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Volumn 123, Issue 2, 2000, Pages 645-654

Calcium-calmodulin suppresses the filamentous actin-binding activity of a 135-kilodalton actin-bundling protein isolated from lily pollen tubes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BUNDLING PROTEIN; ACTIN FILAMENT; BINDING KINETICS; CALCIUM; CALMODULIN; POLLEN TUBE; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; REACTION MECHANISM;

EID: 0034047688     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.123.2.645     Document Type: Article
Times cited : (71)

References (67)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 2
    • 0018869290 scopus 로고
    • Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner
    • Bretscher A, Weber K (1980) Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner. Cell 20: 839-847
    • (1980) Cell , vol.20 , pp. 839-847
    • Bretscher, A.1    Weber, K.2
  • 3
    • 0000425655 scopus 로고
    • Subcellular localization of actin depolymerizing factor in mature and germinating pollen
    • Chung Y-Y, Magnuson NS, An G (1995) Subcellular localization of actin depolymerizing factor in mature and germinating pollen. Mol Cell 5: 224-229
    • (1995) Mol Cell , vol.5 , pp. 224-229
    • Chung, Y.-Y.1    Magnuson, N.S.2    An, G.3
  • 4
    • 0025992588 scopus 로고
    • Calcium/calmodulin affects microtubule stability in lysed protoplasts
    • Cyr RJ (1991) Calcium/calmodulin affects microtubule stability in lysed protoplasts. J Cell Sci 100: 311-317
    • (1991) J Cell Sci , vol.100 , pp. 311-317
    • Cyr, R.J.1
  • 5
    • 0028445306 scopus 로고
    • A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α
    • Durso NA, Cyr RJ (1994) A calmodulin-sensitive interaction between microtubules and a higher plant homolog of elongation factor-1α. Plant Cell 6: 893-905
    • (1994) Plant Cell , vol.6 , pp. 893-905
    • Durso, N.A.1    Cyr, R.J.2
  • 6
    • 0027132676 scopus 로고
    • Calcium levels affect the ability to immunolocalize calmodulin to cortical microtubules
    • Fisher DD, Cyr RJ (1993) Calcium levels affect the ability to immunolocalize calmodulin to cortical microtubules. Plant Physiol 103: 543-551
    • (1993) Plant Physiol , vol.103 , pp. 543-551
    • Fisher, D.D.1    Cyr, R.J.2
  • 7
    • 0029728952 scopus 로고    scopus 로고
    • Evidence for opposing effects of calmodulin on cortical microtubules
    • Fisher DD, Gilroy S, Cyr RJ (1996) Evidence for opposing effects of calmodulin on cortical microtubules. Plant Physiol 112: 1079-1087
    • (1996) Plant Physiol , vol.112 , pp. 1079-1087
    • Fisher, D.D.1    Gilroy, S.2    Cyr, R.J.3
  • 8
    • 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, 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
  • 10
    • 0019780969 scopus 로고
    • F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments
    • Glenney JR Jr, Kaulfus P, Matsudaira P, Weber K (1981) F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. J Biol Chem 256: 9283-9288
    • (1981) J Biol Chem , vol.256 , pp. 9283-9288
    • Glenney J.R., Jr.1    Kaulfus, P.2    Matsudaira, P.3    Weber, K.4
  • 11
    • 0002929571 scopus 로고
    • Calmodulin in tip-growing plant cells, visualized by fluorescing calmodulin-binding phenothiazines
    • Hauβer I, Herth W, Reiss H-D (1984) Calmodulin in tip-growing plant cells, visualized by fluorescing calmodulin-binding phenothiazines. Planta 162: 33-39
    • (1984) Planta , vol.162 , pp. 33-39
    • Hauer, I.1    Herth, W.2    Reiss, H.-D.3
  • 12
    • 0018906488 scopus 로고
    • Calcium-regulated modulator protein interacting agents inhibits smooth muscle calcium-stimulated protein kinase and ATPase
    • Hidaka H, Yamaki T, Naka M, Tanaka T, Hayashi H, Kabayashi R (1980) Calcium-regulated modulator protein interacting agents inhibits smooth muscle calcium-stimulated protein kinase and ATPase. Mol Pharmacol 17: 66-72
    • (1980) Mol Pharmacol , vol.17 , pp. 66-72
    • Hidaka, H.1    Yamaki, T.2    Naka, M.3    Tanaka, T.4    Hayashi, H.5    Kabayashi, R.6
  • 13
    • 0031412197 scopus 로고    scopus 로고
    • Pollen tube growth and the intra-cellular cytosolic calcium gradient oscillate in phase while extracellular calcium influx is delayed
    • Holdaway-Clarke TL, Feijó JA, Hackett GR, Kunkel JG, Hepler PK (1997) Pollen tube growth and the intra-cellular 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
  • 14
    • 0030138167 scopus 로고    scopus 로고
    • The Arabidopsis profilin gene family: Evidence for an ancient split between constitutive and pollen-specific profilin genes
    • Huang S, McDowell JM, Weise MJ, Meagher RB (1996) The Arabidopsis profilin gene family: evidence for an ancient split between constitutive and pollen-specific profilin genes. Plant Physiol 111: 115-126
    • (1996) Plant Physiol , vol.111 , pp. 115-126
    • Huang, S.1    McDowell, J.M.2    Weise, M.J.3    Meagher, R.B.4
  • 15
    • 0027353586 scopus 로고
    • Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor
    • Kim S-R, Kim Y, An G (1993) Molecular cloning and characterization of anther-preferential cDNA encoding a putative actin-depolymerizing factor. Plant Mol Biol 21: 39-45
    • (1993) Plant Mol Biol , vol.21 , pp. 39-45
    • Kim, S.-R.1    Kim, Y.2    An, G.3
  • 16
    • 0002533445 scopus 로고
    • 2+ and target proteins
    • P Cohen, CB Klee, eds, Elsevier Biomedical Press, Amsterdam
    • 2+ and target proteins. In P Cohen, CB Klee, eds, Calmodulin: Molecular Aspects of Cellular Regulation, Vol. 5. Elsevier Biomedical Press, Amsterdam, pp 35-56
    • (1988) Calmodulin: Molecular Aspects of Cellular Regulation , vol.5 , pp. 35-56
    • Klee, C.B.1
  • 17
    • 0019507459 scopus 로고
    • Amino acid incorporation rates into myofibrillar proteins of dystrophic chicken skeletal muscle
    • Kohama K (1981) Amino acid incorporation rates into myofibrillar proteins of dystrophic chicken skeletal muscle. J Biochem 90: 497-501
    • (1981) J Biochem , vol.90 , pp. 497-501
    • Kohama, K.1
  • 18
    • 0003014883 scopus 로고
    • Pollen tube extract supports the movement of actin filaments in vitro
    • Kohno T, Okagaki T, Kohama K, Shimmen T (1991) Pollen tube extract supports the movement of actin filaments in vitro. Protoplasma 161: 75-77
    • (1991) Protoplasma , vol.161 , pp. 75-77
    • Kohno, T.1    Okagaki, T.2    Kohama, K.3    Shimmen, T.4
  • 19
    • 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
  • 21
    • 0025354085 scopus 로고
    • Detection of extracellular calcium gradients with a calcium-specific vibrating electrode
    • Kühtreiber WM, Jaffe LF (1990) Detection of extracellular calcium gradients with a calcium-specific vibrating electrode. J Cell Biol 110: 1565-1573
    • (1990) J Cell Biol , vol.110 , pp. 1565-1573
    • Kühtreiber, W.M.1    Jaffe, L.F.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0001221640 scopus 로고
    • Ultrastructure of the cytoskeleton in freeze-substituted pollen tubes of Nicotiana alata
    • Lancelle SA, Cresti M, Hepler PK (1987) Ultrastructure of the cytoskeleton in freeze-substituted pollen tubes of Nicotiana alata. Protoplasma 140: 141-150
    • (1987) Protoplasma , vol.140 , pp. 141-150
    • Lancelle, S.A.1    Cresti, M.2    Hepler, P.K.3
  • 24
    • 0031042995 scopus 로고    scopus 로고
    • Growth inhibition and recovery in freeze-substituted lilium longiflorum pollen tubes: Structural effects of caffeine
    • Lancelle SA, Cresti M, Hepler PK (1997) Growth inhibition and recovery in freeze-substituted Lilium longiflorum pollen tubes: structural effects of caffeine. Protoplasma 196: 21-33
    • (1997) Protoplasma , vol.196 , pp. 21-33
    • Lancelle, S.A.1    Cresti, M.2    Hepler, P.K.3
  • 25
    • 0000882190 scopus 로고
    • Ultrastructure of freeze-substituted pollen tubes of Lilium longiflorum
    • Lancelle SA, Hepler PK (1992) Ultrastructure of freeze-substituted pollen tubes of Lilium longiflorum. Protoplasma 167: 215-230
    • (1992) Protoplasma , vol.167 , pp. 215-230
    • Lancelle, S.A.1    Hepler, P.K.2
  • 26
    • 0030760444 scopus 로고    scopus 로고
    • Functional interactions among cytoskeleton, membranes, and cell wall in the pollen tube of flowering plants
    • Li Y-Q, Moscatelli A, Cai G, Cresti M (1997) Functional interactions among cytoskeleton, membranes, and cell wall in the pollen tube of flowering plants. Int Rev Cytol 176: 133-199
    • (1997) Int Rev Cytol , vol.176 , pp. 133-199
    • Li, Y.-Q.1    Moscatelli, A.2    Cai, G.3    Cresti, M.4
  • 27
    • 0028221820 scopus 로고
    • Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney
    • Lin C-S, Shen W, Chen ZP, Tu Y-H, Matsudaira P (1994) Identification of I-plastin, a human fimbrin isoform expressed in intestine and kidney. Mol Cell Biol 14: 2457-2467
    • (1994) Mol Cell Biol , vol.14 , pp. 2457-2467
    • Lin, C.-S.1    Shen, W.2    Chen, Z.P.3    Tu, Y.-H.4    Matsudaira, P.5
  • 29
    • 0027947783 scopus 로고
    • Role of cytosolic free calcium in the reorientation of pollen tube growth
    • Malhó R, Read ND, Pais MS, Trewavas AJ (1994) Role of cytosolic free calcium in the reorientation of pollen tube growth. Plant J 5: 331-341
    • (1994) Plant J , vol.5 , pp. 331-341
    • Malhó, R.1    Read, N.D.2    Pais, M.S.3    Trewavas, A.J.4
  • 30
    • 0028812280 scopus 로고
    • Calcium channel activity during pollen tube growth and reorientation
    • Malhó R, Read ND, Trewavas AJ, Pais MS (1995) Calcium channel activity during pollen tube growth and reorientation. Plant Cell 7: 1173-1184
    • (1995) Plant Cell , vol.7 , pp. 1173-1184
    • Malhó, R.1    Read, N.D.2    Trewavas, A.J.3    Pais, M.S.4
  • 31
    • 0030449665 scopus 로고    scopus 로고
    • Localized apical increases of cytosolic free calcium control pollen tube orientation
    • Malhó R, Trewavas AJ (1996) Localized apical increases of cytosolic free calcium control pollen tube orientation. Plant Cell 8: 1935-1949
    • (1996) Plant Cell , vol.8 , pp. 1935-1949
    • Malhó, R.1    Trewavas, A.J.2
  • 32
    • 0027138345 scopus 로고
    • Molecular mechanisms of pollen tube growth and differentiation
    • Mascarenhas JP (1993) Molecular mechanisms of pollen tube growth and differentiation. Plant Cell 5: 1303-1314
    • (1993) Plant Cell , vol.5 , pp. 1303-1314
    • Mascarenhas, J.P.1
  • 33
    • 0023707173 scopus 로고
    • Pieces in the actin-severing protein puzzle
    • Matsudaira P, Janmey P (1988) Pieces in the actin-severing protein puzzle. Cell 54: 139-140
    • (1988) Cell , vol.54 , pp. 139-140
    • Matsudaira, P.1    Janmey, P.2
  • 34
    • 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
  • 36
    • 0030464443 scopus 로고    scopus 로고
    • Actin microfilaments do not form a dense meshwork in Lilium longiflorum pollen tube tips
    • Miller DD, Lancelle SA, Hepler PK (1996) Actin microfilaments do not form a dense meshwork in Lilium longiflorum pollen tube tips. Protoplasma 195: 123-132
    • (1996) Protoplasma , vol.195 , pp. 123-132
    • Miller, D.D.1    Lancelle, S.A.2    Hepler, P.K.3
  • 37
    • 0029152581 scopus 로고
    • Molecular cloning and characterization of profilin from tobacco (Nicotiana tabacum): Increased profilin expression during pollen maturation
    • Mittermann I, Swoboda I, Pierson E, Eller N, Kraft D, Valenta R, Heberle-Bors E (1995) Molecular cloning and characterization of profilin from tobacco (Nicotiana tabacum): increased profilin expression during pollen maturation. Plant Mol Biol 27: 137-146
    • (1995) Plant Mol Biol , vol.27 , pp. 137-146
    • Mittermann, I.1    Swoboda, I.2    Pierson, E.3    Eller, N.4    Kraft, D.5    Valenta, R.6    Heberle-Bors, E.7
  • 38
    • 0032219588 scopus 로고    scopus 로고
    • Elongation factor-1α stabilizes microtubules in a calcium/calmodulin-dependent manner
    • Moore RC, Durso NA, Cyr RJ (1998) Elongation factor-1α stabilizes microtubules in a calcium/calmodulin-dependent manner. Cell Motil Cytoskelet 41: 168-180
    • (1998) Cell Motil Cytoskelet , vol.41 , pp. 168-180
    • Moore, R.C.1    Durso, N.A.2    Cyr, R.J.3
  • 39
    • 0019257347 scopus 로고
    • Regulation of microvillus structure: Calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells
    • Mooseker MS, Graves TA, Wharton KA, Falco N, Howe CL (1980) Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells. J Cell Biol 87: 809-822
    • (1980) J Cell Biol , vol.87 , pp. 809-822
    • Mooseker, M.S.1    Graves, T.A.2    Wharton, K.A.3    Falco, N.4    Howe, C.L.5
  • 40
    • 0031855556 scopus 로고    scopus 로고
    • Distribution of calmodulin protein and mRNA in growing pollen tubes
    • Moutinho A, Love J, Trewavas AJ, Malhó R (1998) Distribution of calmodulin protein and mRNA in growing pollen tubes. Sex Plant Reprod 11: 131-139
    • (1998) Sex Plant Reprod , vol.11 , pp. 131-139
    • Moutinho, A.1    Love, J.2    Trewavas, A.J.3    Malhó, R.4
  • 41
    • 0032504617 scopus 로고    scopus 로고
    • Purification of an actin-binding protein composed of 115-kDa polypeptide from pollen tubes of lily
    • Nakayasu T, Yokota E, 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) Biochem Biophys Res Commun , vol.249 , pp. 61-65
    • Nakayasu, T.1    Yokota, E.2    Shimmen, T.3
  • 42
    • 0026468443 scopus 로고
    • Human T cell L-plastin bundles actin filaments in a calcium-dependent manner
    • Namba Y, Ito M, Zu Y, Shigesada K, Maruyama K (1992) Human T cell L-plastin bundles actin filaments in a calcium-dependent manner. J Biochem 112: 503-507
    • (1992) J Biochem , vol.112 , pp. 503-507
    • Namba, Y.1    Ito, M.2    Zu, Y.3    Shigesada, K.4    Maruyama, K.5
  • 43
    • 0032100916 scopus 로고    scopus 로고
    • Characterization of microtubule binding domain in the Arabidopsis kinesin-like calmodulin binding protein
    • Narasimhulu SB, Reddy ASN (1998) Characterization of microtubule binding domain in the Arabidopsis kinesin-like calmodulin binding protein. Plant Cell 10: 957-965
    • (1998) Plant Cell , vol.10 , pp. 957-965
    • Narasimhulu, S.B.1    Reddy, A.S.N.2
  • 44
    • 0028140561 scopus 로고
    • Actin-bundling proteins
    • Otto JJ (1994) Actin-bundling proteins. Curr Opin Cell Biol 6: 105-109
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 105-109
    • Otto, J.J.1
  • 45
    • 0027048869 scopus 로고
    • Cytoskeleton and cytoplasmic organization of pollen and pollen tubes
    • Pierson ES, Cresti M (1992) Cytoskeleton and cytoplasmic organization of pollen and pollen tubes. Int Rev Cytol 140: 73-125
    • (1992) Int Rev Cytol , vol.140 , pp. 73-125
    • Pierson, E.S.1    Cresti, M.2
  • 46
    • 0028675663 scopus 로고
    • Pollen tube growth is coupled to the extracellular calcium ion flux and the intracellular calcium gradient: Effect of BAPTA-type buffers and hypertonic media
    • Pierson ES, Miller DD, Callaham DA, Shipley AM, Rivers BA, Cresti M, Hepler PK (1994) Pollen tube growth is coupled to the extracellular calcium ion flux and the intracellular calcium gradient: effect of BAPTA-type buffers and hypertonic media. Plant Cell 6: 1815-1828
    • (1994) Plant Cell , vol.6 , pp. 1815-1828
    • Pierson, E.S.1    Miller, D.D.2    Callaham, D.A.3    Shipley, A.M.4    Rivers, B.A.5    Cresti, M.6    Hepler, P.K.7
  • 48
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins: A critical evaluation of mechanisms and functions
    • Pollard TD, Cooper JA (1986) Actin and actin-binding proteins: a critical evaluation of mechanisms and functions. Annu Rev Biochem 55: 987-1035
    • (1986) Annu Rev Biochem , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 49
    • 0030790823 scopus 로고    scopus 로고
    • Interaction of a dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes
    • Prassler J, Stocker S, Marriott G, Heidecker M, Kellermann J, Gerisch G (1997) Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes. Mol Biol Cell 8: 83-95
    • (1997) Mol Biol Cell , vol.8 , pp. 83-95
    • Prassler, J.1    Stocker, S.2    Marriott, G.3    Heidecker, M.4    Kellermann, J.5    Gerisch, G.6
  • 51
    • 0029966327 scopus 로고    scopus 로고
    • A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain
    • Reddy ASN, Safadi F, Narasimhulu SB, Golovkin M, Hu X (1996) A novel plant calmodulin-binding protein with a kinesin heavy chain motor domain. J Biol Chem 271: 7052-7060
    • (1996) J Biol Chem , vol.271 , pp. 7052-7060
    • Reddy, A.S.N.1    Safadi, F.2    Narasimhulu, S.B.3    Golovkin, M.4    Hu, X.5
  • 52
    • 0000665321 scopus 로고    scopus 로고
    • Modulation of calmodulin mRNA and protein levels in barley aleurone
    • Schuurink RC, Chan PV, Jones RL (1996) Modulation of calmodulin mRNA and protein levels in barley aleurone. Plant Physiol 111: 371-380
    • (1996) Plant Physiol , vol.111 , pp. 371-380
    • Schuurink, R.C.1    Chan, P.V.2    Jones, R.L.3
  • 53
    • 0031022621 scopus 로고    scopus 로고
    • In vitro motility of AtKCBP, a calmodulin-binding kinesin protein of Arabidopsis
    • Song H, Golovkin M, Reddy ASN, Endow SA (1997) In vitro motility of AtKCBP, a calmodulin-binding kinesin protein of Arabidopsis. Proc Natl Acad Sci USA 94: 322-327
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 322-327
    • Song, H.1    Golovkin, M.2    Reddy, A.S.N.3    Endow, S.A.4
  • 55
    • 0020000902 scopus 로고
    • 2+-calmodulin complex with calmodulin antagonists naphthalenesulfonamide derivatives
    • 2+-calmodulin complex with calmodulin antagonists naphthalenesulfonamide derivatives. Mol Pharmacol 22: 403-407
    • (1982) Mol Pharmacol , vol.22 , pp. 403-407
    • Tanaka, T.1    Ohmura, T.2    Hidaka, H.3
  • 57
    • 0028370023 scopus 로고
    • Confocal image analysis of spatial variations in immunocytochemically identified calmodulin during pollen hydration, germination and pollen tube tip growth in Nicotiana tabacum L
    • Tirlapur UK, Scali M, Moscatelli A, Casino CD, Cai G, Tiezzi A, Cresti M (1994) Confocal image analysis of spatial variations in immunocytochemically identified calmodulin during pollen hydration, germination and pollen tube tip growth in Nicotiana tabacum L. Zygote 2: 63-68
    • (1994) Zygote , vol.2 , pp. 63-68
    • Tirlapur, U.K.1    Scali, M.2    Moscatelli, A.3    Casino, C.D.4    Cai, G.5    Tiezzi, A.6    Cresti, M.7
  • 58
    • 0002611052 scopus 로고
    • Organization of the cytoskeleton in pollen tubes of Pyrus communis: A study employing conventional and freeze-substitution electron microscopy, immunofluorescence, and rhodamine-phalloidin
    • Tiwari SC, Polito VS (1988) Organization of the cytoskeleton in pollen tubes of Pyrus communis: a study employing conventional and freeze-substitution electron microscopy, immunofluorescence, and rhodamine-phalloidin. Protoplasma 147: 100-112
    • (1988) Protoplasma , vol.147 , pp. 100-112
    • Tiwari, S.C.1    Polito, V.S.2
  • 60
    • 0022111816 scopus 로고
    • Characterization and immunocytochemical distribution of calmodulin in higher plant endosperm cells: Localization in the mitotic apparatus
    • Vantard M, Lambert A-M, Mey JD, Picquot P, Van Eldik LJ (1985) Characterization and immunocytochemical distribution of calmodulin in higher plant endosperm cells: localization in the mitotic apparatus. J Cell Biol 101: 488-499
    • (1985) J Cell Biol , vol.101 , pp. 488-499
    • Vantard, M.1    Lambert, A.-M.2    Mey, J.D.3    Picquot, P.4    Van Eldik, L.J.5
  • 61
    • 0030909875 scopus 로고    scopus 로고
    • Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum
    • Vidali L, Hepler PK (1997) Characterization and localization of profilin in pollen grains and tubes of Lilium longiflorum. Cell Motil Cytoskelet 36: 323-338
    • (1997) Cell Motil Cytoskelet , vol.36 , pp. 323-338
    • Vidali, L.1    Hepler, P.K.2
  • 62
    • 0033395843 scopus 로고    scopus 로고
    • The 135-kDa actin-bundling protein from lilium longiflorum pollen is the plant homologue of villin
    • Vidali L, Yokota E, Cheung AY, Shimmen T, Hepler PK (1999) The 135-kDa actin-bundling protein from Lilium longiflorum pollen is the plant homologue of villin. Protoplasma 209: 283-291
    • (1999) Protoplasma , vol.209 , pp. 283-291
    • Vidali, L.1    Yokota, E.2    Cheung, A.Y.3    Shimmen, T.4    Hepler, P.K.5
  • 63
    • 0031913168 scopus 로고    scopus 로고
    • Calmodulin is uniformly distributed during cell division in living stamen hair cells of Tradescantia virginiana
    • Vos JW, Hepler PK (1998) Calmodulin is uniformly distributed during cell division in living stamen hair cells of Tradescantia virginiana. Protoplasma 201: 158-171
    • (1998) Protoplasma , vol.201 , pp. 158-171
    • Vos, J.W.1    Hepler, P.K.2
  • 64
    • 0000484778 scopus 로고
    • Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells
    • Wick SM, Muto S, Duniec J (1985) Double immunofluorescence labeling of calmodulin and tubulin in dividing plant cells. Protoplasma 126: 198-206
    • (1985) Protoplasma , vol.126 , pp. 198-206
    • Wick, S.M.1    Muto, S.2    Duniec, J.3
  • 66
    • 0032867689 scopus 로고    scopus 로고
    • The 135-kDa actin-bundling protein from lily pollen tubes arranges F-actin into bundles with uniform polarity
    • Yokota E, Shimmen T (1999) The 135-kDa actin-bundling protein from lily pollen tubes arranges F-actin into bundles with uniform polarity. Planta 209: 264-266
    • (1999) Planta , vol.209 , pp. 264-266
    • Yokota, E.1    Shimmen, T.2
  • 67
    • 0000806896 scopus 로고    scopus 로고
    • Actin-bundling protein isolated from pollen tubes of lily: Biochemical and immunocytochemical characterization
    • Yokota E, Takahara K, 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    Takahara, K.2    Shimmen, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.