메뉴 건너뛰기




Volumn 23, Issue 2, 2011, Pages 661-680

BENT UPPERMOST INTERNODE1 Encodes the class II formin FH5 crucial for actin organization and rice development

Author keywords

[No Author keywords available]

Indexed keywords

ORYZA SATIVA;

EID: 79953076043     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.110.081802     Document Type: Article
Times cited : (89)

References (99)
  • 2
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • 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 98: 15009-15013.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 3
    • 0035282059 scopus 로고    scopus 로고
    • Latrunculin B-induced plant dwarfism: Plant cell elongation is F-actin-dependent
    • Baluska, F., Jasik, J., Edelmann, H.G., Salajová, T., and Volkmann, D. (2001). Latrunculin B-induced plant dwarfism: Plant cell elongation is F-actin-dependent. Dev. Biol. 231: 113-124.
    • (2001) Dev. Biol. , vol.231 , pp. 113-124
    • Baluska, F.1    Jasik, J.2    Edelmann, H.G.3    Salajová, T.4    Volkmann, D.5
  • 5
    • 18044379419 scopus 로고    scopus 로고
    • Actin nucleation: Spire-actin nucleator in a class of its own
    • Baum, B., and Kunda, P. (2005). Actin nucleation: Spire-actin nucleator in a class of its own. Curr. Biol. 15: R305-R308.
    • (2005) Curr. Biol. , vol.15
    • Baum, B.1    Kunda, P.2
  • 6
    • 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. (2000). 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
  • 7
    • 0035032507 scopus 로고    scopus 로고
    • A katanin-like protein regulates normal cell wall biosynthesis and cell elongation
    • Burk, D.H., Liu, B., Zhong, R., Morrison, W.H., and Ye, Z.H. (2001). A katanin-like protein regulates normal cell wall biosynthesis and cell elongation. Plant Cell 13: 807-827.
    • (2001) Plant Cell , vol.13 , pp. 807-827
    • Burk, D.H.1    Liu, B.2    Zhong, R.3    Morrison, W.H.4    Ye, Z.H.5
  • 8
    • 0345393105 scopus 로고    scopus 로고
    • Purification of brain tubulin through two cycles of polymerization-depolymerization in a highmolarity buffer
    • Castoldi, M., and Popov, A.V. (2003). Purification of brain tubulin through two cycles of polymerization-depolymerization in a highmolarity buffer. Protein Expr. Purif. 32: 83-88.
    • (2003) Protein Expr. Purif. , vol.32 , pp. 83-88
    • Castoldi, M.1    Popov, A.V.2
  • 9
    • 0027292636 scopus 로고
    • Identification and preliminary characterization of a 65 kDa higher-plant microtubule-associated protein
    • Chang-Jie, J., and Sonobe, S. (1993). Identification and preliminary characterization of a 65 kDa higher-plant microtubule-associated protein. J. Cell Sci. 105: 891-901.
    • (1993) J. Cell Sci. , vol.105 , pp. 891-901
    • Chang-Jie, J.1    Sonobe, S.2
  • 10
    • 34547803604 scopus 로고    scopus 로고
    • Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin
    • Chaudhry, F., Guérin, C., von Witsch, M., Blanchoin, L., and Staiger, C.J. (2007). Identification of Arabidopsis cyclase-associated protein 1 as the first nucleotide exchange factor for plant actin. Mol. Biol. Cell 18: 3002-3014.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3002-3014
    • Chaudhry, F.1    Guérin, C.2    von Witsch, M.3    Blanchoin, L.4    Staiger, C.J.5
  • 13
    • 77958003282 scopus 로고    scopus 로고
    • A transmembrane formin nucleates subapical actin assembly and controls tip-focused growth in pollen tubes
    • Cheung, A.Y., Niroomand, S., Zou, Y., and Wu, H.M. (2010). A transmembrane formin nucleates subapical actin assembly and controls tip-focused growth in pollen tubes. Proc. Natl. Acad. Sci. USA 107: 16390-16395.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16390-16395
    • Cheung, A.Y.1    Niroomand, S.2    Zou, Y.3    Wu, H.M.4
  • 14
    • 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
  • 15
    • 33645329105 scopus 로고    scopus 로고
    • Hypersensitivity to cytoskeletal antagonists demonstrates microtubule-microfilament cross-talk in the control of root elongation in Arabidopsis thaliana
    • Collings, D.A., Lill, A.W., Himmelspach, R., and Wasteneys, G.O. (2006). Hypersensitivity to cytoskeletal antagonists demonstrates microtubule-microfilament cross-talk in the control of root elongation in Arabidopsis thaliana. New Phytol. 170: 275-290.
    • (2006) New Phytol. , vol.170 , pp. 275-290
    • Collings, D.A.1    Lill, A.W.2    Himmelspach, R.3    Wasteneys, G.O.4
  • 16
    • 9444255105 scopus 로고    scopus 로고
    • Formin homology 2 domains occur in multiple contexts in angiosperms
    • Cvrcková, F., Novotný, M., Pícková, D., and Zárský, V. (2004). Formin homology 2 domains occur in multiple contexts in angiosperms. BMC Genomics 5: 44.
    • (2004) BMC Genomics , vol.5 , pp. 44
    • Cvrcková, F.1    Novotný, M.2    Pícková, D.3    Zárský, V.4
  • 17
    • 33645864068 scopus 로고    scopus 로고
    • Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression
    • Deeks, M.J., Cvrcková, F., Machesky, L.M., Mikitová, V., Ketelaar, T., Zársky, V., Davies, B., and Hussey, P.J. (2005). Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression. New Phytol. 168: 529-540.
    • (2005) New Phytol. , vol.168 , pp. 529-540
    • Deeks, M.J.1    Cvrcková, F.2    Machesky, L.M.3    Mikitová, V.4    Ketelaar, T.5    Zársky, V.6    Davies, B.7    Hussey, P.J.8
  • 18
    • 77951198791 scopus 로고    scopus 로고
    • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain
    • Deeks, M.J., Fendrych, M., Smertenko, A., Bell, K.S., Oparka, K., Cvrcková, F., Zársky, V., and Hussey, P.J. (2010). The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule-binding domain. J. Cell Sci. 123: 1209-1215.
    • (2010) J. Cell Sci. , vol.123 , pp. 1209-1215
    • Deeks, M.J.1    Fendrych, M.2    Smertenko, A.3    Bell, K.S.4    Oparka, K.5    Cvrcková, F.6    Zársky, V.7    Hussey, P.J.8
  • 19
    • 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
  • 21
    • 0034949515 scopus 로고    scopus 로고
    • ADF proteins are involved in the control of flowering and regulate F-actin organization, cell expansion, and organ growth in Arabidopsis
    • Dong, C.H., Xia, G.X., Hong, Y., Ramachandran, S., Kost, B., and Chua, N.H. (2001). ADF proteins are involved in the control of flowering and regulate F-actin organization, cell expansion, and organ growth in Arabidopsis. Plant Cell 13: 1333-1346.
    • (2001) Plant Cell , vol.13 , pp. 1333-1346
    • Dong, C.H.1    Xia, G.X.2    Hong, Y.3    Ramachandran, S.4    Kost, B.5    Chua, N.H.6
  • 23
    • 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
  • 24
    • 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
  • 25
    • 0037263483 scopus 로고    scopus 로고
    • Arabidopsis actin gene ACT7 plays an essential role in germination and root growth
    • Gilliland, L.U., Pawloski, L.C., Kandasamy, M.K., and Meagher, R.B. (2003). Arabidopsis actin gene ACT7 plays an essential role in germination and root growth. Plant J. 33: 319-328.
    • (2003) Plant J. , vol.33 , pp. 319-328
    • Gilliland, L.U.1    Pawloski, L.C.2    Kandasamy, M.K.3    Meagher, R.B.4
  • 26
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode, B.L., and Eck, M.J. (2007). Mechanism and function of formins in the control of actin assembly. Annu. Rev. Biochem. 76: 593-627.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 27
    • 44049099703 scopus 로고    scopus 로고
    • Roots of angiosperm formins: The evolutionary history of plant FH2 domain-containing proteins
    • Grunt, M., Zárský, V., and Cvrcková, F. (2008). Roots of angiosperm formins: The evolutionary history of plant FH2 domain-containing proteins. BMC Evol. Biol. 8: 115.
    • (2008) BMC Evol. Biol. , vol.8 , pp. 115
    • Grunt, M.1    Zárský, V.2    Cvrcková, F.3
  • 28
    • 67650079304 scopus 로고    scopus 로고
    • Arabidopsis cortical microtubules position cellulose synthase delivery to the plasma membrane and interact with cellulose synthase trafficking compartments
    • Gutierrez, R., Lindeboom, J.J., Paredez, A.R., Emons, A.M., and Ehrhardt, D.W. (2009). Arabidopsis cortical microtubules position cellulose synthase delivery to the plasma membrane and interact with cellulose synthase trafficking compartments. Nat. Cell Biol. 11: 797-806.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 797-806
    • Gutierrez, R.1    Lindeboom, J.J.2    Paredez, A.R.3    Emons, A.M.4    Ehrhardt, D.W.5
  • 29
    • 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
  • 30
    • 33646867122 scopus 로고    scopus 로고
    • Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2
    • Harris, E.S., Rouiller, I., Hanein, D., and Higgs, H.N. (2006). Mechanistic differences in actin bundling activity of two mammalian formins, FRL1 and mDia2. J. Biol. Chem. 281: 14383-14392.
    • (2006) J. Biol. Chem. , vol.281 , pp. 14383-14392
    • Harris, E.S.1    Rouiller, I.2    Hanein, D.3    Higgs, H.N.4
  • 32
    • 35648992928 scopus 로고    scopus 로고
    • Actin microfilament dynamics and actin side-binding proteins in plants
    • Higaki, T., Sano, T., and Hasezawa, S. (2007). Actin microfilament dynamics and actin side-binding proteins in plants. Curr. Opin. Plant Biol. 10: 549-556.
    • (2007) Curr. Opin. Plant Biol. , vol.10 , pp. 549-556
    • Higaki, T.1    Sano, T.2    Hasezawa, S.3
  • 33
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • Higgs, H.N., Blanchoin, L., and Pollard, T.D. (1999). Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the 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
  • 34
    • 0346398513 scopus 로고    scopus 로고
    • Roles of actin-depleted zone and preprophase band in determining the division site of higher-plant cells, a tobacco BY-2 cell line expressing GFP-tubulin
    • Hoshino, H., Yoneda, A., Kumagai, F., and Hasezawa, S. (2003). Roles of actin-depleted zone and preprophase band in determining the division site of higher-plant cells, a tobacco BY-2 cell line expressing GFP-tubulin. Protoplasma 222: 157-165.
    • (2003) Protoplasma , vol.222 , pp. 157-165
    • Hoshino, H.1    Yoneda, A.2    Kumagai, F.3    Hasezawa, S.4
  • 35
    • 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
  • 36
    • 34547138125 scopus 로고    scopus 로고
    • SB401, a pollen-specific protein from Solanum berthaultii, binds to and bundles microtubules and F-actin
    • Huang, S., Jin, L., Du, J., Li, H., Zhao, Q., Ou, G., Ao, G., and Yuan, M. (2007). SB401, a pollen-specific protein from Solanum berthaultii, binds to and bundles microtubules and F-actin. Plant J. 51: 406-418.
    • (2007) Plant J. , vol.51 , pp. 406-418
    • Huang, S.1    Jin, L.2    Du, J.3    Li, H.4    Zhao, Q.5    Ou, G.6    Ao, G.7    Yuan, M.8
  • 37
  • 38
    • 33745628866 scopus 로고    scopus 로고
    • Control of the actin cytoskeleton in plant cell growth
    • Hussey, P.J., Ketelaar, T., and Deeks, M.J. (2006). Control of the actin cytoskeleton in plant cell growth. Annu. Rev. Plant Biol. 57: 109-125.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 109-125
    • Hussey, P.J.1    Ketelaar, T.2    Deeks, M.J.3
  • 40
    • 34347226330 scopus 로고    scopus 로고
    • Helical microtubule arrays in a collection of twisting tubulin mutants of Arabidopsis thaliana
    • Ishida, T., Kaneko, Y., Iwano, M., and Hashimoto, T. (2007). Helical microtubule arrays in a collection of twisting tubulin mutants of Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 104: 8544-8549.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8544-8549
    • Ishida, T.1    Kaneko, Y.2    Iwano, M.3    Hashimoto, T.4
  • 41
    • 66449103502 scopus 로고    scopus 로고
    • A single vegetative actin isovariant overexpressed under the control of multiple regulatory sequences is sufficient for normal Arabidopsis development
    • Kandasamy, M.K., McKinney, E.C., and Meagher, R.B. (2009). A single vegetative actin isovariant overexpressed under the control of multiple regulatory sequences is sufficient for normal Arabidopsis development. Plant Cell 21: 701-718.
    • (2009) Plant Cell , vol.21 , pp. 701-718
    • Kandasamy, M.K.1    McKinney, E.C.2    Meagher, R.B.3
  • 43
    • 1142277951 scopus 로고    scopus 로고
    • The actin-interacting protein AIP1 is essential for actin organization and plant development
    • Ketelaar, T., Allwood, E.G., Anthony, R., Voigt, B., Menzel, D., and Hussey, P.J. (2004). The actin-interacting protein AIP1 is essential for actin organization and plant development. Curr. Biol. 14: 145-149.
    • (2004) Curr. Biol. , vol.14 , pp. 145-149
    • Ketelaar, T.1    Allwood, E.G.2    Anthony, R.3    Voigt, B.4    Menzel, D.5    Hussey, P.J.6
  • 44
    • 0037253769 scopus 로고    scopus 로고
    • Unstable F-actin specifies the area and microtubule direction of cell expansion in Arabidopsis root hairs
    • Ketelaar, T., de Ruijter, N.C., and Emons, A.M. (2003). Unstable F-actin specifies the area and microtubule direction of cell expansion in Arabidopsis root hairs. Plant Cell 15: 285-292.
    • (2003) Plant Cell , vol.15 , pp. 285-292
    • Ketelaar, T.1    de Ruijter, N.C.2    Emons, A.M.3
  • 45
    • 23644442920 scopus 로고    scopus 로고
    • Actin filaments play a critical role in vacuolar trafficking at the Golgi complex in plant cells
    • Kim, H., Park, M., Kim, S.J., and Hwang, I. (2005). Actin filaments play a critical role in vacuolar trafficking at the Golgi complex in plant cells. Plant Cell 17: 888-902.
    • (2005) Plant Cell , vol.17 , pp. 888-902
    • Kim, H.1    Park, M.2    Kim, S.J.3    Hwang, I.4
  • 46
    • 30344444895 scopus 로고    scopus 로고
    • Analysis of the rice mutant dwarf and gladius leaf 1. Aberrant kataninmediated microtubule organization causes up-regulation of gibberellin biosynthetic genes independently of gibberellin signaling
    • Komorisono, M., Ueguchi-Tanaka, M., Aichi, I., Hasegawa, Y., Ashikari, M., Kitano, H., Matsuoka, M., and Sazuka, T. (2005). Analysis of the rice mutant dwarf and gladius leaf 1. Aberrant kataninmediated microtubule organization causes up-regulation of gibberellin biosynthetic genes independently of gibberellin signaling. Plant Physiol. 138: 1982-1993.
    • (2005) Plant Physiol. , vol.138 , pp. 1982-1993
    • Komorisono, M.1    Ueguchi-Tanaka, M.2    Aichi, I.3    Hasegawa, Y.4    Ashikari, M.5    Kitano, H.6    Matsuoka, M.7    Sazuka, T.8
  • 47
    • 30844449003 scopus 로고    scopus 로고
    • Molecular details of formin-mediated actin assembly
    • Kovar, D.R. (2006). Molecular details of formin-mediated actin assembly. Curr. Opin. Cell Biol. 18: 11-17.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 11-17
    • Kovar, D.R.1
  • 48
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • Kovar, D.R., Harris, E.S., Mahaffy, R., Higgs, H.N., and Pollard, T.D. (2006). Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124: 423-435.
    • (2006) Cell , vol.124 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 49
    • 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
  • 50
    • 6944220067 scopus 로고    scopus 로고
    • Insertional assembly of actin filament barbed ends in association with formins produces piconewton forces
    • Kovar, D.R., and Pollard, T.D. (2004). 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. USA , vol.101 , pp. 14725-14730
    • Kovar, D.R.1    Pollard, T.D.2
  • 51
    • 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
  • 52
    • 77957781458 scopus 로고    scopus 로고
    • The type II Arabidopsis formin14 interacts with microtubules and microfilaments to regulate cell division
    • Li, Y., Shen, Y., Cai, C., Zhong, C., Zhu, L., Yuan, M., and Ren, H. (2010). The type II Arabidopsis formin14 interacts with microtubules and microfilaments to regulate cell division. Plant Cell 22: 2710-2726.
    • (2010) Plant Cell , vol.22 , pp. 2710-2726
    • Li, Y.1    Shen, Y.2    Cai, C.3    Zhong, C.4    Zhu, L.5    Yuan, M.6    Ren, H.7
  • 53
    • 0345871043 scopus 로고    scopus 로고
    • Microtubules and the shape of plants to come
    • Lloyd, C., and Chan, J. (2004). Microtubules and the shape of plants to come. Nat. Rev. Mol. Cell Biol. 5: 13-22.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 13-22
    • Lloyd, C.1    Chan, J.2
  • 54
    • 56349087880 scopus 로고    scopus 로고
    • The parallel lives of microtubules and cellulose microfibrils
    • Lloyd, C., and Chan, J. (2008). The parallel lives of microtubules and cellulose microfibrils. Curr. Opin. Plant Biol. 11: 641-646.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 641-646
    • Lloyd, C.1    Chan, J.2
  • 56
    • 9444265411 scopus 로고    scopus 로고
    • Cell shape development in plants
    • Mathur, J. (2004). Cell shape development in plants. Trends Plant Sci. 9: 583-590.
    • (2004) Trends Plant Sci. , vol.9 , pp. 583-590
    • Mathur, J.1
  • 57
    • 27744591230 scopus 로고    scopus 로고
    • The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1
    • Michelot, A., Guérin, C., Huang, S., Ingouff, M., Richard, S., Rodiuc, N., Staiger, C.J., and Blanchoin, L. (2005). The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1. Plant Cell 17: 2296-2313.
    • (2005) Plant Cell , vol.17 , pp. 2296-2313
    • Michelot, A.1    Guérin, C.2    Huang, S.3    Ingouff, M.4    Richard, S.5    Rodiuc, N.6    Staiger, C.J.7    Blanchoin, L.8
  • 58
    • 65549124105 scopus 로고    scopus 로고
    • mDia2 shuttles between the nucleus and the cytoplasm through the importin-a/b- and CRM1- mediated nuclear transport mechanism
    • Miki, T., Okawa, K., Sekimoto, T., Yoneda, Y., Watanabe, S., Ishizaki, T., and Narumiya, S. (2009). mDia2 shuttles between the nucleus and the cytoplasm through the importin-a/b- and CRM1- mediated nuclear transport mechanism. J. Biol. Chem. 284: 5753-5762.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5753-5762
    • Miki, T.1    Okawa, K.2    Sekimoto, T.3    Yoneda, Y.4    Watanabe, S.5    Ishizaki, T.6    Narumiya, S.7
  • 59
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • Moseley, J.B., and Goode, B.L. (2005). Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J. Biol. Chem. 280: 28023-28033.
    • (2005) J. Biol. Chem. , vol.280 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 60
    • 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
  • 61
    • 0034907213 scopus 로고    scopus 로고
    • mDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A.F., Cook, T.A., Alberts, A.S., and Gundersen, G.G. (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    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 62
    • 47249146894 scopus 로고    scopus 로고
    • Cortical actin filaments at the division site of mitotic plant cells: A reconsideration of the 'actin-depleted zone'
    • Panteris, E. (2008). Cortical actin filaments at the division site of mitotic plant cells: A reconsideration of the 'actin-depleted zone'. New Phytol. 179: 334-341.
    • (2008) New Phytol. , vol.179 , pp. 334-341
    • Panteris, E.1
  • 63
    • 33749555581 scopus 로고    scopus 로고
    • Microtubule cortical array organization and plant cell morphogenesis
    • Paradez, A., Wright, A., and Ehrhardt, D.W. (2006). Microtubule cortical array organization and plant cell morphogenesis. Curr. Opin. Plant Biol. 9: 571-578.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 571-578
    • Paradez, A.1    Wright, A.2    Ehrhardt, D.W.3
  • 64
    • 33745000523 scopus 로고    scopus 로고
    • Visualization of cellulose synthase demonstrates functional association with microtubules
    • Paredez, A.R., Somerville, C.R., and Ehrhardt, D.W. (2006). Visualization of cellulose synthase demonstrates functional association with microtubules. Science 312: 1491-1495.
    • (2006) Science , vol.312 , pp. 1491-1495
    • Paredez, A.R.1    Somerville, C.R.2    Ehrhardt, D.W.3
  • 65
    • 40149105917 scopus 로고    scopus 로고
    • The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation
    • Paul, A., and Pollard, T. (2008). The role of the FH1 domain and profilin in formin-mediated actin-filament elongation and nucleation. Curr. Biol. 18: 9-19.
    • (2008) Curr. Biol. , vol.18 , pp. 9-19
    • Paul, A.1    Pollard, T.2
  • 66
    • 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
  • 67
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D., and Borisy, G.G. (2003). Cellular motility driven by assembly and disassembly of actin filaments. Cell 112: 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 68
  • 69
    • 13444292982 scopus 로고    scopus 로고
    • Drosophila Spire is an actin nucleation factor
    • Quinlan, M.E., Heuser, J.E., Kerkhoff, E., and Mullins, R.D. (2005). Drosophila Spire is an actin nucleation factor. Nature 433: 382-388.
    • (2005) Nature , vol.433 , pp. 382-388
    • Quinlan, M.E.1    Heuser, J.E.2    Kerkhoff, E.3    Mullins, R.D.4
  • 73
    • 33644684966 scopus 로고    scopus 로고
    • Appearance of actin microfilament 'twin peaks' in mitosis and their function in cell plate formation, as visualized in tobacco BY-2 cells expressing GFP-fimbrin
    • Sano, T., Higaki, T., Oda, Y., Hayashi, T., and Hasezawa, S. (2005). Appearance of actin microfilament 'twin peaks' in mitosis and their function in cell plate formation, as visualized in tobacco BY-2 cells expressing GFP-fimbrin. Plant J. 44: 595-605.
    • (2005) Plant J. , vol.44 , pp. 595-605
    • Sano, T.1    Higaki, T.2    Oda, Y.3    Hayashi, T.4    Hasezawa, S.5
  • 75
    • 26844554009 scopus 로고    scopus 로고
    • Spatial control of cell expansion by the plant cytoskeleton
    • Smith, L.G., and Oppenheimer, D.G. (2005). Spatial control of cell expansion by the plant cytoskeleton. Annu. Rev. Cell Dev. Biol. 21: 271-295.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 271-295
    • Smith, L.G.1    Oppenheimer, D.G.2
  • 76
    • 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
  • 77
    • 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
  • 78
    • 33749860518 scopus 로고    scopus 로고
    • Actin dynamics: Old friends with new stories
    • Staiger, C.J., and Blanchoin, L. (2006). Actin dynamics: old friends with new stories. Curr. Opin. Plant Biol. 9: 554-562.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 554-562
    • Staiger, C.J.1    Blanchoin, L.2
  • 79
    • 0023368658 scopus 로고
    • An actin network is present in the cytoplasm throughout the cell cycle of carrot cells and associates with the dividing nucleus
    • Traas, J.A., Doonan, J.H., Rawlins, D.J., Shaw, P.J., Watts, J., and Lloyd, C.W. (1987). An actin network is present in the cytoplasm throughout the cell cycle of carrot cells and associates with the dividing nucleus. J. Cell Biol. 105: 387-395.
    • (1987) J. Cell Biol. , vol.105 , pp. 387-395
    • Traas, J.A.1    Doonan, J.H.2    Rawlins, D.J.3    Shaw, P.J.4    Watts, J.5    Lloyd, C.W.6
  • 80
    • 34648827390 scopus 로고    scopus 로고
    • Cortical division zone establishment in plant cells
    • Van Damme, D., Vanstraelen, M., and Geelen, D. (2007). Cortical division zone establishment in plant cells. Trends Plant Sci. 12: 458-464.
    • (2007) Trends Plant Sci. , vol.12 , pp. 458-464
    • van Damme, D.1    Vanstraelen, M.2    Geelen, D.3
  • 81
    • 0030909875 scopus 로고    scopus 로고
    • Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum
    • Vidali, L., and Hepler, P.K. (1997). Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum. Cell Motil. Cytoskeleton 36: 323-338.
    • (1997) Cell Motil. Cytoskeleton , vol.36 , pp. 323-338
    • Vidali, L.1    Hepler, P.K.2
  • 82
    • 37848999440 scopus 로고    scopus 로고
    • Profilin is essential for tip growth in the moss Physcomitrella patens
    • Vidali, L., Augustinea, R.C., Kleinmanb, K.P., and Bezanillaa, M. (2007). Profilin is essential for tip growth in the moss Physcomitrella patens. Plant Cell 19: 3705-3722.
    • (2007) Plant Cell , vol.19 , pp. 3705-3722
    • Vidali, L.1    Augustinea, R.C.2    Kleinmanb, K.P.3    Bezanillaa, M.4
  • 84
    • 27644435558 scopus 로고    scopus 로고
    • Functional characterization of Gossypium hirsutum profilin 1 gene (GhPFN1) in tobacco suspension cells. Characterization of in vivo functions of a cotton profilin gene
    • Wang, H.Y., Yu, Y., Chen, Z.L., and Xia, G.X. (2005). Functional characterization of Gossypium hirsutum profilin 1 gene (GhPFN1) in tobacco suspension cells. Characterization of in vivo functions of a cotton profilin gene. Planta 222: 594-603.
    • (2005) Planta , vol.222 , pp. 594-603
    • Wang, H.Y.1    Yu, Y.2    Chen, Z.L.3    Xia, G.X.4
  • 85
    • 18944390005 scopus 로고    scopus 로고
    • A practical vector for efficient knockdown of gene expression in rice (Oryza sativa L.)
    • Wang, M., Chen, C., Xu, Y.Y., Jiang, R.X., Han, Y., Xu, Z.H., and Chong, K. (2004). A practical vector for efficient knockdown of gene expression in rice (Oryza sativa L.). Plant Mol. Biol. Rep. 22: 409-417.
    • (2004) Plant Mol. Biol. Rep. , vol.22 , pp. 409-417
    • Wang, M.1    Chen, C.2    Xu, Y.Y.3    Jiang, R.X.4    Han, Y.5    Xu, Z.H.6    Chong, K.7
  • 86
    • 44949162989 scopus 로고    scopus 로고
    • Molecular basis of plant architecture
    • Wang, Y., and Li, J. (2008). Molecular basis of plant architecture. Annu. Rev. Plant Biol. 59: 253-279.
    • (2008) Annu. Rev. Plant Biol. , vol.59 , pp. 253-279
    • Wang, Y.1    Li, J.2
  • 87
    • 37349068518 scopus 로고    scopus 로고
    • Improved imaging of actin filaments in transgenic Arabidopsis plants expressing a green fluorescent protein fusion to the C- and N-termini of the fimbrin actinbinding domain 2
    • Wang, Y.S., Yoo, C.M., and Blancaflor, E.B. (2008). Improved imaging of actin filaments in transgenic Arabidopsis plants expressing a green fluorescent protein fusion to the C- and N-termini of the fimbrin actinbinding domain 2. New Phytol. 177: 525-536.
    • (2008) New Phytol. , vol.177 , pp. 525-536
    • Wang, Y.S.1    Yoo, C.M.2    Blancaflor, E.B.3
  • 88
    • 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
  • 89
    • 0025007616 scopus 로고
    • 'Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik, R.P., Maas, R.L., Zeller, R., Vogt, T.F., and Leder, P. (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    Maas, R.L.2    Zeller, R.3    Vogt, T.F.4    Leder, P.5
  • 90
    • 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
  • 91
    • 75649130777 scopus 로고    scopus 로고
    • Arabidopsis formin3 directs the formation of actin cables and polarized growth in pollen tubes
    • Ye, J., Zheng, Y., Yan, A., Chen, N., Wang, Z., Huang, S., and Yang, Z. (2009). Arabidopsis formin3 directs the formation of actin cables and polarized growth in pollen tubes. Plant Cell 21: 3868-3884.
    • (2009) Plant Cell , vol.21 , pp. 3868-3884
    • Ye, J.1    Zheng, Y.2    Yan, A.3    Chen, N.4    Wang, Z.5    Huang, S.6    Yang, Z.7
  • 92
    • 26944466154 scopus 로고    scopus 로고
    • Cloning and functional characterization of a formin-like protein (AtFH8) from Arabidopsis
    • Yi, K., Guo, C., Chen, D., Zhao, B., Yang, B., and Ren, H. (2005). Cloning and functional characterization of a formin-like protein (AtFH8) from Arabidopsis. Plant Physiol. 138: 1071-1082.
    • (2005) Plant Physiol. , vol.138 , pp. 1071-1082
    • Yi, K.1    Guo, C.2    Chen, D.3    Zhao, B.4    Yang, B.5    Ren, H.6
  • 94
  • 95
    • 79953121217 scopus 로고    scopus 로고
    • RICE MORPHOLOGY DETERMINANT encodes the type II formin FH5 and regulates rice morphogenesis
    • Zhang, Z., Zhang, Y., Tan, H., Wang, Y., Li, G., Liang, W., Yuan, Z., Hu, J., Ren, H., and Zhang, D. (2011). RICE MORPHOLOGY DETERMINANT encodes the type II formin FH5 and regulates rice morphogenesis. Plant Cell 23: 681-700.
    • (2011) Plant Cell , vol.23 , pp. 681-700
    • Zhang, Z.1    Zhang, Y.2    Tan, H.3    Wang, Y.4    Li, G.5    Liang, W.6    Yuan, Z.7    Hu, J.8    Ren, H.9    Zhang, D.10
  • 96
    • 26844526208 scopus 로고    scopus 로고
    • Mutation of SAC1, an Arabidopsis SAC domain phosphoinositide phosphatase, causes alterations in cell morphogenesis, cell wall synthesis, and actin organization
    • Zhong, R., Burk, D.H., Nairn, C.J., Wood-Jones, A., Morrison, W.H., III, and Ye, Z.H. (2005). Mutation of SAC1, an Arabidopsis SAC domain phosphoinositide phosphatase, causes alterations in cell morphogenesis, cell wall synthesis, and actin organization. Plant Cell 17: 1449-1466.
    • (2005) Plant Cell , vol.17 , pp. 1449-1466
    • Zhong, R.1    Burk, D.H.2    Nairn, C.J.3    Wood-Jones, A.4    Morrison III, W.H.5    Ye, Z.H.6
  • 97
    • 33645949148 scopus 로고    scopus 로고
    • ELONGATED UPPERMOST INTERNODE encodes a cytochrome P450 monooxygenase that epoxidizes gibberellins in a novel deactivation reaction in rice
    • Zhu, Y., et al. (2006). ELONGATED UPPERMOST INTERNODE encodes a cytochrome P450 monooxygenase that epoxidizes gibberellins in a novel deactivation reaction in rice. Plant Cell 18: 442-456.
    • (2006) Plant Cell , vol.18 , pp. 442-456
    • Zhu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.