메뉴 건너뛰기




Volumn 73, Issue 5, 2013, Pages 747-760

Oryza sativa actin-interacting protein 1 is required for rice growth by promoting actin turnover

Author keywords

actin; actin turnover; actin binding protein; ADF; AIP1; Oryza sativa

Indexed keywords

ACTIN; ACTIN TURNOVER; ACTIN-BINDING PROTEINS; ADF; AIP1; ORYZA SATIVA;

EID: 84874476826     PISSN: 09607412     EISSN: 1365313X     Source Type: Journal    
DOI: 10.1111/tpj.12065     Document Type: Article
Times cited : (30)

References (71)
  • 1
    • 0032803529 scopus 로고    scopus 로고
    • Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin
    • DOI 10.1046/j.1365-2443.1999.00262.x
    • Aizawa, H., Katadae, M., Maruya, M., Sameshima, M., Murakami-Murofushi, K., and, Yahara, I., (1999) Hyperosmotic stress-induced reorganization of actin bundles in Dictyostelium cells over-expressing cofilin. Genes Cells, 4, 311-324. (Pubitemid 29359447)
    • (1999) Genes to Cells , vol.4 , Issue.6 , pp. 311-324
    • Aizawa, H.1    Katadae, M.2    Maruya, M.3    Sameshima, M.4    Murakami-Murofushi, K.5    Yahara, I.6
  • 3
    • 0035910096 scopus 로고    scopus 로고
    • Direct real-time observation of actin filament branching mediated by Arp2/3 complex using total internal reflection fluorescence microscopy
    • DOI 10.1073/pnas.211556398
    • 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. (Pubitemid 34013960)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.26 , pp. 15009-15013
    • Amann, K.J.1    Pollard, T.D.2
  • 4
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D.C., Basart, E., and, Botstein, D., (1995) Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2, 28-35.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 5
    • 33749046492 scopus 로고    scopus 로고
    • Mechanism of Actin Filament Turnover by Severing and Nucleation at Different Concentrations of ADF/Cofilin
    • DOI 10.1016/j.molcel.2006.08.006, PII S109727650600565X
    • 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. (Pubitemid 44466682)
    • (2006) Molecular Cell , vol.24 , Issue.1 , pp. 13-23
    • Andrianantoandro, E.1    Pollard, T.D.2
  • 6
    • 82755195651 scopus 로고    scopus 로고
    • Actin interacting protein1 and actin depolymerizing factor drive rapid actin dynamics in Physcomitrella patens
    • Augustine, R.C., Pattavina, K.A., Tuzel, E., Vidali, L., and, Bezanilla, M., (2011) Actin interacting protein1 and actin depolymerizing factor drive rapid actin dynamics in Physcomitrella patens. Plant Cell, 23, 3696-3710.
    • (2011) Plant Cell , vol.23 , pp. 3696-3710
    • Augustine, R.C.1    Pattavina, K.A.2    Tuzel, E.3    Vidali, L.4    Bezanilla, M.5
  • 7
    • 0035282059 scopus 로고    scopus 로고
    • Latrunculin B-induced plant dwarfism: Plant cell elongation is F-actin-dependent
    • DOI 10.1006/dbio.2000.0115
    • Baluska, F., Jasik, J., Edelmann, H.G., Salajova, T., and, Volkmann, D., (2001) Latrunculin B-induced plant dwarfism: plant cell elongation is F-actin-dependent. Dev. Biol. 231, 113-124. (Pubitemid 32198391)
    • (2001) Developmental Biology , vol.231 , Issue.1 , pp. 113-124
    • Baluska, F.1    Jasik, J.2    Edelmann, H.G.3    Salajova, T.4    Volkmann, D.5
  • 8
    • 33847213280 scopus 로고    scopus 로고
    • A novel system for gene silencing using siRNAs in rice leaf and stem-derived protoplasts
    • Bart, R., Chern, M., Park, C.J., Bartley, L., and, Ronald, P.C., (2006) A novel system for gene silencing using siRNAs in rice leaf and stem-derived protoplasts. Plant Methods, 2, 13.
    • (2006) Plant Methods , vol.2 , pp. 13
    • Bart, R.1    Chern, M.2    Park, C.J.3    Bartley, L.4    Ronald, P.C.5
  • 9
    • 78649617189 scopus 로고    scopus 로고
    • Actin dynamics in plant cells: A team effort from multiple proteins orchestrates this very fast-paced game
    • Blanchoin, L., Boujemaa-Paterski, R., Henty, J.L., Khurana, P., and, Staiger, C.J., (2010) Actin dynamics in plant cells: a team effort from multiple proteins orchestrates this very fast-paced game. Curr. Opin. Plant Biol. 13, 714-723.
    • (2010) Curr. Opin. Plant Biol. , vol.13 , pp. 714-723
    • Blanchoin, L.1    Boujemaa-Paterski, R.2    Henty, J.L.3    Khurana, P.4    Staiger, C.J.5
  • 10
    • 33750365532 scopus 로고    scopus 로고
    • Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1
    • DOI 10.1083/jcb.200603149
    • Brieher, W.M., Kueh, H.Y., Ballif, B.A., and, Mitchison, T.J., (2006) Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1. J. Cell Biol. 175, 315-324. (Pubitemid 44631425)
    • (2006) Journal of Cell Biology , vol.175 , Issue.2 , pp. 315-324
    • Brieher, W.M.1    Hao, Y.K.2    Ballif, B.A.3    Mitchison, T.J.4
  • 11
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: Implication in actin-based motility
    • DOI 10.1083/jcb.136.6.1307
    • Carlier, M.F., Laurent, V., Santolini, J., Melki, R., Didry, D., Xia, G.X., Hong, Y., Chua, N.H., and, Pantaloni, D., (1997) Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover: implication in actin-based motility. J. Cell Biol. 136, 1307-1322. (Pubitemid 27421917)
    • (1997) Journal of Cell Biology , vol.136 , Issue.6 , pp. 1307-1322
    • Carlier, M.-F.1    Laurent, V.2    Santolini, J.3    Melki, R.4    Didry, D.5    Xia, G.-X.6    Hong, Y.7    Chua, N.-H.8    Pantaloni, D.9
  • 12
    • 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
  • 13
    • 79960657553 scopus 로고    scopus 로고
    • Gene coexpression network analysis as a source of functional annotation for rice genes
    • Childs, K.L., Davidson, R.M., and, Buell, C.R., (2011) Gene coexpression network analysis as a source of functional annotation for rice genes. PLoS ONE, 6, e22196.
    • (2011) PLoS ONE , vol.6
    • Childs, K.L.1    Davidson, R.M.2    Buell, C.R.3
  • 14
    • 33745350929 scopus 로고    scopus 로고
    • A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities
    • DOI 10.1091/mbc.E05-10-0956
    • Clark, M.G., Teply, J., Haarer, B.K., Viggiano, S.C., Sept, D., and, Amberg, D.C., (2006) A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities. Mol. Biol. Cell, 17, 1971-1984. (Pubitemid 44011611)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1971-1984
    • Clark, M.G.1    Teply, J.2    Haarer, B.K.3    Viggiano, S.C.4    Sept, D.5    Amberg, D.C.6
  • 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
    • 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
  • 17
    • 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
    • DOI 10.1105/tpc.13.6.1333
    • 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. (Pubitemid 32592907)
    • (2001) Plant Cell , vol.13 , Issue.6 , pp. 1333-1346
    • Dong, C.-H.1    Xia, G.-X.2    Hong, Y.3    Ramachandran, S.4    Kost, B.5    Chua, N.-H.6
  • 18
    • 0027968554 scopus 로고
    • Purification, characterization and crystallization of human platelet profilin expressed in Escherichia coli
    • DOI 10.1006/jmbi.1994.1522
    • 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. (Pubitemid 24266059)
    • (1994) Journal of Molecular Biology , vol.241 , Issue.3 , pp. 480-482
    • Fedorov, A.A.1    Pollard, T.D.2    Almo, S.C.3
  • 20
    • 0346849714 scopus 로고    scopus 로고
    • ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments
    • DOI 10.1083/jcb.200308144
    • Galkin, V.E., Orlova, A., VanLoock, M.S., Shvetsov, A., Reisler, E., and, Egelman, E.H., (2003) ADF/cofilin use an intrinsic mode of F-actin instability to disrupt actin filaments. J. Cell Biol. 163, 1057-1066. (Pubitemid 37541881)
    • (2003) Journal of Cell Biology , vol.163 , Issue.5 , pp. 1057-1066
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Shvetsov, A.4    Reisler, E.5    Egelman, E.H.6
  • 22
    • 0347992840 scopus 로고    scopus 로고
    • Actin-Binding Proteins Required for Reliable Chromosome Segregation in Mitosis
    • DOI 10.1002/cm.10150
    • Gerisch, G., Faix, J., Kohler, J., and, Muller-Taubenberger, A., (2004) Actin-binding proteins required for reliable chromosome segregation in mitosis. Cell Motil. Cytoskeleton, 57, 18-25. (Pubitemid 38036813)
    • (2004) Cell Motility and the Cytoskeleton , vol.57 , Issue.1 , pp. 18-25
    • Gerisch, G.1    Faix, J.2    Kohler, J.3    Muller-Taubenberger, A.4
  • 23
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin Promotes Actin Polymerization and Defines the Direction of Cell Motility
    • DOI 10.1126/science.1094561
    • Ghosh, M., Song, X., Mouneimne, G., Sidani, M., Lawrence, D.S., and, Condeelis, J.S., (2004) Cofilin promotes actin polymerization and defines the direction of cell motility. Science, 304, 743-746. (Pubitemid 38560882)
    • (2004) Science , vol.304 , Issue.5671 , pp. 743-746
    • Ghosh, M.1    Song, X.2    Mouneimne, G.3    Sidani, M.4    Lawrence, D.S.5    Condeelis, J.S.6
  • 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. (Pubitemid 27487701)
    • (1997) Biochemical Journal , vol.327 , Issue.3 , pp. 909-915
    • Gibbon, B.C.1    Ren, H.2    Staiger, C.J.3
  • 25
    • 33745726920 scopus 로고    scopus 로고
    • Distribution of G-actin is related to root hair growth of wheat
    • DOI 10.1093/aob/mcl084
    • He, X., Liu, Y.M., Wang, W., and, Li, Y., (2006) Distribution of G-actin is related to root hair growth of wheat. Ann. Bot. 98, 49-55. (Pubitemid 43999595)
    • (2006) Annals of Botany , vol.98 , Issue.1 , pp. 49-55
    • He, X.1    Liu, Y.-M.2    Wang, W.3    Li, Y.4
  • 26
    • 82755161219 scopus 로고    scopus 로고
    • Arabidopsis actin depolymerizing factor4 modulates the stochastic dynamic behavior of actin filaments in the cortical array of epidermal cells
    • Henty, J.L., Bledsoe, S.W., Khurana, P., Meagher, R.B., Day, B., Blanchoin, L., and, Staiger, C.J., (2011) Arabidopsis actin depolymerizing factor4 modulates the stochastic dynamic behavior of actin filaments in the cortical array of epidermal cells. Plant Cell, 23, 3711-3726.
    • (2011) Plant Cell , vol.23 , pp. 3711-3726
    • Henty, J.L.1    Bledsoe, S.W.2    Khurana, P.3    Meagher, R.B.4    Day, B.5    Blanchoin, L.6    Staiger, C.J.7
  • 27
    • 0242666072 scopus 로고    scopus 로고
    • Arabidopsis Capping Protein (AtCP) Is a Heterodimer That Regulates Assembly at the Barbed Ends of Actin Filaments
    • DOI 10.1074/jbc.M306670200
    • 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. (Pubitemid 37377242)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.45 , pp. 44832-44842
    • Huang, S.1    Blanchoin, L.2    Kovar, D.R.3    Staiger, C.J.4
  • 28
    • 2542452087 scopus 로고    scopus 로고
    • A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments
    • DOI 10.1074/jbc.M312973200
    • 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. (Pubitemid 38685646)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 23364-23375
    • Huang, S.1    Blanchoin, L.2    Chaudhry, F.3    Franklin-Tong, V.E.4    Staiger, C.J.5
  • 29
    • 33745359833 scopus 로고    scopus 로고
    • Heterodimeric capping protein from Arabiaopsis is regulated by phosphatidic acid
    • DOI 10.1091/mbc.E05-09-0840
    • 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. (Pubitemid 44011609)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.4 , pp. 1946-1958
    • Huang, S.1    Gao, L.2    Blanchoin, L.3    Staiger, C.J.4
  • 30
    • 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
  • 31
    • 50949092996 scopus 로고    scopus 로고
    • Critical roles of actin-interacting protein 1 in cytokinesis and chemotactic migration of mammalian cells
    • Kato, A., Kurita, S., Hayashi, A., Kaji, N., Ohashi, K., and, Mizuno, K., (2008) Critical roles of actin-interacting protein 1 in cytokinesis and chemotactic migration of mammalian cells. Biochem. J. 414, 261-270.
    • (2008) Biochem. J. , vol.414 , pp. 261-270
    • Kato, A.1    Kurita, S.2    Hayashi, A.3    Kaji, N.4    Ohashi, K.5    Mizuno, K.6
  • 32
    • 1142277951 scopus 로고    scopus 로고
    • The Actin-Interacting Protein AIP1 Is Essential for Actin Organization and Plant Development
    • DOI 10.1016/j.cub.2004.01.004
    • 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. (Pubitemid 38211234)
    • (2004) Current Biology , vol.14 , Issue.2 , pp. 145-149
    • Ketelaar, T.1    Allwood, E.G.2    Anthony, R.3    Voigt, B.4    Menzel, D.5    Hussey, P.J.6
  • 33
    • 0033606768 scopus 로고    scopus 로고
    • DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility
    • DOI 10.1083/jcb.146.2.453
    • Konzok, A., Weber, I., Simmeth, E., Hacker, U., Maniak, M., and, Muller-Taubenberger, A., (1999) DAip1, a Dictyostelium homologue of the yeast actin-interacting protein 1, is involved in endocytosis, cytokinesis, and motility. J. Cell Biol. 146, 453-464. (Pubitemid 29369780)
    • (1999) Journal of Cell Biology , vol.146 , Issue.2 , pp. 453-464
    • Konzok, A.1    Weber, I.2    Simmeth, E.3    Hacker, U.4    Maniak, M.5    Muller-Taubenberger, A.6
  • 34
    • 0034525206 scopus 로고    scopus 로고
    • AtFim1 is an actin filament crosslinking protein from Arabidopsis thaliana
    • DOI 10.1046/j.1365-313X.2000.00907.x
    • 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. (Pubitemid 32040062)
    • (2000) Plant Journal , vol.24 , Issue.5 , pp. 625-636
    • Kovar, D.R.1    Staiger, C.J.2    Weaver, E.A.3    McCurdy, D.W.4
  • 36
    • 48249121534 scopus 로고    scopus 로고
    • Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers
    • Kueh, H.Y., Charras, G.T., Mitchison, T.J., and, Brieher, W.M., (2008) Actin disassembly by cofilin, coronin, and Aip1 occurs in bursts and is inhibited by barbed-end cappers. J. Cell Biol. 182, 341-353.
    • (2008) J. Cell Biol. , vol.182 , pp. 341-353
    • Kueh, H.Y.1    Charras, G.T.2    Mitchison, T.J.3    Brieher, W.M.4
  • 37
    • 18844389128 scopus 로고    scopus 로고
    • Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy
    • DOI 10.1529/biophysj.104.047399
    • Kuhn, J.R., and, Pollard, T.D., (2005) Real-time measurements of actin filament polymerization by total internal reflection fluorescence microscopy. Biophys. J. 88, 1387-1402. (Pubitemid 40975966)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 1387-1402
    • Kuhn, J.R.1    Pollard, T.D.2
  • 38
    • 56049089381 scopus 로고    scopus 로고
    • Collection and comparative analysis of 1888 full-length cDNAs from wild rice Oryza rufipogon Griff W1943
    • Lu, T., Yu, S., Fan, D., Mu, J., Shangguan, Y., Wang, Z., Minobe, Y., Lin, Z., and, Han, B., (2008) Collection and comparative analysis of 1888 full-length cDNAs from wild rice Oryza rufipogon Griff W1943. DNA Res. 15, 285-295.
    • (2008) DNA Res. , vol.15 , pp. 285-295
    • Lu, T.1    Yu, S.2    Fan, D.3    Mu, J.4    Shangguan, Y.5    Wang, Z.6    Minobe, Y.7    Lin, Z.8    Han, B.9
  • 39
    • 0033588258 scopus 로고    scopus 로고
    • ADF/cofilin weakens lateral contacts in the actin filament
    • DOI 10.1006/jmbi.1999.2968
    • McGough, A., and, Chiu, W., (1999) ADF/cofilin weakens lateral contacts in the actin filament. J. Mol. Biol. 291, 513-519. (Pubitemid 29392629)
    • (1999) Journal of Molecular Biology , vol.291 , Issue.3 , pp. 513-519
    • McGough, A.1    Chiu, W.2
  • 40
    • 0030820734 scopus 로고    scopus 로고
    • Cofilin changes the twist of F-actin: Implications for actin filament dynamics and cellular function
    • DOI 10.1083/jcb.138.4.771
    • McGough, A., Pope, B., Chiu, W., and, Weeds, A., (1997) Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 138, 771-781. (Pubitemid 27365041)
    • (1997) Journal of Cell Biology , vol.138 , Issue.4 , pp. 771-781
    • McGough, A.1    Pope, B.2    Chiu, W.3    Weeds, A.4
  • 41
    • 33847326948 scopus 로고    scopus 로고
    • A large-scale collection of phenotypic data describing an insertional mutant population to facilitate functional analysis of rice genes
    • Miyao, A., Iwasaki, Y., Kitano, H., Itoh, J., Maekawa, M., Murata, K., Yatou, O., Nagato, Y., and, Hirochika, H., (2007) A large-scale collection of phenotypic data describing an insertional mutant population to facilitate functional analysis of rice genes. Plant Mol. Biol. 63, 625-635.
    • (2007) Plant Mol. Biol. , vol.63 , pp. 625-635
    • Miyao, A.1    Iwasaki, Y.2    Kitano, H.3    Itoh, J.4    Maekawa, M.5    Murata, K.6    Yatou, O.7    Nagato, Y.8    Hirochika, H.9
  • 42
    • 0242351058 scopus 로고    scopus 로고
    • Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform
    • DOI 10.1242/jcs.00717
    • Mohri, K., and, Ono, S., (2003) Actin filament disassembling activity of Caenorhabditis elegans actin-interacting protein 1 (UNC-78) is dependent on filament binding by a specific ADF/cofilin isoform. J. Cell Sci. 116, 4107-4118. (Pubitemid 37337085)
    • (2003) Journal of Cell Science , vol.116 , Issue.20 , pp. 4107-4118
    • Mohri, K.1    Ono, S.2
  • 43
    • 33745745585 scopus 로고    scopus 로고
    • Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle
    • DOI 10.1091/mbc.E05-11-1016
    • Mohri, K., Ono, K., Yu, R., Yamashiro, S., and, Ono, S., (2006) Enhancement of actin-depolymerizing factor/cofilin-dependent actin disassembly by actin-interacting protein 1 is required for organized actin filament assembly in the Caenorhabditis elegans body wall muscle. Mol. Biol. Cell, 17, 2190-2199. (Pubitemid 44011735)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.5 , pp. 2190-2199
    • Mohri, K.1    Ono, K.2    Yu, R.3    Yamashiro, S.4    Ono, S.5
  • 45
    • 0033050852 scopus 로고    scopus 로고
    • XAIP1: A Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins
    • Okada, K., Obinata, T., and, Abe, H., (1999) XAIP1: a Xenopus homologue of yeast actin interacting protein 1 (AIP1), which induces disassembly of actin filaments cooperatively with ADF/cofilin family proteins. J. Cell Sci. 112, 1553-1565. (Pubitemid 29261317)
    • (1999) Journal of Cell Science , vol.112 , Issue.10 , pp. 1553-1565
    • Okada, K.1    Obinata, T.2    Abe, H.3
  • 46
    • 0037044771 scopus 로고    scopus 로고
    • Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends
    • DOI 10.1074/jbc.M203111200
    • Okada, K., Blanchoin, L., Abe, H., Chen, H., Pollard, T.D., and, Bamburg, J.R., (2002) Xenopus actin-interacting protein 1 (XAip1) enhances cofilin fragmentation of filaments by capping filament ends. J. Biol. Chem. 277, 43011-43016. (Pubitemid 35285681)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.45 , pp. 43011-43016
    • Okada, K.1    Blanchoin, L.2    Abe, H.3    Chen, H.4    Pollard, T.D.5    Bamburg, J.R.6
  • 47
    • 33745613278 scopus 로고    scopus 로고
    • Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: A coordinated mechanism for severing and capping filaments
    • DOI 10.1091/mbc.E06-02-0135
    • Okada, K., Ravi, H., Smith, E.M., and, Goode, B.L., (2006) Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Mol. Biol. Cell, 17, 2855-2868. (Pubitemid 43993492)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.7 , pp. 2855-2868
    • Okada, K.1    Ravi, H.2    Smith, E.M.3    Goode, B.L.4
  • 48
    • 0035911962 scopus 로고    scopus 로고
    • The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments
    • DOI 10.1083/jcb.152.6.1313
    • Ono, S., (2001) The Caenorhabditis elegans unc-78 gene encodes a homologue of actin-interacting protein 1 required for organized assembly of muscle actin filaments. J. Cell Biol. 152, 1313-1319. (Pubitemid 34280188)
    • (2001) Journal of Cell Biology , vol.152 , Issue.6 , pp. 1313-1319
    • Ono, S.1
  • 49
    • 1842790731 scopus 로고    scopus 로고
    • Microscopic Evidence That Actin-interacting Protein 1 Actively Disassembles Actin-depolymerizing Factor/Cofilin-bound Actin Filaments
    • DOI 10.1074/jbc.M313418200
    • Ono, S., Mohri, K., and, Ono, K., (2004) Microscopic evidence that actin-interacting protein 1 actively disassembles actin-depolymerizing factor/cofilin-bound actin filaments. J. Biol. Chem. 279, 14207-14212. (Pubitemid 38468959)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.14 , pp. 14207-14212
    • Ono, S.1    Mohri, K.2    Ono, K.3
  • 50
    • 79959893244 scopus 로고    scopus 로고
    • The two actin-interacting protein 1 genes have overlapping and essential function for embryonic development in Caenorhabditis elegans
    • Ono, S., Nomura, K., Hitosugi, S., Tu, D.K., Lee, J.A., Baillie, D.L., and, Ono, K., (2011) The two actin-interacting protein 1 genes have overlapping and essential function for embryonic development in Caenorhabditis elegans. Mol. Biol. Cell, 22, 2258-2269.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 2258-2269
    • Ono, S.1    Nomura, K.2    Hitosugi, S.3    Tu, D.K.4    Lee, J.A.5    Baillie, D.L.6    Ono, K.7
  • 51
    • 0027328612 scopus 로고
    • A conformational change in the actin subunit can change the flexibility of the actin filament
    • DOI 10.1006/jmbi.1993.1393
    • Orlova, A., and, Egelman, E.H., (1993) A conformational change in the actin subunit can change the flexibility of the actin filament. J. Mol. Biol. 232, 334-341. (Pubitemid 23251162)
    • (1993) Journal of Molecular Biology , vol.232 , Issue.2 , pp. 334-341
    • Orlova, A.1    Egelman, E.H.2
  • 52
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • DOI 10.1016/0092-8674(93)90544-Z
    • Pantaloni, D., and, Carlier, M.F., (1993) How profilin promotes actin filament assembly in the presence of thymosin β4. Cell, 75, 1007-1014. (Pubitemid 24014557)
    • (1993) Cell , vol.75 , Issue.5 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.-F.2
  • 54
    • 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
  • 56
    • 0034521760 scopus 로고    scopus 로고
    • Profilin plays a role in cell elongation, cell shape maintenance, and flowering in Arabidopsis
    • DOI 10.1104/pp.124.4.1637
    • Ramachandran, S., Christensen, H.E., Ishimaru, Y., Dong, C.H., Chao-Ming, W., Cleary, A.L., and, Chua, N.H., (2000) Profilin plays a role in cell elongation, cell shape maintenance, and flowering in Arabidopsis. Plant Physiol. 124, 1637-1647. (Pubitemid 32053498)
    • (2000) Plant Physiology , vol.124 , Issue.4 , pp. 1637-1647
    • Ramachandran, S.1    Christensen, H.E.M.2    Ishimaru, Y.3    Dong, C.-H.4    Chao-Ming, W.5    Cleary, A.L.6    Chua, N.-H.7
  • 58
    • 77956900248 scopus 로고    scopus 로고
    • Strategies of actin reorganisation in plant cells
    • Smertenko, A.P., Deeks, M.J., and, Hussey, P.J., (2010) Strategies of actin reorganisation in plant cells. J. Cell Sci. 123, 3019-3028.
    • (2010) J. Cell Sci. , vol.123 , pp. 3019-3028
    • Smertenko, A.P.1    Deeks, M.J.2    Hussey, P.J.3
  • 59
    • 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
  • 62
    • 33748319354 scopus 로고    scopus 로고
    • Early infection of scutellum tissue with Agrobacterium allows high-speed transformation of rice
    • DOI 10.1111/j.1365-313X.2006.02836.x
    • Toki, S., Hara, N., Ono, K., Onodera, H., Tagiri, A., Oka, S., and, Tanaka, H., (2006) Early infection of scutellum tissue with Agrobacterium allows high-speed transformation of rice. Plant J. 47, 969-976. (Pubitemid 44326445)
    • (2006) Plant Journal , vol.47 , Issue.6 , pp. 969-976
    • Toki, S.1    Hara, N.2    Ono, K.3    Onodera, H.4    Tagiri, A.5    Oka, S.6    Tanaka, H.7
  • 63
    • 18944390005 scopus 로고    scopus 로고
    • A practical vector for efficient knockdown of gene expression in rice (Oryza sativa L.)
    • Wang, Z., Chen, C., Xu, Y., Jiang, R., Xu, Z., 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. (Pubitemid 40706530)
    • (2004) Plant Molecular Biology Reporter , vol.22 , Issue.4 , pp. 409-417
    • Wang, Z.1    Chen, C.2    Xu, Y.3    Jiang, R.4    Han, Y.5    Xu, Z.6    Chong, K.7
  • 65
    • 79953076043 scopus 로고    scopus 로고
    • BENT UPPERMOST INTERNODE1 encodes the class II formin FH5 crucial for actin organization and rice development
    • Yang, W., Ren, S., Zhang, X., Gao, M., Ye, S., Qi, Y., Zheng, Y., Wang, J., Zeng, L., Li, Q., Huang, S., and, He, Z., (2011) BENT UPPERMOST INTERNODE1 encodes the class II formin FH5 crucial for actin organization and rice development. Plant Cell, 23, 661-680.
    • (2011) Plant Cell , vol.23 , pp. 661-680
    • Yang, W.1    Ren, S.2    Zhang, X.3    Gao, M.4    Ye, S.5    Qi, Y.6    Zheng, Y.7    Wang, J.8    Zeng, L.9    Li, Q.10    Huang, S.11    He, Z.12
  • 66
    • 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
  • 67
    • 28244445008 scopus 로고    scopus 로고
    • RMD: A rice mutant database for functional analysis of the rice genome
    • Zhang, J., Li, C., Wu, C., Xiong, L., Chen, G., Zhang, Q., and, Wang, S., (2006) RMD: a rice mutant database for functional analysis of the rice genome. Nucleic Acids Res. 34, D745-D748.
    • (2006) Nucleic Acids Res. , vol.34
    • Zhang, J.1    Li, C.2    Wu, C.3    Xiong, L.4    Chen, G.5    Zhang, Q.6    Wang, S.7
  • 68
  • 70
    • 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., (2011b) 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
  • 71
    • 0027293382 scopus 로고
    • Recent quantitative studies of actin filament turnover during cell locomotion
    • Zigmond, S.H., (1993) Recent quantitative studies of actin filament turnover during cell locomotion. Cell Motil. Cytoskeleton, 25, 309-316. (Pubitemid 23225031)
    • (1993) Cell Motility and the Cytoskeleton , vol.25 , Issue.4 , pp. 309-316
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.