.37 , pp. 255-267
    • Lassing, I.1    Lindberg, U.2
  • 18
    • 0025308055 scopus 로고
    • 2 and inhibits its hydrolysis by phospholipase C
    • 2 and inhibits its hydrolysis by phospholipase C. Science 247, 1575-1578
    • (1990) Science , vol.247 , pp. 1575-1578
    • Goldschmidt-Clermont, P.J.1
  • 19
    • 0028105664 scopus 로고
    • Inhibition of plant plasma-membrane phosphoinositide phospholipase-C by the actin-binding protein, profilin
    • Drøbak, B.K. et al. (1994) Inhibition of plant plasma-membrane phosphoinositide phospholipase-C by the actin-binding protein, profilin. Plant J. 6, 389-400
    • (1994) Plant J. , vol.6 , pp. 389-400
    • Drøbak, B.K.1
  • 20
    • 0030930427 scopus 로고    scopus 로고
    • F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)
    • Jiang, C.J. et al. (1997) F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF). Proc. Natl. Acad. Sci. U. S. A. 94, 9973-9978
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9973-9978
    • Jiang, C.J.1
  • 21
    • 0039699925 scopus 로고    scopus 로고
    • Redistribution of actin, profilin and phosphatidylinositol-4,5-bisphosphate in growing and maturing root hairs
    • Braun, M. et al. (1999) Redistribution of actin, profilin and phosphatidylinositol-4,5-bisphosphate in growing and maturing root hairs. Planta 209, 435-443
    • (1999) Planta , vol.209 , pp. 435-443
    • Braun, M.1
  • 22
    • 0034669149 scopus 로고    scopus 로고
    • Root hair formation: F-actin-dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges
    • Baluska, F. et al. (2000) Root hair formation: F-actin-dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges. Dev. Biol. 227, 618-632
    • (2000) Dev. Biol. , vol.227 , pp. 618-632
    • Baluska, F.1
  • 23
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt, M.R. and Koffer, A. (2001) Cell motility: proline-rich proteins promote protrusions. Trends Cell Biol. 11, 38-46
    • (2001) Trends Cell Biol. , vol.11 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 24
    • 0033563261 scopus 로고    scopus 로고
    • Polyproline binding is an essential function of human profilin in yeast
    • Ostrander, D.B. et al. (1997) Polyproline binding is an essential function of human profilin in yeast. Eur. J. Biochem. 262, 26-35
    • (1997) Eur. J. Biochem. , vol.262 , pp. 26-35
    • Ostrander, D.B.1
  • 25
    • 0035887313 scopus 로고    scopus 로고
    • A WASP-VASP complex regulates actin polymerization at the plasma membrane
    • Castellano, F. et al. (2001) A WASP-VASP complex regulates actin polymerization at the plasma membrane. EMBO J. 20, 5603-5614
    • (2001) EMBO J. , vol.20 , pp. 5603-5614
    • Castellano, F.1
  • 26
    • 0035889090 scopus 로고    scopus 로고
    • A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast
    • Lechler, T. et al. (2001) A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J. Cell Biol. 155, 261-270
    • (2001) J. Cell Biol. , vol.155 , pp. 261-270
    • Lechler, T.1
  • 27
    • 0035809163 scopus 로고    scopus 로고
    • A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, inducesArp2/3 complex activation independent of Cdc42
    • Fukuoka, M. et al. (2001) A novel neural Wiskott-Aldrich syndrome protein (N-WASP) binding protein, WISH, inducesArp2/3 complex activation independent of Cdc42. J. Cell Biol. 152, 471-482
    • (2001) J. Cell Biol. , vol.152 , pp. 471-482
    • Fukuoka, M.1
  • 28
    • 0035914408 scopus 로고    scopus 로고
    • mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation
    • Satoh, S. and Tominaga, T. (2001) mDia-interacting protein acts downstream of Rho-mDia and modifies Src activation and stress fiber formation. J. Biol. Chem. 276, 39290-39294
    • (2001) J. Biol. Chem. , vol.276 , pp. 39290-39294
    • Satoh, S.1    Tominaga, T.2
  • 29
    • 0033741452 scopus 로고    scopus 로고
    • The ROP GTPase: An emerging signaling switch in plants
    • Zheng, Z.L. and Yang, Z. (2000) The ROP GTPase: an emerging signaling switch in plants. Plant Mol. Biol. 44, 1-9
    • (2000) Plant Mol. Biol. , vol.44 , pp. 1-9
    • Zheng, Z.L.1    Yang, Z.2
  • 30
    • 0035047583 scopus 로고    scopus 로고
    • Actin and pollen tube growth
    • Vidali, L. and Hepler, P.K. (2001) Actin and pollen tube growth. Protoplasma 215, 64-76
    • (2001) Protoplasma , vol.215 , pp. 64-76
    • Vidali, L.1    Hepler, P.K.2
  • 31
    • 0344417107 scopus 로고    scopus 로고
    • Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth
    • Kost, B. et al. (1999) Rac homologues and compartmentalized phosphatidylinositol 4, 5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J. Cell Biol. 145, 317-330
    • (1999) J. Cell Biol. , vol.145 , pp. 317-330
    • Kost, B.1
  • 32
    • 0031412148 scopus 로고    scopus 로고
    • Inhibition of pollen tube elongation by microinjected anti-Rop1ps antibodies suggests a crucial role for Rho-type GTPases in the control of tip growth
    • Lin, Y. and Yang, Z. (1997) Inhibition of pollen tube elongation by microinjected anti-Rop1ps antibodies suggests a crucial role for Rho-type GTPases in the control of tip growth. Plant Cell 9, 1647-1659
    • (1997) Plant Cell , vol.9 , pp. 1647-1659
    • Lin, Y.1    Yang, Z.2
  • 33
    • 0035355361 scopus 로고    scopus 로고
    • Arabidopsis thaliana ROP GTPases are localized to tips of root hairs and control polar growth
    • Molendijk, A.J. et al. (2001) Arabidopsis thaliana ROP GTPases are localized to tips of root hairs and control polar growth. EMBO J. 20, 2779-2788
    • (2001) EMBO J. , vol.20 , pp. 2779-2788
    • Molendijk, A.J.1
  • 34
    • 0035999366 scopus 로고    scopus 로고
    • The ROP2 GTPase controls the formation of cortical fine F-actin and the early phase of directional cell expansion during Arabidopsis organogenesis
    • Fu, Y. et al. (2002) The ROP2 GTPase controls the formation of cortical fine F-actin and the early phase of directional cell expansion during Arabidopsis organogenesis. Plant Cell 14, 777-794
    • (2002) Plant Cell , vol.14 , pp. 777-794
    • Fu, Y.1
  • 35
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik, R.P. et al. (1990) 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature 346, 850-853
    • (1990) Nature , vol.346 , pp. 850-853
    • Woychik, R.P.1
  • 36
    • 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. (1997) Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science 278, 1315-1318
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1
  • 37
    • 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. and Wasserman, S.A. (1994) Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120, 3367-3377
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.H.1    Wasserman, S.A.2
  • 38
    • 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. (1998) cyk-1: a C. elegans FH gene required for a late step in embryonic cytokinesis. J. Cell Sci. 111, 2017-2027
    • (1998) J. Cell Sci. , vol.111 , pp. 2017-2027
    • Swan, K.A.1
  • 39
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M. et al. (2002) Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat. Cell Biol. 4, 32-41
    • (2002) Nat. Cell Biol. , vol.4 , pp. 32-41
    • Evangelista, M.1
  • 40
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot, I. et al. (2002) Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat. Cell Biol. 4, 42-50
    • (2002) Nat. Cell Biol. , vol.4 , pp. 42-50
    • Sagot, I.1
  • 41
    • 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. (1998) 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) J. Cell Biol. , vol.141 , pp. 1217-1228
    • Petersen, J.1
  • 42
    • 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. (1997) 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, 169-182
    • (1997) J. Cell Biol. , vol.137 , pp. 169-182
    • Chang, 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. and Chang, F. (2001) Roles of the fission yeast formin For3p in cell polarity, actin cable formation and symmetric cell division. Curr. Biol. 11, 1656-1665
    • (2001) Curr. Biol. , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 44
    • 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. (1995) 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, 2482-2494
    • (1995) Genes Dev. , vol.9 , pp. 2482-2494
    • Emmons, S.1
  • 45
    • 0033535351 scopus 로고    scopus 로고
    • Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p
    • Lee, L. et al. (1999) Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p. J. Cell Biol. 144, 947-961
    • (1999) J. Cell Biol. , vol.144 , pp. 947-961
    • Lee, L.1
  • 46
    • 0034907213 scopus 로고    scopus 로고
    • mDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A.F. et al. (2001) mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3, 723-729
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1
  • 47
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells
    • Kato, T. et al. (2000) Localization of a mammalian homolog of diaphanous, mDia1, to the mitotic spindle in HeLa cells. J. Cell Sci. 114, 775-784
    • (2000) J. Cell Sci. , vol.114 , pp. 775-784
    • Kato, T.1
  • 48
    • 0033563261 scopus 로고    scopus 로고
    • Polyproline binding is an essential function of human profilin in yeast
    • Darin, B. et al. (1999) Polyproline binding is an essential function of human profilin in yeast. Eur. J. Biochem. 262, 26-35
    • (1999) Eur. J. Biochem. , vol.262 , pp. 26-35
    • Darin, B.1
  • 49
    • 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. (1997) 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) EMBO J. , vol.16 , pp. 3044-3056
    • Watanabe, N.1
  • 50
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe, N. et al. (1999) Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat. Cell Biol. 1, 136-143
    • (1999) Nat. Cell Biol. , vol.1 , pp. 136-143
    • Watanabe, N.1
  • 51
    • 0037178706 scopus 로고    scopus 로고
    • Role of formins in actin assembly: Nucleation and barbed-end association
    • Pruyne, D. et al. (2002) Role of formins in actin assembly: nucleation and barbed-end association. Science 297, 612-615
    • (2002) Science , vol.297 , pp. 612-615
    • Pruyne, D.1
  • 52
    • 0036049615 scopus 로고    scopus 로고
    • An actin nucleation mechanism mediated by Bni1 and profilin
    • Sagot, I. et al. (2002) An actin nucleation mechanism mediated by Bni1 and profilin. Nat. Cell Biol. 4, 626-631
    • (2002) Nat. Cell Biol. , vol.4 , pp. 626-631
    • Sagot, I.1
  • 53
    • 0035141074 scopus 로고    scopus 로고
    • Coordination of microtubules and the actin cytoskeleton by the Rho effector mDial
    • Ishizaki, T. et al. (2001) Coordination of microtubules and the actin cytoskeleton by the Rho effector mDial. Nat. Cell Biol. 3, 8-14
    • (2001) Nat. Cell Biol. , vol.3 , pp. 8-14
    • Ishizaki, T.1
  • 54
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoregulatory domain
    • Alberts, A.S. (2001) Identification of a carboxyl-terminal Diaphanous-related formin homology protein autoregulatory domain. J. Biol. Chem. 276, 2824-2830
    • (2001) J. Biol. Chem. , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 55
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerising protein N-WASP
    • Miki, H. et al. (1998) Induction of filopodium formation by a WASP-related actin-depolymerising protein N-WASP. Nature 391, 93-96
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1
  • 56
    • 0033604447 scopus 로고    scopus 로고
    • An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae
    • Kikyo, M. et al. (1999) An FH domain-containing Bnr1p is a multifunctional protein interacting with a variety of cytoskeletal proteins in Saccharomyces cerevisiae. Oncogene 18, 7046-7054
    • (1999) Oncogene , vol.18 , pp. 7046-7054
    • Kikyo, M.1
  • 57
    • 0031665143 scopus 로고    scopus 로고
    • Rho1p-Bni1p-Spa2p interactions: Implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae
    • Fujiwara, T. et al. (1998) Rho1p-Bni1p-Spa2p interactions: implication in localization of Bni1p at the bud site and regulation of the actin cytoskeleton in Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1221-1233
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1221-1233
    • Fujiwara, T.1
  • 58
    • 0034121194 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis formin-like proteinAFH1 and its interacting protein
    • Banno, H. and Chua, N.H. (2000) Characterization of the Arabidopsis formin-like proteinAFH1 and its interacting protein. Plant Cell Physiol. 41, 617-626
    • (2000) Plant Cell Physiol. , vol.41 , pp. 617-626
    • Banno, H.1    Chua, N.H.2
  • 59
    • 0033648030 scopus 로고    scopus 로고
    • Are plant formins integral membrane proteins?
    • research001.1-001.7
    • Cvrcková, F. (2000) Are plant formins integral membrane proteins? Genome Biol. 1(1) research001.1-001.7 (http://genomebiology.com/2000/1/1/research/001)
    • (2000) Genome Biol. , vol.1 , Issue.1
    • Cvrcková, F.1
  • 60
    • 0032144201 scopus 로고    scopus 로고
    • Stacks on tracks: The plant Golgi apparatus traffics on an actin/ER network
    • Boevink, P. et al. (1998) Stacks on tracks: the plant Golgi apparatus traffics on an actin/ER network. Plant J. 15, 441-447
    • (1998) Plant J. , vol.15 , pp. 441-447
    • Boevink, P.1
  • 61
    • 0026563095 scopus 로고
    • The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts
    • Reinhard, M. et al. (1992) The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts. EMBO J. 11, 2063-2070
    • (1992) EMBO J. , vol.11 , pp. 2063-2070
    • Reinhard, M.1
  • 62
    • 17944375813 scopus 로고    scopus 로고
    • Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
    • Fukui, Y. et al. (2001) Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration. Nature 412, 826-831
    • (2001) Nature , vol.412 , pp. 826-831
    • Fukui, Y.1
  • 63
    • 0032213110 scopus 로고    scopus 로고
    • Activation of Rac1 by a Crk SH3-binding protein, DOCK180
    • Kiyokawa, E. et al. (1998) Activation of Rac1 by a Crk SH3-binding protein, DOCK180. Genes Dev. 12, 3331-3336
    • (1998) Genes Dev. , vol.12 , pp. 3331-3336
    • Kiyokawa, E.1
  • 64
    • 0036007917 scopus 로고    scopus 로고
    • The Arabidopsis SPIKE1 gene is required for normal cell shape control and tissue development
    • Qiu, J.L. et al. (2002) The Arabidopsis SPIKE1 gene is required for normal cell shape control and tissue development. Plant Cell 4, 101-118
    • (2002) Plant Cell , vol.4 , pp. 101-118
    • Qiu, J.L.1
  • 65
    • 0035542789 scopus 로고    scopus 로고
    • A genome-wide analysis of Arabidopsis ROP-interactive CRIB motif-containing proteins that act as ROP GTPase targets
    • Wu, G. et al. (2001) A genome-wide analysis of Arabidopsis ROP-interactive CRIB motif-containing proteins that act as ROP GTPase targets. Plant Cell 13, 2841-2856
    • (2001) Plant Cell , vol.13 , pp. 2841-2856
    • Wu, G.1
  • 66
    • 0031745642 scopus 로고    scopus 로고
    • Detection of deleterious genotypes in multigenerational studies. I. Disruptions in individual Arabidopsis actin genes
    • Gilliland, L.U. et al. (1998) Detection of deleterious genotypes in multigenerational studies. I. Disruptions in individual Arabidopsis actin genes. Genetics 149, 717-725
    • (1998) Genetics , vol.149 , pp. 717-725
    • Gilliland, L.U.1
  • 67
    • 0030019558 scopus 로고    scopus 로고
    • Structure and evolution of the actin gene family in Arabidopsis thaliana
    • McDowell, J.M. et al. (1996) Structure and evolution of the actin gene family in Arabidopsis thaliana. Genetics 142, 587-602
    • (1996) Genetics , vol.142 , pp. 587-602
    • McDowell, J.M.1
  • 68
    • 0036086410 scopus 로고    scopus 로고
    • Recent improvements to the SMART domain-based sequence annotation resource
    • Letunic, I. et al. (2002) Recent improvements to the SMART domain-based sequence annotation resource. Nucleic Acids Res. 30, 242-244
    • (2002) Nucleic Acids Res. , vol.30 , pp. 242-244
    • Letunic, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.