메뉴 건너뛰기




Volumn 22, Issue 8, 2010, Pages 2749-2767

Arabidopsis VILLIN5, an actin filament bundling and severing protein, is necessary for normal pollen tube growth

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; EUKARYOTA;

EID: 77957814647     PISSN: 10404651     EISSN: 1532298X     Source Type: Journal    
DOI: 10.1105/tpc.110.076257     Document Type: Article
Times cited : (131)

References (75)
  • 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
    • 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
  • 2
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin
    • Andrianantoandro, E., and Pollard, T.D. (2006). Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin. Mol. Cell 24: 13-23.
    • (2006) Mol. Cell , vol.24 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 3
    • 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
  • 4
    • 0344975376 scopus 로고
    • Villin: The major microfilamentassociated protein of the intestinal microvillus
    • Bretscher, A., and Weber, K. (1979). Villin: The major microfilamentassociated protein of the intestinal microvillus. Proc. Natl. Acad. Sci. USA 76: 2321-2325.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2321-2325
    • Bretscher, A.1    Weber, K.2
  • 5
    • 48549104131 scopus 로고    scopus 로고
    • Pollen tube growth oscillations and intracellular calcium levels are reversibly modulated by actin polymerization
    • Cardenas, L., Lovy-Wheeler, A., Kunkel, J.G., and Hepler, P.K. (2008). Pollen tube growth oscillations and intracellular calcium levels are reversibly modulated by actin polymerization. Plant Physiol. 146: 1611-1621.
    • (2008) Plant Physiol. , vol.146 , pp. 1611-1621
    • Cardenas, L.1    Lovy-Wheeler, A.2    Kunkel, J.G.3    Hepler, P.K.4
  • 6
    • 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
  • 7
    • 68449084443 scopus 로고    scopus 로고
    • Regulation of actin dynamics in pollen tubes: Control of actin polymer level
    • Chen, N., Qu, X., Wu, Y., and Huang, S. (2009). Regulation of actin dynamics in pollen tubes: Control of actin polymer level. J. Integr. Plant Biol. 51: 740-750.
    • (2009) J. Integr. Plant Biol. , vol.51 , pp. 740-750
    • Chen, N.1    Qu, X.2    Wu, Y.3    Huang, S.4
  • 8
    • 44949226058 scopus 로고    scopus 로고
    • Structural and signaling networks for the polar cell growth machinery in pollen tubes. Annu
    • Cheung, A.Y., and Wu, H.M. (2008). Structural and signaling networks for the polar cell growth machinery in pollen tubes. Annu. Rev. Plant Biol. 59: 547-572.
    • (2008) Rev. Plant Biol. , vol.59 , pp. 547-572
    • Cheung, A.Y.1    Wu, H.M.2
  • 9
    • 33749547214 scopus 로고    scopus 로고
    • Polarized growth: Maintaining focus on the tip
    • Cole, R.A., and Fowler, J.E. (2006). Polarized growth: Maintaining focus on the tip. Curr. Opin. Plant Biol. 9: 579-588.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 579-588
    • Cole, R.A.1    Fowler, J.E.2
  • 10
    • 0023427610 scopus 로고
    • Effects of cytochalasin and phalloidin on actin
    • Cooper, J.A. (1987). Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105: 1473-1478.
    • (1987) J. Cell Biol. , vol.105 , pp. 1473-1478
    • Cooper, J.A.1
  • 11
    • 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
  • 12
    • 0033598132 scopus 로고    scopus 로고
    • In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders
    • Ferrary, E., et al. (1999). In vivo, villin is required for Ca(2+)-dependent F-actin disruption in intestinal brush borders. J. Cell Biol. 146: 819-830.
    • (1999) J. Cell Biol. , vol.146 , pp. 819-830
    • Ferrary, E.1
  • 13
    • 0024317269 scopus 로고
    • Villin induces microvilli growth and actin redistribution in transfected fibroblasts
    • Friederich, E., Huet, C., Arpin, M., and Louvard, D. (1989). Villin induces microvilli growth and actin redistribution in transfected fibroblasts. Cell 59: 461-475.
    • (1989) Cell , vol.59 , pp. 461-475
    • Friederich, E.1    Huet, C.2    Arpin, M.3    Louvard, D.4
  • 14
    • 0025492527 scopus 로고
    • From the structure to the function of villin, an actin-binding protein of the brush border
    • Friederich, E., Pringault, E., Arpin, M., and Louvard, D. (1990). From the structure to the function of villin, an actin-binding protein of the brush border. Bioessays 12: 403-408.
    • (1990) Bioessays , vol.12 , pp. 403-408
    • Friederich, E.1    Pringault, E.2    Arpin, M.3    Louvard, D.4
  • 15
    • 0029913313 scopus 로고    scopus 로고
    • Inhibition of intracellular pectin transport in pollen tubes by monensin, brefeldin A and cytochalasin D
    • Geitmann, A., Wojciechowicz, K., and Cresti, M. (1996). Inhibition of intracellular pectin transport in pollen tubes by monensin, brefeldin A and cytochalasin D. Bot. Acta 109: 373-381.
    • (1996) Bot. Acta. , vol.109 , pp. 373-381
    • Geitmann, A.1    Wojciechowicz, K.2    Cresti, M.3
  • 16
    • 34548839356 scopus 로고    scopus 로고
    • Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders
    • George, S.P., Wang, Y., Mathew, S., Srinivasan, K., and Khurana, S. (2007). Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders. J. Biol. Chem. 282: 26528-26541.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26528-26541
    • George, S.P.1    Wang, Y.2    Mathew, S.3    Srinivasan, K.4    Khurana, S.5
  • 17
    • 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
  • 18
    • 0019450881 scopus 로고
    • F-actin assembly modulated by villin - Ca++-dependent nucleation and capping of the barbed end
    • Glenney, J.R., Kaulfus, P., and Weber, K. (1981). F-actin assembly modulated by villin - Ca++-dependent nucleation and capping of the barbed end. Cell 24: 471-480.
    • (1981) Cell , vol.24 , pp. 471-480
    • Glenney, J.R.1    Kaulfus, P.2    Weber, K.3
  • 20
    • 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
  • 21
    • 0026783523 scopus 로고
    • Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly
    • Hofmann, A., Eichinger, L., Andre, E., Rieger, D., and Schleicher, M. (1992). Cap100, a novel phosphatidylinositol 4,5-bisphosphate-regulated protein that caps actin filaments but does not nucleate actin assembly. Cell Motil. Cytoskeleton 23: 133-144.
    • (1992) Cell Motil. Cytoskeleton , vol.23 , pp. 133-144
    • Hofmann, A.1    Eichinger, L.2    Andre, E.3    Rieger, D.4    Schleicher, M.5
  • 22
    • 0031412197 scopus 로고    scopus 로고
    • Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed
    • Holdaway-Clarke, T.L., Feijo, J.A., Hackett, G.R., Kunkel, J.G., and Hepler, P.K. (1997). Pollen tube growth and the intracellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed. Plant Cell 9: 1999-2010.
    • (1997) Plant Cell , vol.9 , pp. 1999-2010
    • Holdaway-Clarke, T.L.1    Feijo, J.A.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 23
    • 0038120839 scopus 로고    scopus 로고
    • Comparative analysis of the Arabidopsis pollen transcriptome
    • Honys, D., and Twell, D. (2003). Comparative analysis of the Arabidopsis pollen transcriptome. Plant Physiol. 132: 640-652.
    • (2003) Plant Physiol. , vol.132 , pp. 640-652
    • Honys, D.1    Twell, D.2
  • 24
    • 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
  • 25
    • 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
  • 26
    • 33745359833 scopus 로고    scopus 로고
    • Heterodimeric capping protein from Arabidopsis is regulated by phosphatidic acid
    • Huang, S., Gao, L., Blanchoin, L., and Staiger, C.J. (2006). Heterodimeric capping protein from Arabidopsis is regulated by phosphatidic acid. Mol. Biol. Cell 17: 1946-1958.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1946-1958
    • Huang, S.1    Gao, L.2    Blanchoin, L.3    Staiger, C.J.4
  • 27
  • 28
    • 0342444416 scopus 로고
    • GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants
    • Jefferson, R.A., Kavanagh, T.A., and Bevan, M.W. (1987). GUS fusions: Beta-glucuronidase as a sensitive and versatile gene fusion marker in higher plants. EMBO J. 6: 3901-3907.
    • (1987) EMBO J , vol.6 , pp. 3901-3907
    • Jefferson, R.A.1    Kavanagh, T.A.2    Bevan, M.W.3
  • 29
    • 44449128840 scopus 로고    scopus 로고
    • Regulation of cell structure and function by actin-binding proteins: Villin's perspective
    • Khurana, S., and George, S.P. (2008). Regulation of cell structure and function by actin-binding proteins: Villin's perspective. FEBS Lett. 582: 2128-2139.
    • (2008) FEBS Lett. , vol.582 , pp. 2128-2139
    • Khurana, S.1    George, S.P.2
  • 30
    • 77957796109 scopus 로고    scopus 로고
    • Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities in actin bundle formation and turnover
    • Khurana, P., Henty, J.L., Huang, S., Staiger, A.M., Blanchoin, L., and Staiger, C.J. (2010). Arabidopsis VILLIN1 and VILLIN3 have overlapping and distinct activities in actin bundle formation and turnover. Plant Cell 22: 2727-2748.
    • (2010) Plant Cell , vol.22 , pp. 2727-2748
    • Khurana, P.1    Henty, J.L.2    Huang, S.3    Staiger, A.M.4    Blanchoin, L.5    Staiger, C.J.6
  • 31
    • 0033759043 scopus 로고    scopus 로고
    • Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis
    • Klahre, U., Friederich, E., Kost, B., Louvard, D., and Chua, N.H. (2000). Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis. Plant Physiol. 122: 35-48.
    • (2000) Plant Physiol. , vol.122 , pp. 35-48
    • Klahre, U.1    Friederich, E.2    Kost, B.3    Louvard, D.4    Chua, N.H.5
  • 32
    • 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. (2000). 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
  • 33
    • 56349141069 scopus 로고    scopus 로고
    • Tip growth: Signaling in the apical dome
    • Lee, Y.J., and Yang, Z. (2008). Tip growth: Signaling in the apical dome. Curr. Opin. Plant Biol. 11: 662-671.
    • (2008) Curr. Opin. Plant Biol. , vol.11 , pp. 662-671
    • Lee, Y.J.1    Yang, Z.2
  • 34
    • 18044372483 scopus 로고    scopus 로고
    • Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube
    • Lovy-Wheeler, A., Wilsen, K.L., Baskin, T.I., and Hepler, P.K. (2005). Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube. Planta 221: 95-104.
    • (2005) Planta , vol.221 , pp. 95-104
    • Lovy-Wheeler, A.1    Wilsen, K.L.2    Baskin, T.I.3    Hepler, P.K.4
  • 35
    • 0027931456 scopus 로고
    • The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis
    • Mahajan-Miklos, S., and Cooley, L. (1994). The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis. Cell 78: 291-301.
    • (1994) Cell , vol.78 , pp. 291-301
    • Mahajan-Miklos, S.1    Cooley, L.2
  • 36
    • 0031260156 scopus 로고    scopus 로고
    • Analysis of SCARECROW expression using a rapid system for assessing transgene expression in Arabidopsis roots
    • Malamy, J.E., and Benfey, P.N. (1997). Analysis of SCARECROW expression using a rapid system for assessing transgene expression in Arabidopsis roots. Plant J. 12: 957-963.
    • (1997) Plant J. , vol.12 , pp. 957-963
    • Malamy, J.E.1    Benfey, P.N.2
  • 37
    • 0033387744 scopus 로고    scopus 로고
    • Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells
    • Matova, N., Mahajan-Miklos, S., Mooseker, M.S., and Cooley, L. (1999). Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells. Development 126: 5645-5657.
    • (1999) Development , vol.126 , pp. 5645-5657
    • Matova, N.1    Mahajan-Miklos, S.2    Mooseker, M.S.3    Cooley, L.4
  • 38
    • 0018578513 scopus 로고
    • Identification and organization of the components in the isolated microvillus cytoskeleton
    • Matsudaira, P.T., and Burgess, D.R. (1979). Identification and organization of the components in the isolated microvillus cytoskeleton. J. Cell Biol. 83: 667-673.
    • (1979) J. Cell Biol. , vol.83 , pp. 667-673
    • Matsudaira, P.T.1    Burgess, D.R.2
  • 39
    • 0141761142 scopus 로고    scopus 로고
    • The gelsolin family of actin regulatory proteins: Modular structures, versatile functions
    • McGough, A.M., Staiger, C.J., Min, J.K., and Simonetti, K.D. (2003). The gelsolin family of actin regulatory proteins: Modular structures, versatile functions. FEBS Lett. 552: 75-81.
    • (2003) FEBS Lett. , vol.552 , pp. 75-81
    • McGough, A.M.1    Staiger, C.J.2    Min, J.K.3    Simonetti, K.D.4
  • 40
    • 0343183390 scopus 로고    scopus 로고
    • Periodic increases in elongation rate precede increases in cytosolic Ca2+ during pollen tube growth
    • Messerli, M.A., Creton, R., Jaffe, L.F., and Robinson, K.R. (2000). Periodic increases in elongation rate precede increases in cytosolic Ca2+ during pollen tube growth. Dev. Biol. 222: 84-98.
    • (2000) Dev. Biol. , vol.222 , pp. 84-98
    • Messerli, M.A.1    Creton, R.2    Jaffe, L.F.3    Robinson, K.R.4
  • 42
    • 27744591230 scopus 로고    scopus 로고
    • The formin homology 1 domain modulates the actin nucleation and bundling activity of Arabidopsis FORMIN1
    • Michelot, A., Guerin, 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    Guerin, C.2    Huang, S.3    Ingouff, M.4    Richard, S.5    Rodiuc, N.6    Staiger, C.J.7    Blanchoin, L.8
  • 43
    • 32144457693 scopus 로고    scopus 로고
    • Formin proteins: Purification and measurement of effects on actin assembly
    • Moseley, J.B., Maiti, S., and Goode, B.L. (2006). Formin proteins: Purification and measurement of effects on actin assembly. Methods Enzymol. 406: 215-234.
    • (2006) Methods Enzymol. , vol.406 , pp. 215-234
    • Moseley, J.B.1    Maiti, S.2    Goode, B.L.3
  • 44
    • 0032504617 scopus 로고    scopus 로고
    • Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily. Biochem
    • Nakayasu, T., Yokota, E., and Shimmen, T. (1998). Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily. Biochem. Biophys. Res. Commun. 249: 61-65.
    • (1998) Biophys. Res. Commun. , vol.249 , pp. 61-65
    • Nakayasu, T.1    Yokota, E.2    Shimmen, T.3
  • 45
    • 26944493068 scopus 로고    scopus 로고
    • Gene family analysis of the Arabidopsis pollen transcriptome reveals biological implications for cell growth, division control, and gene expression regulation
    • Pina, C., Pinto, F., Feijo, J.A., and Becker, J.D. (2005). Gene family analysis of the Arabidopsis pollen transcriptome reveals biological implications for cell growth, division control, and gene expression regulation. Plant Physiol. 138: 744-756.
    • (2005) Plant Physiol. , vol.138 , pp. 744-756
    • Pina, C.1    Pinto, F.2    Feijo, J.A.3    Becker, J.D.4
  • 46
    • 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
  • 47
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T.D., and Cooper, J.A. (2009). Actin, a central player in cell shape and movement. Science 326: 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 50
    • 0034634639 scopus 로고    scopus 로고
    • A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats
    • Safadi, F., Reddy, V.S., and Reddy, A.S. (2000). A pollen-specific novel calmodulin-binding protein with tetratricopeptide repeats. J. Biol. Chem. 275: 35457-35470.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35457-35470
    • Safadi, F.1    Reddy, V.S.2    Reddy, A.S.3
  • 51
    • 16644371716 scopus 로고    scopus 로고
    • A green fluorescent protein fusion to actin-binding domain 2 of Arabidopsis fimbrin highlights new features of a dynamic actin cytoskeleton in live plant cells
    • Sheahan, M.B., Staiger, C.J., Rose, R.J., and McCurdy, D.W. (2004). A green fluorescent protein fusion to actin-binding domain 2 of Arabidopsis fimbrin highlights new features of a dynamic actin cytoskeleton in live plant cells. Plant Physiol. 136: 3968-3978.
    • (2004) Plant Physiol. , vol.136 , pp. 3968-3978
    • Sheahan, M.B.1    Staiger, C.J.2    Rose, R.J.3    McCurdy, D.W.4
  • 53
    • 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
  • 54
    • 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
  • 55
    • 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
  • 57
    • 60849130414 scopus 로고    scopus 로고
    • Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array
    • Staiger, C.J., Sheahan, M.B., Khurana, P., Wang, X., McCurdy, D.W., and Blanchoin, L. (2009). Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array. J Cell Biol 184: 269-280.
    • (2009) J Cell Biol. , vol.184 , pp. 269-280
    • Staiger, C.J.1    Sheahan, M.B.2    Khurana, P.3    Wang, X.4    McCurdy, D.W.5    Blanchoin, L.6
  • 58
    • 34547883183 scopus 로고    scopus 로고
    • The villin/gelsolin/fragmin superfamily proteins in plants
    • Su, H., Wang, T., Dong, H., and Ren, H. (2007). The villin/gelsolin/fragmin superfamily proteins in plants. J Integr. Plant Biol. 49: 1183-1191.
    • (2007) J Integr. Plant Biol. , vol.49 , pp. 1183-1191
    • Su, H.1    Wang, T.2    Dong, H.3    Ren, H.4
  • 59
    • 33749252177 scopus 로고    scopus 로고
    • Tobacco WLIM1 is a novel F-actin binding protein involved in actin cytoskeleton remodeling
    • Thomas, C., Hoffmann, C., Dieterle, M., Van Troys, M., Ampe, C., and Steinmetz, A. (2006). Tobacco WLIM1 is a novel F-actin binding protein involved in actin cytoskeleton remodeling. Plant Cell 18: 2194-2206.
    • (2006) Plant Cell , vol.18 , pp. 2194-2206
    • Thomas, C.1    Hoffmann, C.2    Dieterle, M.3    van Troys, M.4    Ampe, C.5    Steinmetz, A.6
  • 62
    • 0034020244 scopus 로고    scopus 로고
    • The role of plant villin in the organization of the actin cytoskeleton, cytoplasmic streaming and the architecture of the transvacuolar strand in root hair cells of Hydrocharis
    • Tominaga, M., Yokota, E., Vidali, L., Sonobe, S., Hepler, P.K., and Shimmen, T. (2000). The role of plant villin in the organization of the actin cytoskeleton, cytoplasmic streaming and the architecture of the transvacuolar strand in root hair cells of Hydrocharis. Planta 210: 836-843.
    • (2000) Planta , vol.210 , pp. 836-843
    • Tominaga, M.1    Yokota, E.2    Vidali, L.3    Sonobe, S.4    Hepler, P.K.5    Shimmen, T.6
  • 63
    • 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
  • 64
    • 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
  • 65
    • 66749090381 scopus 로고    scopus 로고
    • Lifeact-mEGFP reveals a dynamic apical F-actin network in tip growing plant cells
    • Vidali, L., Rounds, C.M., Hepler, P.K., and Bezanilla, M. (2009). Lifeact-mEGFP reveals a dynamic apical F-actin network in tip growing plant cells. PLoS ONE 4: e5744.
    • (2009) PLoS ONE , vol.e5744 , pp. 4
    • Vidali, L.1    Rounds, C.M.2    Hepler, P.K.3    Bezanilla, M.4
  • 66
    • 0021701201 scopus 로고
    • Calcium dependence of villin-induced actin depolymerization
    • Walsh, T.P., Weber, A., Davis, K., Bonder, E., and Mooseker, M. (1984a). Calcium dependence of villin-induced actin depolymerization. Biochemistry 23: 6099-6102.
    • (1984) Biochemistry , vol.23 , pp. 6099-6102
    • Walsh, T.P.1    Weber, A.2    Davis, K.3    Bonder, E.4    Mooseker, M.5
  • 68
    • 53749092909 scopus 로고    scopus 로고
    • An actin-binding protein, LlLIM1, mediates calcium and hydrogen regulation of actin dynamics in pollen tubes
    • Wang, H.J., Wan, A.R., and Jauh, G.Y. (2008). An actin-binding protein, LlLIM1, mediates calcium and hydrogen regulation of actin dynamics in pollen tubes. Plant Physiol. 147: 1619-1636.
    • (2008) Plant Physiol. , vol.147 , pp. 1619-1636
    • Wang, H.J.1    Wan, A.R.2    Jauh, G.Y.3
  • 69
    • 34547658952 scopus 로고    scopus 로고
    • ACTIN BINDING PROTEIN 29 from Lilium pollen plays an important role in dynamic actin remodeling
    • Xiang, Y., Huang, X., Wang, T., Zhang, Y., Liu, Q., Hussey, P.J., and Ren, H. (2007). ACTIN BINDING PROTEIN 29 from Lilium pollen plays an important role in dynamic actin remodeling. Plant Cell 19: 1930-1946.
    • (2007) Plant Cell , vol.19 , pp. 1930-1946
    • Xiang, Y.1    Huang, X.2    Wang, T.3    Zhang, Y.4    Liu, Q.5    Hussey, P.J.6    Ren, H.7
  • 70
    • 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
  • 71
    • 0034047688 scopus 로고    scopus 로고
    • Calcium-calmodulin suppresses the filamentous actin-binding activity of a 135-kilodalton actin-bundling protein isolated from lily pollen tubes
    • Yokota, E., Muto, S., and Shimmen, T. (2000). Calcium-calmodulin suppresses the filamentous actin-binding activity of a 135-kilodalton actin-bundling protein isolated from lily pollen tubes. Plant Physiol. 123: 645-654.
    • (2000) Plant Physiol. , vol.123 , pp. 645-654
    • Yokota, E.1    Muto, S.2    Shimmen, T.3
  • 72
    • 0000806896 scopus 로고    scopus 로고
    • Actin-bundling protein isolated from pollen tubes of lily. Biochemical and immunocytochemical characterization
    • Yokota, E., and Shimmen, T. (1998). Actin-bundling protein isolated from pollen tubes of lily. Biochemical and immunocytochemical characterization. Plant Physiol. 116: 1421-1429.
    • (1998) Plant Physiol. , vol.116 , pp. 1421-1429
    • Yokota, E.1    Shimmen, T.2
  • 73
    • 27744528049 scopus 로고    scopus 로고
    • Plant villin, lily P-135-ABP, possesses G-actin binding activity and accelerates the polymerization and depolymerization of actin in a Ca2+-sensitive manner
    • Yokota, E., Tominaga, M., Mabuchi, I., Tsuji, Y., Staiger, C.J., Oiwa, K., and Shimmen, T. (2005). Plant villin, lily P-135-ABP, possesses G-actin binding activity and accelerates the polymerization and depolymerization of actin in a Ca2+-sensitive manner. Plant Cell Physiol. 46: 1690-1703.
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1690-1703
    • Yokota, E.1    Tominaga, M.2    Mabuchi, I.3    Tsuji, Y.4    Staiger, C.J.5    Oiwa, K.6    Shimmen, T.7
  • 74
    • 0242569607 scopus 로고    scopus 로고
    • Plant 115-kDa actinfilament bundling protein, P-115-ABP, is a homologue of plant villin and is widely distributed in cells
    • Yokota, E., Vidali, L., Tominaga, M., Tahara, H., Orii, H., Morizane, Y., Hepler, P.K., and Shimmen, T. (2003). Plant 115-kDa actinfilament bundling protein, P-115-ABP, is a homologue of plant villin and is widely distributed in cells. Plant Cell Physiol. 44: 1088-1099.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1088-1099
    • Yokota, E.1    Vidali, L.2    Tominaga, M.3    Tahara, H.4    Orii, H.5    Morizane, Y.6    Hepler, P.K.7    Shimmen, T.8
  • 75
    • 0035965218 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton
    • Zhai, L., Zhao, P., Panebra, A., Guerrerio, A.L., and Khurana, S. (2001). Tyrosine phosphorylation of villin regulates the organization of the actin cytoskeleton. J. Biol. Chem. 276: 36163-36167.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36163-36167
    • Zhai, L.1    Zhao, P.2    Panebra, A.3    Guerrerio, A.L.4    Khurana, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.