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Volumn 17, Issue 8, 2005, Pages 2296-2313

The formin homology 1 domain modulates the actin nucleation and bundling activity of arabidopsis FORMIN1

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; MONOMERS; NUCLEATION; POLYMERIZATION;

EID: 27744591230     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.105.030908     Document Type: Article
Times cited : (157)

References (74)
  • 1
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • USA
    • Amann, K.J., and Pollard, T.D. (2001). Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy. Proc. Natl. Acad. Sci. USA 981, 15009-15013.
    • (2001) Proc. Natl. Acad. Sci. , vol.981 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 3
    • 0034121194 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis formin-like protein AFH1 and its interacting protein
    • Banno, H., and Chua, N.H. (2000). Characterization of the Arabidopsis formin-like protein AFH1 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
  • 4
    • 0034720293 scopus 로고    scopus 로고
    • Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins
    • Blanchoin, L., Amann, K.J., Higgs, H.N., Marchand, J.B., Kaiser, D.A., and Pollard, T.D. (2000b). Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404, 1007-1011.
    • (2000) Nature , vol.404 , pp. 1007-1011
    • Blanchoin, L.1    Amann, K.J.2    Higgs, H.N.3    Marchand, J.B.4    Kaiser, D.A.5    Pollard, T.D.6
  • 5
    • 0034687235 scopus 로고    scopus 로고
    • Interaction of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks
    • Blanchoin, L., Pollard, T.D., and Mullins, R.D. (2000a). Interaction of ADF/cofilin, Arp2/3 complex, capping protein and profilin in remodeling of branched actin filament networks. Curr. Biol. 10, 1273-1282.
    • (2000) Curr. Biol. , vol.10 , pp. 1273-1282
    • Blanchoin, L.1    Pollard, T.D.2    Mullins, R.D.3
  • 6
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • Carlier, M.F., Laurent, V., Santolini, J., Melki, R., Didry, D., Xia, G.X., Hong, Y., Chua, N.H., and Pantaloni, D. (1997). Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility. J. Cell Biol. 136, 1307-1322.
    • (1997) J. Cell Biol. , vol.136 , pp. 1307-1322
    • Carlier, M.F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.X.6    Hong, Y.7    Chua, N.H.8    Pantaloni, D.9
  • 7
    • 0036741550 scopus 로고    scopus 로고
    • The regulation of actin organization by actin-depolymerizing factor in elongating pollen tubes
    • Chen, C.Y., Wong, E.I., Vidali, L., Estavillo, A., Hepler, P.K., Wu, H.M., and Cheung, A.Y. (2002). The regulation of actin organization by actin-depolymerizing factor in elongating pollen tubes. Plant Cell 14, 2175-2190.
    • (2002) Plant Cell , vol.14 , pp. 2175-2190
    • Chen, C.Y.1    Wong, E.I.2    Vidali, L.3    Estavillo, A.4    Hepler, P.K.5    Wu, H.M.6    Cheung, A.Y.7
  • 8
    • 0842291746 scopus 로고    scopus 로고
    • Overexpression of an Arabidopsis formin stimulates supernumerary actin cable formation from pollen tube cell membrane
    • Cheung, A.Y., and Wu, H.M. (2004). Overexpression of an Arabidopsis formin stimulates supernumerary actin cable formation from pollen tube cell membrane. Plant Cell 16, 257-269.
    • (2004) Plant Cell , vol.16 , pp. 257-269
    • Cheung, A.Y.1    Wu, H.M.2
  • 9
    • 0033648030 scopus 로고    scopus 로고
    • Are plant formins integral membrane proteins?
    • Cvrcková, F. (2000). Are plant formins integral membrane proteins? Genome Biol. 1, 1-7.
    • (2000) Genome Biol. , vol.1 , pp. 1-7
    • Cvrcková, F.1
  • 10
    • 9444255105 scopus 로고    scopus 로고
    • Formin homology 2 domains occur in multiple contexts in angiosperms
    • Cvrcková, F., Novotny, M., Pickova, D., and Zársky, V. (2004). Formin homology 2 domains occur in multiple contexts in angiosperms. BMC Genomics 5, 1-18.
    • (2004) BMC Genomics , vol.5 , pp. 1-18
    • Cvrcková, F.1    Novotny, M.2    Pickova, D.3    Zársky, V.4
  • 11
    • 0345014818 scopus 로고    scopus 로고
    • Arp2/3 and 'the shape of things to come'
    • Deeks, M.J., and Hussey, P.J. (2003). Arp2/3 and 'the shape of things to come'. Curr. Opin. Plant Biol. 6, 561-567.
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 561-567
    • Deeks, M.J.1    Hussey, P.J.2
  • 12
    • 0036835889 scopus 로고    scopus 로고
    • Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization
    • Deeks, M.J., Hussey, P.J., and Davies, B. (2002). Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization. Trends Plant Sci. 7, 492-498.
    • (2002) Trends Plant Sci. , vol.7 , pp. 492-498
    • Deeks, M.J.1    Hussey, P.J.2    Davies, B.3
  • 13
    • 0030932405 scopus 로고    scopus 로고
    • Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis
    • Evangelista, M., Blundell, K., Longtine, M., Chow, C., Adames, N., Pringle, J., Peter, M., and Boone, C. (1997). Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Science 276, 118-122.
    • (1997) Science , vol.276 , pp. 118-122
    • Evangelista, M.1    Blundell, K.2    Longtine, M.3    Chow, C.4    Adames, N.5    Pringle, J.6    Peter, M.7    Boone, C.8
  • 14
    • 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., and Bretscher, A. (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    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 16
    • 0027968554 scopus 로고
    • Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli
    • Fedorov, A.A., Pollard, T.D., and Almo, S.C. (1994). Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli. J. Mol. Biol. 241, 480-482.
    • (1994) J. Mol. Biol. , vol.241 , pp. 480-482
    • Fedorov, A.A.1    Pollard, T.D.2    Almo, S.C.3
  • 17
    • 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
  • 18
    • 0033397748 scopus 로고    scopus 로고
    • Latrunculin B has different effects on pollen germination and tube growth
    • Gibbon, B.C., Kovar, D.R., and Staiger, C.J. (1999). Latrunculin B has different effects on pollen germination and tube growth. Plant Cell 11, 2349-2363.
    • (1999) Plant Cell , vol.11 , pp. 2349-2363
    • Gibbon, B.C.1    Kovar, D.R.2    Staiger, C.J.3
  • 19
    • 0030700770 scopus 로고    scopus 로고
    • Characterization of maize (Zea mays) pollen profilin function in vitro and in live cells
    • Gibbon, B.C., Ren, H., and Staiger, C.J. (1997). Characterization of maize (Zea mays) pollen profilin function in vitro and in live cells. Biochem. J. 327, 909-915.
    • (1997) Biochem. J. , vol.327 , pp. 909-915
    • Gibbon, B.C.1    Ren, H.2    Staiger, C.J.3
  • 20
    • 3142530596 scopus 로고    scopus 로고
    • Actin cytoskeleton: Formins lead the way
    • Harris, E.S., and Higgs, H.N. (2004). Actin cytoskeleton: Formins lead the way. Curr. Biol. 14, R520-R522.
    • (2004) Curr. Biol. , vol.14
    • Harris, E.S.1    Higgs, H.N.2
  • 21
    • 2442473140 scopus 로고    scopus 로고
    • The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments
    • Harris, E.S., Li, F., and Higgs, H.N. (2004). The mouse formin, FRLalpha, slows actin filament barbed end elongation, competes with capping protein, accelerates polymerization from monomers, and severs filaments. J. Biol. Chem. 279, 20076-20087.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20076-20087
    • Harris, E.S.1    Li, F.2    Higgs, H.N.3
  • 24
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization
    • Higgs, H.N., Blanchoin, L., and Pollard, T.D. (1999). Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization. Biochemistry 38, 15212-15222.
    • (1999) Biochemistry , vol.38 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 25
  • 26
    • 2542452087 scopus 로고    scopus 로고
    • A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments
    • Huang, S., Blanchoin, L., Chaudhry, F., Franklin-Tong, V.E., and Staiger, C.J. (2004). A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments. J. Biol. Chem. 279, 23364-23375.
    • (2004) J. Biol. Chem. , vol.279 , pp. 23364-23375
    • Huang, S.1    Blanchoin, L.2    Chaudhry, F.3    Franklin-Tong, V.E.4    Staiger, C.J.5
  • 27
    • 0242666072 scopus 로고    scopus 로고
    • Arabidopsis capping protein (AtCP) is a heterodimer that regulates assembly at the barbed ends of actin filaments
    • Huang, S., Blanchoin, L., Kovar, D.R., and Staiger, C.J. (2003). Arabidopsis capping protein (AtCP) is a heterodimer that regulates assembly at the barbed ends of actin filaments. J. Biol. Chem. 278, 44832-44842.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44832-44842
    • Huang, S.1    Blanchoin, L.2    Kovar, D.R.3    Staiger, C.J.4
  • 28
  • 30
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama, T., and Mihashi, K. (1981). Fluorimetry study of N-(1-pyrenyl) iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur. J. Biochem. 114, 33-38.
    • (1981) Eur. J. Biochem. , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 31
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • Kovar, D.R., Drobak, B.K., and Staiger, C.J. (2000a). Maize profilin isoforms are functionally distinct. Plant Cell 12, 583-598.
    • (2000) Plant Cell , vol.12 , pp. 583-598
    • Kovar, D.R.1    Drobak, B.K.2    Staiger, C.J.3
  • 32
    • 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., and Pollard, T.D. (2003). The fission yeast cytokinesis formin Cdc12p is a barbed end actin filament capping protein gated by profilin. J. Cell Biol. 161, 875-887.
    • (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
  • 33
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • USA
    • Kovar, D.R., and Pollard, T.D. (2004a). Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces. Proc. Natl. Acad. Sci. USA 101, 14725-14730.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 34
    • 10344234183 scopus 로고    scopus 로고
    • Progressing actin: Formin as a processive elongation machine
    • Kovar, D.R., and Pollard, T.D. (2004b). Progressing actin: Formin as a processive elongation machine. Nat. Cell Biol. 6, 1158-1159.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1158-1159
    • Kovar, D.R.1    Pollard, T.D.2
  • 35
    • 0034525206 scopus 로고    scopus 로고
    • AtFim1 is an actin filament crosslinking protein from Arabidopsis thaliana
    • Kovar, D.R., Staiger, C.J., Weaver, E.A., and McCurdy, D.W. (2000b). AtFim1 is an actin filament crosslinking protein from Arabidopsis thaliana. Plant J. 24, 625-636.
    • (2000) Plant J. , vol.24 , pp. 625-636
    • Kovar, D.R.1    Staiger, C.J.2    Weaver, E.A.3    McCurdy, D.W.4
  • 36
    • 0042701884 scopus 로고    scopus 로고
    • Requirements for Arabidopsis ATARP2 and ATARP3 during epidermal development
    • Le, J., El-Assal Sel, D., Basu, D., Saad, M.E., and Szymanski, D.B. (2003). Requirements for Arabidopsis ATARP2 and ATARP3 during epidermal development. Curr. Biol. 13, 1341-1347.
    • (2003) Curr. Biol. , vol.13 , pp. 1341-1347
    • Le, J.1    El-Assal Sel, D.2    Basu, D.3    Saad, M.E.4    Szymanski, D.B.5
  • 37
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li, F., and Higgs, H.N. (2003). The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr. Biol. 13, 1335-1340.
    • (2003) Curr. Biol. , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 38
    • 0037097589 scopus 로고    scopus 로고
    • Arp2/3 complex is required for actin polymerization during platelet shape change
    • Li, Z., Kim, E.S., and Bearer, E.L (2002). Arp2/3 complex is required for actin polymerization during platelet shape change. Blood 99, 4466-4474.
    • (2002) Blood , vol.99 , pp. 4466-4474
    • Li, Z.1    Kim, E.S.2    Bearer, E.L.3
  • 39
    • 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
  • 40
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose
    • Machesky, L.M., Atkinson, S.J., Ampe, C., Vandekerckhove, J., and Pollard, T.D. (1994). Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose. J. Cell Biol. 127, 107-115.
    • (1994) J. Cell Biol. , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 41
    • 0036264824 scopus 로고    scopus 로고
    • The ADF/cofilin family: Actin-remodeling proteins
    • Maciver, S.K., and Hussey, P.J. (2002). The ADF/cofilin family: Actin-remodeling proteins. Genome Biol. 3.
    • (2002) Genome Biol. , vol.3
    • Maciver, S.K.1    Hussey, P.J.2
  • 42
    • 0018891631 scopus 로고
    • Mechanism of action of cytochalasin B on actin
    • MacLean-Fletcher, S., and Pollard, T.D. (1980). Mechanism of action of cytochalasin B on actin. Cell 20, 329-341.
    • (1980) Cell , vol.20 , pp. 329-341
    • MacLean-Fletcher, S.1    Pollard, T.D.2
  • 43
    • 0037704913 scopus 로고    scopus 로고
    • Mutations in actin-related proteins 2 and 3 affect cell shape development in Arabidopsis
    • Mathur, J., Mathur, N., Kemebeck, B., and Hulskamp, M. (2003a). Mutations in actin-related proteins 2 and 3 affect cell shape development in Arabidopsis. Plant Cell 15, 1632-1645.
    • (2003) Plant Cell , vol.15 , pp. 1632-1645
    • Mathur, J.1    Mathur, N.2    Kemebeck, B.3    Hulskamp, M.4
  • 44
    • 0041669579 scopus 로고    scopus 로고
    • Arabidopsis CROOKED encodes for the smallest subunit of the ARP2/3 complex and controls cell shape by region specific fine F-actin formation
    • Mathur, J., Mathur, N., Kirik, V., Kernebeck, B., Srinivas, B.P., and Hulskamp, M. (2003b). Arabidopsis CROOKED encodes for the smallest subunit of the ARP2/3 complex and controls cell shape by region specific fine F-actin formation. Development 130, 3137-3146.
    • (2003) Development , vol.130 , pp. 3137-3146
    • Mathur, J.1    Mathur, N.2    Kirik, V.3    Kernebeck, B.4    Srinivas, B.P.5    Hulskamp, M.6
  • 45
    • 0742305302 scopus 로고    scopus 로고
    • A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin
    • Moseley, J.B., Sagot, I., Manning, A.L., Xu, Y., Eck, M.J., Pellman, D., and Goode, B.L. (2004). A conserved mechanism for Bni1- and mDia1-induced actin assembly and dual regulation of Bni1 by Bud6 and profilin. Mol. Biol. Cell 15, 896-907.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 896-907
    • Moseley, J.B.1    Sagot, I.2    Manning, A.L.3    Xu, Y.4    Eck, M.J.5    Pellman, D.6    Goode, B.L.7
  • 46
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed end capping, and formation of branching networks of filaments
    • USA
    • Mullins, R.D., Heuser, J.A., and Pollard, T.D. (1998). The interaction of Arp2/3 complex with actin: Nucleation, high-affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA 95, 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 47
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • Otomo, T., Tomchick, D.R., Otomo, C., Panchal, S.C., Machius, M., and Rosen, M.K. (2005). Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488-494.
    • (2005) Nature , vol.433 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 48
    • 0021200245 scopus 로고
    • Polymerization of ADP-actin
    • Pollard, T.D. (1984). Polymerization of ADP-actin. J. Cell Biol. 99, 769-777.
    • (1984) J. Cell Biol. , vol.99 , pp. 769-777
    • Pollard, T.D.1
  • 49
    • 0033895234 scopus 로고    scopus 로고
    • Molecular mechanisms controlling actin filament dynamics in nonmuscle cells
    • Pollard, T.D., Blanchoin, L., and Mullins, R.D. (2000). Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545-576.
    • (2000) Annu. Rev. Biophys. Biomol. Struct. , vol.29 , pp. 545-576
    • Pollard, T.D.1    Blanchoin, L.2    Mullins, R.D.3
  • 50
  • 51
  • 53
    • 7044224754 scopus 로고    scopus 로고
    • Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis
    • Romero, S., Le Clainche, C., Didry, D., Egile, C., Pantaloni, D., and Carlier, M.F. (2004). Formin is a processive motor that requires profilin to accelerate actin assembly and associated ATP hydrolysis. Cell 119, 419-429.
    • (2004) Cell , vol.119 , pp. 419-429
    • Romero, S.1    Le Clainche, C.2    Didry, D.3    Egile, C.4    Pantaloni, D.5    Carlier, M.F.6
  • 54
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot, I., Klee, S.K., and Pellman, D. (2002a). 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    Klee, S.K.2    Pellman, D.3
  • 56
    • 1542285173 scopus 로고    scopus 로고
    • The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization
    • Shimada, A., Nyitrai, M., Vetter, I.R., Kuhlmann, D., Bugyi, B., Narumjya, S., Geeves, M.A., and Wittinghofer, A. (2004). The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization. Mol. Cell 13, 511-522.
    • (2004) Mol. Cell , vol.13 , pp. 511-522
    • Shimada, A.1    Nyitrai, M.2    Vetter, I.R.3    Kuhlmann, D.4    Bugyi, B.5    Narumjya, S.6    Geeves, M.A.7    Wittinghofer, A.8
  • 57
  • 58
    • 1242265771 scopus 로고    scopus 로고
    • Actin polymerization: Riding the wave
    • Smith, L.G., and Li, R. (2004). Actin polymerization: Riding the wave. Curr. Biol. 14, R109-R111.
    • (2004) Curr. Biol. , vol.14
    • Smith, L.G.1    Li, R.2
  • 59
    • 0036801753 scopus 로고    scopus 로고
    • Signal-mediated depolymerization of actin in pollen during the self-incompatibility response
    • Snowman, B.N., Kovar, D.R., Shevchenko, G., Franklin-Tong, V.E., and Staiger, C.J. (2002). Signal-mediated depolymerization of actin in pollen during the self-incompatibility response. Plant Cell 14, 2613-2626.
    • (2002) Plant Cell , vol.14 , pp. 2613-2626
    • Snowman, B.N.1    Kovar, D.R.2    Shevchenko, G.3    Franklin-Tong, V.E.4    Staiger, C.J.5
  • 60
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and Watt, S. (1971). The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246, 4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 61
    • 0039005860 scopus 로고    scopus 로고
    • Signaling to the actin cytoskeleton in plants
    • Staiger, C.J. (2000). Signaling to the actin cytoskeleton in plants. Annu. Rev. Plant Physiol. 51, 257-288.
    • (2000) Annu. Rev. Plant Physiol. , vol.51 , pp. 257-288
    • Staiger, C.J.1
  • 63
    • 0028385716 scopus 로고
    • Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments
    • Staiger, C.J., Yuan, M., Valenta, R., Shaw, P.J., Warn, R.M., and Lloyd, C.W. (1994). Microinjected profilin affects cytoplasmic streaming in plant cells by rapidly depolymerizing actin microfilaments. Curr. Biol. 4, 215-219.
    • (1994) Curr. Biol. , vol.4 , pp. 215-219
    • Staiger, C.J.1    Yuan, M.2    Valenta, R.3    Shaw, P.J.4    Warn, R.M.5    Lloyd, C.W.6
  • 64
    • 0033391596 scopus 로고    scopus 로고
    • Organized F-actin is essential for normal trichome morphogenesis in Arabidopsis
    • Szymanski, D.B., Marks, M.D., and Wick, S.M. (1999). Organized F-actin is essential for normal trichome morphogenesis in Arabidopsis. Plant Cell 11, 2331-2347.
    • (1999) Plant Cell , vol.11 , pp. 2331-2347
    • Szymanski, D.B.1    Marks, M.D.2    Wick, S.M.3
  • 65
    • 7044246167 scopus 로고    scopus 로고
    • Molecular dissection of plant cytokinesis and phragmoplast structure: A survey of GFP-tagged proteins
    • Van Damme, D., Bouget, F.Y., Van Poucke, K., Inze, D., and Geelen, D. (2004). Molecular dissection of plant cytokinesis and phragmoplast structure: A survey of GFP-tagged proteins. Plant J. 40, 386-398.
    • (2004) Plant J. , vol.40 , pp. 386-398
    • Van Damme, D.1    Bouget, F.Y.2    Van Poucke, K.3    Inze, D.4    Geelen, D.5
  • 66
    • 0036883456 scopus 로고    scopus 로고
    • Actin polymerization processes in plant cells
    • Vantard, M., and Blanchoin, L. (2002). Actin polymerization processes in plant cells. Curr. Opin. Plant Biol. 5, 502-506.
    • (2002) Curr. Opin. Plant Biol. , vol.5 , pp. 502-506
    • Vantard, M.1    Blanchoin, L.2
  • 67
    • 0035172425 scopus 로고    scopus 로고
    • Actin polymerization is essential for pollen tube growth
    • Vidali, L., McKenna, S.T., and Hepler, P.K. (2001). Actin polymerization is essential for pollen tube growth. Mol. Biol. Cell 12, 2534-2545.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2534-2545
    • Vidali, L.1    McKenna, S.T.2    Hepler, P.K.3
  • 68
    • 0042765607 scopus 로고    scopus 로고
    • Remodeling the cytoskeleton for growth and form: An overview with some new views
    • Wasteneys, G.O., and Galway, M.E. (2003). Remodeling the cytoskeleton for growth and form: An overview with some new views. Annu. Rev. Plant Biol. 54, 691-722.
    • (2003) Annu. Rev. Plant Biol. , vol.54 , pp. 691-722
    • Wasteneys, G.O.1    Galway, M.E.2
  • 69
    • 14744267175 scopus 로고    scopus 로고
    • New views on the plant cytoskeleton
    • Wasteneys, G.O., and Yang, Z. (2004). New views on the plant cytoskeleton. Plant Physiol. 136, 3884-3891.
    • (2004) Plant Physiol. , vol.136 , pp. 3884-3891
    • Wasteneys, G.O.1    Yang, Z.2
  • 70
    • 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., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B., and Narumiya, S. (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    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6    Saito, Y.7    Nakao, K.8    Jockusch, B.9    Narumiya, S.10
  • 71
    • 4043147895 scopus 로고    scopus 로고
    • Capping protein: New insights into mechanism and regulation
    • Wear, M.A., and Cooper, J.A. (2004). Capping protein: New insights into mechanism and regulation. Trends Biochem. Sci. 29, 418-428.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 418-428
    • Wear, M.A.1    Cooper, J.A.2
  • 72
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture
    • Xu, Y., Moseley, J.B., Sagot, I., Poy, F., Pellman, D., Goode, B.L., and Eck, M.J. (2004). Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723.
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 73
    • 0029159038 scopus 로고
    • Polymerization of actin from maize pollen
    • Yen, L.F., Liu, X., and Cai, S. (1995). Polymerization of actin from maize pollen. Plant Physiol. 107, 73-76.
    • (1995) Plant Physiol. , vol.107 , pp. 73-76
    • Yen, L.F.1    Liu, X.2    Cai, S.3


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