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Volumn 14, Issue 10, 2002, Pages 2613-2626

Signal-mediated depolymerization of actin in pollen during the self-incompatibility response

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; ENZYME INHIBITION; GROWTH KINETICS; POLYMERIZATION;

EID: 0036801753     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.002998     Document Type: Article
Times cited : (155)

References (81)
  • 2
    • 0035876055 scopus 로고    scopus 로고
    • Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase
    • Allwood, E.G., Smertenko, A.P., and Hussey, P.J. (2001). Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase. FEBS Lett. 499, 97-100.
    • (2001) FEBS Lett. , vol.499 , pp. 97-100
    • Allwood, E.G.1    Smertenko, A.P.2    Hussey, P.J.3
  • 3
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative
    • Arabidopsis Genome Initiative. (2000). Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408, 796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 4
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg, J.R. (1999). Proteins of the ADF/cofilin family: Essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185-230.
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 5
    • 0032925035 scopus 로고    scopus 로고
    • Reorganization of filamentous actin and myosin-II in zebrafish eggs correlates temporally and spatially with cortical granule exocytosis
    • Becker, K.A., and Hart, N.H. (1999). Reorganization of filamentous actin and myosin-II in zebrafish eggs correlates temporally and spatially with cortical granule exocytosis. J. Cell Sci. 112, 97-110.
    • (1999) J. Cell Sci. , vol.112 , pp. 97-110
    • Becker, K.A.1    Hart, N.H.2
  • 6
    • 0000149716 scopus 로고    scopus 로고
    • Rearrangement of actin microfilaments in plant root hairs responding to Rhizobium etli nodulation signals
    • Cárdenas, L., Vidali, L., Domínguez, J., Pérez, H., Sánchez, F., Hepler, P.K., and Quinto, C. (1998). Rearrangement of actin microfilaments in plant root hairs responding to Rhizobium etli nodulation signals. Plant Physiol. 116, 871-877.
    • (1998) Plant Physiol. , vol.116 , pp. 871-877
    • Cárdenas, L.1    Vidali, L.2    Domínguez, J.3    Pérez, H.4    Sánchez, F.5    Hepler, P.K.6    Quinto, C.7
  • 7
    • 0018574775 scopus 로고
    • Reorganization of actin in platelets stimulated by thrombin as measured by DNase I inhibition assay
    • Carlsson, L., Markey, F., Blikstad, I., Persson, T., and Lindberg, U. (1979). Reorganization of actin in platelets stimulated by thrombin as measured by DNase I inhibition assay. Proc. Natl. Acad. Sci. USA 76, 6376-6380.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6376-6380
    • Carlsson, L.1    Markey, F.2    Blikstad, I.3    Persson, T.4    Lindberg, U.5
  • 8
    • 0032100337 scopus 로고    scopus 로고
    • A potential signaling role for profilin in pollen of Papaver rhoeas
    • Clarke, S.R., Staiger, C.J., Gibbon, B.C., and Franklin-Tong, V.E. (1998). A potential signaling role for profilin in pollen of Papaver rhoeas. Plant Cell 10, 967-980.
    • (1998) Plant Cell , vol.10 , pp. 967-980
    • Clarke, S.R.1    Staiger, C.J.2    Gibbon, B.C.3    Franklin-Tong, V.E.4
  • 9
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper, J.A., and Schafer, D.A. (2000). Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell Biol. 12, 97-103.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 10
    • 0032497567 scopus 로고    scopus 로고
    • Caspases and programmed cell death in the hypersensitive response of plants to pathogens
    • del Pozo, O., and Lam, E. (1998). Caspases and programmed cell death in the hypersensitive response of plants to pathogens. Curr. Biol. 8, 1129-1132.
    • (1998) Curr. Biol. , vol.8 , pp. 1129-1132
    • Del Pozo, O.1    Lam, E.2
  • 11
    • 0032772496 scopus 로고    scopus 로고
    • Rhizobium Nod factors induce an increase in sub-apical fine bundles of actin filaments in Vicia sativa root hairs within minutes
    • de Ruijter, N.C.A., Bisseling, T., and Emons, A.M.C. (1999). Rhizobium Nod factors induce an increase in sub-apical fine bundles of actin filaments in Vicia sativa root hairs within minutes. Mol. Plant-Microbe Interact. 12, 829-832.
    • (1999) Mol. Plant-Microbe Interact. , vol.12 , pp. 829-832
    • De Ruijter, N.C.A.1    Bisseling, T.2    Emons, A.M.C.3
  • 12
    • 0025965365 scopus 로고
    • Vasopressin depolymerizes F-actin in toad bladder epithelial cells
    • Ding, G., Franki, N., Condeelis, J., and Hays, R.M. (1991). Vasopressin depolymerizes F-actin in toad bladder epithelial cells. Am. J. Physiol. 260, C9-C16.
    • (1991) Am. J. Physiol. , vol.260
    • Ding, G.1    Franki, N.2    Condeelis, J.3    Hays, R.M.4
  • 13
    • 0026527780 scopus 로고
    • Phorbol ester-induced actin assembly in neutrophils: Role of protein kinase C
    • Downey, G.P., Chan, C.K., Lea, P., Takai, A., and Grinstein, S. (1992). Phorbol ester-induced actin assembly in neutrophils: Role of protein kinase C. J. Cell Biol. 116, 695-706.
    • (1992) J. Cell Biol. , vol.116 , pp. 695-706
    • Downey, G.P.1    Chan, C.K.2    Lea, P.3    Takai, A.4    Grinstein, S.5
  • 14
    • 0032534468 scopus 로고    scopus 로고
    • Activation of cysteine proteases in cowpea plants during the hypersensitive response: A form of programmed cell death
    • D'Silva, I., Poirer, G.G., and Heath, M.C. (1998). Activation of cysteine proteases in cowpea plants during the hypersensitive response: A form of programmed cell death. Exp. Cell Res. 245, 389-399.
    • (1998) Exp. Cell Res. , vol.245 , pp. 389-399
    • D'Silva, I.1    Poirer, G.G.2    Heath, M.C.3
  • 15
    • 0028588657 scopus 로고
    • Cloning and characterization of a maize pollen-specific calcium-dependent calmodulin-independent protein kinase
    • Estruch, J.J., Kadwell, S., Merlin, E., and Crossland, L. (1994). Cloning and characterization of a maize pollen-specific calcium-dependent calmodulin-independent protein kinase. Proc. Natl. Acad. Sci. USA 91, 8837-8841.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8837-8841
    • Estruch, J.J.1    Kadwell, S.2    Merlin, E.3    Crossland, L.4
  • 16
    • 0031403892 scopus 로고    scopus 로고
    • Actin filaments of guard cells are reorganized in response to light and abscisic acid
    • Eun, S.-O., and Lee, Y. (1997). Actin filaments of guard cells are reorganized in response to light and abscisic acid. Plant Physiol. 115, 1491-1498.
    • (1997) Plant Physiol. , vol.115 , pp. 1491-1498
    • Eun, S.-O.1    Lee, Y.2
  • 18
    • 0029832826 scopus 로고    scopus 로고
    • Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate
    • Franklin-Tong, V.E., Drøbak, B.K., Allan, A.C., Watkins, P.A.C., and Trewavas, A.J. (1996). Growth of pollen tubes of Papaver rhoeas is regulated by a slow-moving calcium wave propagated by inositol 1,4,5-trisphosphate. Plant Cell 8, 1305-1321.
    • (1996) Plant Cell , vol.8 , pp. 1305-1321
    • Franklin-Tong, V.E.1    Drøbak, B.K.2    Allan, A.C.3    Watkins, P.A.C.4    Trewavas, A.J.5
  • 19
    • 0031436401 scopus 로고    scopus 로고
    • i in the self-incompatibility response in pollen tubes of Papaver rhoeas
    • i in the self-incompatibility response in pollen tubes of Papaver rhoeas. Plant J. 12, 1375-1386.
    • (1997) Plant J. , vol.12 , pp. 1375-1386
    • Franklin-Tong, V.E.1    Hackett, G.2    Hepler, P.K.3
  • 20
    • 0036008582 scopus 로고    scopus 로고
    • Involvement of extracellular calcium influx in the self-incompatibility response of Papaver rhoeas
    • Franklin-Tong, V.E., Holdaway-Clarke, T.L., Straatman, K.R., Kunkel, J.G., and Hepler, P.K. (2002). Involvement of extracellular calcium influx in the self-incompatibility response of Papaver rhoeas. Plant J. 29, 333-345.
    • (2002) Plant J. , vol.29 , pp. 333-345
    • Franklin-Tong, V.E.1    Holdaway-Clarke, T.L.2    Straatman, K.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 22
    • 0000351423 scopus 로고
    • The self-incompatibility response in Papaver rhoeas is mediated by cytosolic free calcium
    • Franklin-Tong, V.E., Ride, J.P., Read, N.D., Trewavas, A.J., and Franklin, F.C.H. (1993). The self-incompatibility response in Papaver rhoeas is mediated by cytosolic free calcium. Plant J. 4, 163-177.
    • (1993) Plant J. , vol.4 , pp. 163-177
    • Franklin-Tong, V.E.1    Ride, J.P.2    Read, N.D.3    Trewavas, A.J.4    Franklin, F.C.H.5
  • 23
    • 0035809915 scopus 로고    scopus 로고
    • Rop GTPase-dependent dynamics of tip-localized F-actin controls tip growth in pollen tubes
    • Fu, Y., Wu, G., and Yang, Z. (2001). Rop GTPase-dependent dynamics of tip-localized F-actin controls tip growth in pollen tubes. J. Cell Biol. 152, 1019-1032.
    • (2001) J. Cell Biol. , vol.152 , pp. 1019-1032
    • Fu, Y.1    Wu, G.2    Yang, Z.3
  • 24
    • 0035543399 scopus 로고    scopus 로고
    • Rop GTPase: A master switch of cell polarity development in plants
    • Fu, Y., and Yang, Z. (2001). Rop GTPase: A master switch of cell polarity development in plants. Trends Plant Sci. 6, 545-547.
    • (2001) Trends Plant Sci. , vol.6 , pp. 545-547
    • Fu, Y.1    Yang, Z.2
  • 25
    • 0034095607 scopus 로고    scopus 로고
    • The cytoskeleton in plant and fungal cell tip growth
    • Geitmann, A., and Emons, A.M.C. (2000). The cytoskeleton in plant and fungal cell tip growth. J. Microsc. 198, 218-245.
    • (2000) J. Microsc. , vol.198 , pp. 218-245
    • Geitmann, A.1    Emons, A.M.C.2
  • 26
    • 0033898396 scopus 로고    scopus 로고
    • Alterations in the actin cytoskeleton of pollen tubes are induced by the self-incompatibility reaction in Papaver rhoeas
    • Geitmann, A., Snowman, B.N., Emons, A.M.C., and Franklin-Tong, V.E. (2000). Alterations in the actin cytoskeleton of pollen tubes are induced by the self-incompatibility reaction in Papaver rhoeas. Plant Cell 12, 1239-1251.
    • (2000) Plant Cell , vol.12 , pp. 1239-1251
    • Geitmann, A.1    Snowman, B.N.2    Emons, A.M.C.3    Franklin-Tong, V.E.4
  • 27
    • 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
  • 28
    • 0002464281 scopus 로고    scopus 로고
    • Profilin
    • C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Gibbon, B.C., and Staiger, C.J. (2000). Profilin. In Actin: A Dynamic Framework for Multiple Plant Cell Functions, C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 45-65.
    • (2000) Actin: A Dynamic Framework for Multiple Plant Cell Functions , pp. 45-65
    • Gibbon, B.C.1    Staiger, C.J.2
  • 29
    • 0025820447 scopus 로고
    • Ca(2+)-independent F-actin assembly and disassembly during Fc receptor-mediated phagocytosis in mouse macrophages
    • Greenberg, S., el Khoury, J., di Virgilio, F., Kaplan, E.M., and Silverstein, S.C. (1991). Ca(2+)-independent F-actin assembly and disassembly during Fc receptor-mediated phagocytosis in mouse macrophages. J. Cell Biol. 113, 757-767.
    • (1991) J. Cell Biol. , vol.113 , pp. 757-767
    • Greenberg, S.1    El Khoury, J.2    Di Virgilio, F.3    Kaplan, E.M.4    Silverstein, S.C.5
  • 31
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998). Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 32
    • 0024044667 scopus 로고
    • Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells
    • Hall, A.L., Schlein, A., and Condeelis, J. (1988). Relationship of pseudopod extension to chemotactic hormone-induced actin polymerization in amoeboid cells. J. Cell. Biochem. 37, 285-299.
    • (1988) J. Cell. Biochem. , vol.37 , pp. 285-299
    • Hall, A.L.1    Schlein, A.2    Condeelis, J.3
  • 34
    • 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., Feijó, 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    Feijó, J.A.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 35
    • 0022181812 scopus 로고
    • The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils
    • Howard, T.H., and Oresajo, C.O. (1985a). The kinetics of chemotactic peptide-induced change in F-actin content, F-actin distribution, and the shape of neutrophils. J. Cell Biol. 101, 1078-1085.
    • (1985) J. Cell Biol. , vol.101 , pp. 1078-1085
    • Howard, T.H.1    Oresajo, C.O.2
  • 36
    • 0022293456 scopus 로고
    • A method for quantifying F-actin in chemotactic peptide activated neutrophils: Study of the effect of tBOC peptide
    • Howard, T.H., and Oresajo, C.O. (1985b). A method for quantifying F-actin in chemotactic peptide activated neutrophils: Study of the effect of tBOC peptide. Cell Motil. 5, 545-557.
    • (1985) Cell Motil. , vol.5 , pp. 545-557
    • Howard, T.H.1    Oresajo, C.O.2
  • 37
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey, P.A. (1998). The cytoskeleton and cell signaling: Component localization and mechanical coupling. Physiol. Rev. 78, 763-781.
    • (1998) Physiol. Rev. , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 38
    • 0033845632 scopus 로고    scopus 로고
    • Evidence for DNA fragmentation triggered in the self-incompatibility response in pollen of Papaver rhoeas
    • Jordan, N.D., Franklin, F.C.H., and Franklin-Tong, V.E. (2000). Evidence for DNA fragmentation triggered in the self-incompatibility response in pollen of Papaver rhoeas. Plant J. 23, 471-479.
    • (2000) Plant J. , vol.23 , pp. 471-479
    • Jordan, N.D.1    Franklin, F.C.H.2    Franklin-Tong, V.E.3
  • 39
    • 0032695844 scopus 로고    scopus 로고
    • Profilin is predominantly associated with monomeric actin in Acanthamoeba
    • Kaiser, D.A., Vinson, V.K., Murphy, D.B., and Pollard, T.D. (1999). Profilin is predominantly associated with monomeric actin in Acanthamoeba. J. Cell Sci. 112, 3779-3790.
    • (1999) J. Cell Sci. , vol.112 , pp. 3779-3790
    • Kaiser, D.A.1    Vinson, V.K.2    Murphy, D.B.3    Pollard, T.D.4
  • 40
    • 0032192020 scopus 로고    scopus 로고
    • Identification of residues in a hydrophilic loop of the Papaver rhoeas S protein that play a crucial role in recognition of incompatible pollen
    • Kakeda, K., Jordan, N.D., Conner, A., Ride, J.P., Franklin-Tong, V.E., and Franklin, F.C.H. (1998). Identification of residues in a hydrophilic loop of the Papaver rhoeas S protein that play a crucial role in recognition of incompatible pollen. Plant Cell 10, 1723-1731.
    • (1998) Plant Cell , vol.10 , pp. 1723-1731
    • Kakeda, K.1    Jordan, N.D.2    Conner, A.3    Ride, J.P.4    Franklin-Tong, V.E.5    Franklin, F.C.H.6
  • 41
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang, F., Purich, D.L., and Southwick, F.S. (1999). Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J. Biol. Chem. 274, 36963-36972.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36963-36972
    • Kang, F.1    Purich, D.L.2    Southwick, F.S.3
  • 42
    • 0029883916 scopus 로고    scopus 로고
    • Plant profilins rescue the aberrant phenotype of profilin-deficient Dictyostelium cells
    • Karakesisoglou, I., Schleicher, M., Gibbon, B.C., and Staiger, C.J. (1996). Plant profilins rescue the aberrant phenotype of profilin-deficient Dictyostelium cells. Cell Motil. Cytoskeleton 34, 36-47.
    • (1996) Cell Motil. Cytoskeleton , vol.34 , pp. 36-47
    • Karakesisoglou, I.1    Schleicher, M.2    Gibbon, B.C.3    Staiger, C.J.4
  • 43
    • 0029591856 scopus 로고
    • Actin filaments in yeast are unstable in the absence of capping protein or fimbrin
    • Karpova, T.S., Tatchell, K., and Cooper, J.A. (1995). Actin filaments in yeast are unstable in the absence of capping protein or fimbrin. J. Cell Biol. 131, 1483-1493.
    • (1995) J. Cell Biol. , vol.131 , pp. 1483-1493
    • Karpova, T.S.1    Tatchell, K.2    Cooper, J.A.3
  • 44
    • 0030993416 scopus 로고    scopus 로고
    • Dynamic reorganization of microfilaments and microtubules is necessary for the expression of non-host resistance in barley coleoptile cells
    • Kobayashi, Y., Kobayashi, I., Funaki, Y., Fujimoto, S., Takemoto, T., and Kunoh, H. (1997). Dynamic reorganization of microfilaments and microtubules is necessary for the expression of non-host resistance in barley coleoptile cells. Plant J. 11, 525-537.
    • (1997) Plant J. , vol.11 , pp. 525-537
    • Kobayashi, Y.1    Kobayashi, I.2    Funaki, Y.3    Fujimoto, S.4    Takemoto, T.5    Kunoh, H.6
  • 45
    • 0001110303 scopus 로고
    • 2+-induced fragmentation of actin filaments in pollen tubes
    • 2+-induced fragmentation of actin filaments in pollen tubes. Protoplasma 141, 177-179.
    • (1987) Protoplasma , vol.141 , pp. 177-179
    • Kohno, T.1    Shimmen, T.2
  • 46
    • 0001231453 scopus 로고
    • 2+ inhibition of cytoplasmic streaming in lily pollen tubes
    • 2+ inhibition of cytoplasmic streaming in lily pollen tubes. J. Cell Sci. 91, 501-509.
    • (1988) J. Cell Sci. , vol.91 , pp. 501-509
    • Kohno, T.1    Shimmen, T.2
  • 47
    • 0032810759 scopus 로고    scopus 로고
    • F-actin as a functional target for retro-retinoids: A possible role in anhydroretinol-triggered cell death
    • Korichneva, I., and Hämmerling, U. (1999). F-actin as a functional target for retro-retinoids: A possible role in anhydroretinol-triggered cell death. J. Cell Sci. 112, 2521-2528.
    • (1999) J. Cell Sci. , vol.112 , pp. 2521-2528
    • Korichneva, I.1    Hämmerling, U.2
  • 48
    • 0034674763 scopus 로고    scopus 로고
    • The presence and subcellular localization of caspase 3-like proteinases in plant cells
    • Korthout, H.A.A.J., Berecki, G., Bruin, W., van Duijn, B., and Wang, M. (2000). The presence and subcellular localization of caspase 3-like proteinases in plant cells. FEBS Lett. 475, 139-144.
    • (2000) FEBS Lett. , vol.475 , pp. 139-144
    • Korthout, H.A.A.J.1    Berecki, G.2    Bruin, W.3    Van Duijn, B.4    Wang, M.5
  • 49
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • Kovar, D.R., Drøbak, 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    Drøbak, B.K.2    Staiger, C.J.3
  • 50
    • 0002155413 scopus 로고    scopus 로고
    • Actin depolymerizing factor
    • C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Kovar, D.R., and Staiger, C.J. (2000). Actin depolymerizing factor. In Actin: A Dynamic Framework for Multiple Plant Cell Functions, C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 67-85.
    • (2000) Actin: A Dynamic Framework for Multiple Plant Cell Functions , pp. 67-85
    • Kovar, D.R.1    Staiger, C.J.2
  • 51
    • 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
  • 53
    • 0031735777 scopus 로고    scopus 로고
    • Identification and cloning of related self-incompatibility S-genes in Papaver rhoeas and Papaver nudicaule
    • Kurup, S., Ride, J.P., Jordan, N., Fletcher, G., Franklin-Tong, V.E., and Franklin, F.C.H. (1998). Identification and cloning of related self-incompatibility S-genes in Papaver rhoeas and Papaver nudicaule. Sex. Plant Reprod. 11, 192-198.
    • (1998) Sex. Plant Reprod. , vol.11 , pp. 192-198
    • Kurup, S.1    Ride, J.P.2    Jordan, N.3    Fletcher, G.4    Franklin-Tong, V.E.5    Franklin, F.C.H.6
  • 54
    • 84966189072 scopus 로고
    • The genetical control of self-incompatibility in Papaver rhoeas L.
    • Lawrence, M.J., Afzal, M., and Kenrick, J. (1978). The genetical control of self-incompatibility in Papaver rhoeas L. Heredity 40, 239-285.
    • (1978) Heredity , vol.40 , pp. 239-285
    • Lawrence, M.J.1    Afzal, M.2    Kenrick, J.3
  • 55
    • 0030465874 scopus 로고    scopus 로고
    • Actin polymerization and depolymerization during apoptosis in HL-60 cells
    • Levee, M.G., Dabrowska, M.I., Lelli, J.L.J., and Hinshaw, D.B. (1996). Actin polymerization and depolymerization during apoptosis in HL-60 cells. Am. J. Physiol. 271, C1981-C1992.
    • (1996) Am. J. Physiol. , vol.271
    • Levee, M.G.1    Dabrowska, M.I.2    Lelli, J.L.J.3    Hinshaw, D.B.4
  • 56
    • 0028352176 scopus 로고
    • Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae
    • Lillie, S.H., and Brown, S.S. (1994). Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae. J. Cell Biol. 125, 825-842.
    • (1994) J. Cell Biol. , vol.125 , pp. 825-842
    • Lillie, S.H.1    Brown, S.S.2
  • 57
    • 0035052515 scopus 로고    scopus 로고
    • Actin and actin-binding proteins in higher plants
    • McCurdy, D.W., Kovar, D.R., and Staiger, C.J. (2001). Actin and actin-binding proteins in higher plants. Protoplasma 215, 89-104.
    • (2001) Protoplasma , vol.215 , pp. 89-104
    • McCurdy, D.W.1    Kovar, D.R.2    Staiger, C.J.3
  • 58
    • 0030918142 scopus 로고    scopus 로고
    • 2+ pulses are coincident with peak pulsatile growth rates in pollen tubes of Lilium longiflorum
    • 2+ pulses are coincident with peak pulsatile growth rates in pollen tubes of Lilium longiflorum. J. Cell Sci. 110, 1269-1278.
    • (1997) J. Cell Sci. , vol.110 , pp. 1269-1278
    • Messerli, M.1    Robinson, K.R.2
  • 60
    • 0033034611 scopus 로고    scopus 로고
    • The role of actin in root hair morphogenesis: Studies with lipochito-oligosaccharide as a growth stimulator and cytochalasin as an actin perturbing drug
    • Miller, D.D., de Ruijter, N.C.A., Bisseling, T., and Emons, A.M.C. (1999). The role of actin in root hair morphogenesis: Studies with lipochito-oligosaccharide as a growth stimulator and cytochalasin as an actin perturbing drug. Plant J. 17, 141-154.
    • (1999) Plant J. , vol.17 , pp. 141-154
    • Miller, D.D.1    De Ruijter, N.C.A.2    Bisseling, T.3    Emons, A.M.C.4
  • 61
    • 0035964259 scopus 로고    scopus 로고
    • cAMP acts as a second messenger in pollen tube growth and reorientation
    • Moutinho, A., Hussey, P.J., Trewavas, A.J., and Malhó, R. (2001). cAMP acts as a second messenger in pollen tube growth and reorientation. Proc. Natl. Acad. Sci. USA 98, 10481-10486.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 10481-10486
    • Moutinho, A.1    Hussey, P.J.2    Trewavas, A.J.3    Malhó, R.4
  • 62
    • 0032953989 scopus 로고    scopus 로고
    • Signals, motors, morphogenesis: The cytoskeleton in plant development
    • Nick, P. (1999). Signals, motors, morphogenesis: The cytoskeleton in plant development. Plant Biol. 1, 169-179.
    • (1999) Plant Biol. , vol.1 , pp. 169-179
    • Nick, P.1
  • 64
    • 0008727013 scopus 로고    scopus 로고
    • Alterations of the actin polymerization status as an apoptotic morphological effector in HL-60 cells
    • Rao, J.Y., Jin, Y.S., Zheng, Q.L., Cheng, J., Tai, J., and Hemstreet, G.P.I. (1999). Alterations of the actin polymerization status as an apoptotic morphological effector in HL-60 cells. J. Cell. Biochem. 75, 686-697.
    • (1999) J. Cell. Biochem. , vol.75 , pp. 686-697
    • Rao, J.Y.1    Jin, Y.S.2    Zheng, Q.L.3    Cheng, J.4    Tai, J.5    Hemstreet, G.P.I.6
  • 66
    • 0035654415 scopus 로고    scopus 로고
    • Caspase inhibitors reduce symptom development and limit bacterial proliferation in susceptible plant tissues
    • Richael, C., Lincoln, J.E., Bostock, R.M., and Gilchrist, D.G. (2001). Caspase inhibitors reduce symptom development and limit bacterial proliferation in susceptible plant tissues. Physiol. Mol. Plant Pathol. 59, 213-221.
    • (2001) Physiol. Mol. Plant Pathol. , vol.59 , pp. 213-221
    • Richael, C.1    Lincoln, J.E.2    Bostock, R.M.3    Gilchrist, D.G.4
  • 67
    • 12544260753 scopus 로고    scopus 로고
    • 2+-independent phosphorylation of a 68 kDa pollen protein is stimulated by the self-incompatibility response in Papaver rhoeas
    • 2+-independent phosphorylation of a 68 kDa pollen protein is stimulated by the self-incompatibility response in Papaver rhoeas. Plant J. 12, 507-514.
    • (1997) Plant J. , vol.12 , pp. 507-514
    • Rudd, J.J.1    Franklin, F.C.H.2    Franklin-Tong, V.E.3
  • 68
    • 0000435259 scopus 로고    scopus 로고
    • Increased phosphorylation of a 26-kD pollen protein is induced by the self-incompatibility response in Papaver rhoeas
    • Rudd, J.J., Franklin, F.C.H., Lord, J.M., and Franklin-Tong, V.E. (1996). Increased phosphorylation of a 26-kD pollen protein is induced by the self-incompatibility response in Papaver rhoeas. Plant Cell 8, 713-724.
    • (1996) Plant Cell , vol.8 , pp. 713-724
    • Rudd, J.J.1    Franklin, F.C.H.2    Lord, J.M.3    Franklin-Tong, V.E.4
  • 69
    • 2142788716 scopus 로고    scopus 로고
    • Signals and targets of the self-incompatibility response in pollen of Papaver rhoeas
    • in press
    • Rudd, J.J., and Franklin-Tong, V.E. (2002). Signals and targets of the self-incompatibility response in pollen of Papaver rhoeas. J. Exp. Bot., in press.
    • (2002) J. Exp. Bot.
    • Rudd, J.J.1    Franklin-Tong, V.E.2
  • 70
    • 0031888137 scopus 로고    scopus 로고
    • Rapid and efficient purification of actin from nonmuscle sources
    • Schafer, D.A., Jennings, P.B., and Cooper, J.A. (1998). Rapid and efficient purification of actin from nonmuscle sources. Cell Motil. Cytoskeleton 39, 166-171.
    • (1998) Cell Motil. Cytoskeleton , vol.39 , pp. 166-171
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 72
  • 73
    • 0032053115 scopus 로고    scopus 로고
    • Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity
    • Smertenko, A.P., Jiang, C.-J., Simmons, N.J., Weeds, A.G., Davies, D.R., and Hussey, P.J. (1998). Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity. Plant J. 14, 187-194.
    • (1998) Plant J. , vol.14 , pp. 187-194
    • Smertenko, A.P.1    Jiang, C.-J.2    Simmons, N.J.3    Weeds, A.G.4    Davies, D.R.5    Hussey, P.J.6
  • 76
    • 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
  • 77
    • 0035047583 scopus 로고    scopus 로고
    • Actin and pollen tube growth
    • Vidali, L., and Hepler, P.K. (2001). Actin and pollen tube growth. Protoplasma 215, 64-76.
    • (2001) Protoplasma , vol.215 , pp. 64-76
    • Vidali, L.1    Hepler, P.K.2
  • 78
    • 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
  • 79
    • 0030566833 scopus 로고    scopus 로고
    • Profilin is required for the normal timing of actin polymenzation in response to thermal stress
    • Yeh, J., and Haarer, B.K. (1996). Profilin is required for the normal timing of actin polymenzation in response to thermal stress. FEBS Lett. 398, 303-307.
    • (1996) FEBS Lett. , vol.398 , pp. 303-307
    • Yeh, J.1    Haarer, B.K.2
  • 80
    • 0034047688 scopus 로고    scopus 로고
    • Calcium-calmodulin suppresses the filamentous actin-binding activity of 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 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
  • 81
    • 0002417240 scopus 로고    scopus 로고
    • Characterization of native actin-binding proteins from pollen: Myosin and the actin-bundling proteins, 135-ABP and 115-ABP
    • C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers)
    • Yokota, E., and Shimmen, T. (2000). Characterization of native actin-binding proteins from pollen: Myosin and the actin-bundling proteins, 135-ABP and 115-ABP. In Actin: A Dynamic Framework for Multiple Plant Cell Functions, C.J. Staiger, F. Baluska, D. Volkmann, and P. Barlow, eds (Dordrecht, The Netherlands: Kluwer Academic Publishers), pp. 103-118.
    • (2000) Actin: A Dynamic Framework for Multiple Plant Cell Functions , pp. 103-118
    • Yokota, E.1    Shimmen, T.2


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