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Volumn 288, Issue 45, 2013, Pages 32277-32288

Arabidopsis CROLIN1, a novel plant actin-binding protein, functions in cross-linking and stabilizing actin filaments

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN-BINDING PROTEINS; ARABIDOPSIS GENOME; BIOCHEMICAL ANALYSIS; CYTOPLASMIC STREAMING; ORGANELLE MOVEMENT; PHYSIOLOGICAL PROCESS; POLLEN GERMINATION; POLLEN TUBE GROWTH;

EID: 84887494888     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.483594     Document Type: Article
Times cited : (34)

References (43)
  • 3
    • 0002363582 scopus 로고
    • The plant cytoskeleton
    • (Meyerowitz, E., and Somerville, C., eds), Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Meagher, R. B., and Williamson, R. E. (1994) The plant cytoskeleton. in Arabidopsis (Meyerowitz, E., and Somerville, C., eds) pp. 1049-1084, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • (1994) Arabidopsis , pp. 1049-1084
    • Meagher, R.B.1    Williamson, R.E.2
  • 4
  • 5
    • 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
  • 6
    • 79954822315 scopus 로고    scopus 로고
    • Arabidopsis VILLIN4 is involved in root hair growth through regulating actin organization in a Ca2+-dependent manner
    • Zhang, Y., Xiao, Y., Du, F., Cao, L., Dong, H., and Ren, H. (2011) Arabidopsis VILLIN4 is involved in root hair growth through regulating actin organization in a Ca2+-dependent manner. New Phytol. 190, 667-682
    • (2011) New Phytol , vol.190 , pp. 667-682
    • Zhang, Y.1    Xiao, Y.2    Du, F.3    Cao, L.4    Dong, H.5    Ren, H.6
  • 8
    • 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
  • 10
    • 78049465197 scopus 로고    scopus 로고
    • Arabidopsis LIM proteins. A family of actin bundlers with distinct expression patterns and modes of regulation
    • Papuga, J., Hoffmann, C., Dieterle, M., Moes, D., Moreau, F., Tholl, S., Steinmetz, A., and Thomas, C. (2010) Arabidopsis LIM proteins. A family of actin bundlers with distinct expression patterns and modes of regulation. Plant Cell 22, 3034-3052
    • (2010) Plant Cell , vol.22 , pp. 3034-3052
    • Papuga, J.1    Hoffmann, C.2    Dieterle, M.3    Moes, D.4    Moreau, F.5    Tholl, S.6    Steinmetz, A.7    Thomas, C.8
  • 11
    • 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
  • 12
    • 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
  • 13
    • 78650879023 scopus 로고    scopus 로고
    • Arabidopsis FIMBRIN5, an actin bundling factor, is required for pollen germination and pollen tube growth
    • Wu, Y., Yan, J., Zhang, R., Qu, X., Ren, S., Chen, N., and Huang, S. (2010) Arabidopsis FIMBRIN5, an actin bundling factor, is required for pollen germination and pollen tube growth. Plant Cell 22, 3745-3763
    • (2010) Plant Cell , vol.22 , pp. 3745-3763
    • Wu, Y.1    Yan, J.2    Zhang, R.3    Qu, X.4    Ren, S.5    Chen, N.6    Huang, S.7
  • 14
    • 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
  • 15
    • 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. (2011a) 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
  • 17
    • 77951198791 scopus 로고    scopus 로고
    • The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule binding domain
    • Deeks, M. J., Fendrych, M., Smertenko, A., Bell, K. S., Oparka, K., Cvrckova ́, F., Zársky, V., and Hussey, P. J. (2010) The plant formin AtFH4 interacts with both actin and microtubules, and contains a newly identified microtubule binding domain. J. Cell Sci. 123, 1209-1215
    • (2010) J. Cell Sci , vol.123 , pp. 1209-1215
    • Deeks, M.J.1    Fendrych, M.2    Smertenko, A.3    Bell, K.S.4    Oparka, K.5    Cvrcková, F.6    Zársky, V.7    Hussey, P.J.8
  • 18
    • 77957781458 scopus 로고    scopus 로고
    • The type II Arabidopsis formin14 interacts with microtubules and microfilaments to regulate cell division
    • Li, Y., Shen, Y., Cai, C., Zhong, C., Zhu, L., Yuan, M., and Ren, H. (2010) The type II Arabidopsis formin14 interacts with microtubules and microfilaments to regulate cell division. Plant Cell 22, 2710-2726
    • (2010) Plant Cell , vol.22 , pp. 2710-2726
    • Li, Y.1    Shen, Y.2    Cai, C.3    Zhong, C.4    Zhu, L.5    Yuan, M.6    Ren, H.7
  • 19
    • 79953203617 scopus 로고    scopus 로고
    • AtFH8 is involved in root development under effect of low-dose latrunculin B in dividing cells
    • Xue, X. H., Guo, C. Q., Du, F., Lu, Q. L., Zhang, C. M., and Ren, H. Y. (2011) AtFH8 is involved in root development under effect of low-dose latrunculin B in dividing cells. Mol. Plant 4, 264-278
    • (2011) Mol. Plant , vol.4 , pp. 264-278
    • Xue, X.H.1    Guo, C.Q.2    Du, F.3    Lu, Q.L.4    Zhang, C.M.5    Ren, H.Y.6
  • 21
    • 0037193710 scopus 로고    scopus 로고
    • Actin-binding proteins in the Arabidopsis genome database. Properties of functionally distinct plant actin-depolymerizing factors/cofilins
    • Hussey, P. J., Allwood, E. G., and Smertenko, A. P. (2002) Actin-binding proteins in the Arabidopsis genome database. Properties of functionally distinct plant actin-depolymerizing factors/cofilins. Philos. Trans. R. Soc. Lond. B Biol. Sci. 357, 791-798
    • (2002) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.357 , pp. 791-798
    • Hussey, P.J.1    Allwood, E.G.2    Smertenko, A.P.3
  • 24
    • 84861752350 scopus 로고    scopus 로고
    • Arabidopsis V-ATPase B subunits are involved in actin cytoskeleton remodeling via binding to, bundling, and stabilizing F-actin
    • Ma, B., Qian, D., Nan, Q., Tan, C., An, L., and Xiang, Y. (2012) Arabidopsis V-ATPase B subunits are involved in actin cytoskeleton remodeling via binding to, bundling, and stabilizing F-actin. J. Biol. Chem. 287, 19008-19017
    • (2012) J. Biol. Chem , vol.287 , pp. 19008-19017
    • Ma, B.1    Qian, D.2    Nan, Q.3    Tan, C.4    An, L.5    Xiang, Y.6
  • 26
    • 34547138125 scopus 로고    scopus 로고
    • SB401, a pollen-specific protein from Solanum berthaultii, binds to and bundles microtubules and F-actin
    • Huang, S., Jin, L., Du, J., Li, H., Zhao, Q., Ou, G., Ao, G., and Yuan, M. (2007) SB401, a pollen-specific protein from Solanum berthaultii, binds to and bundles microtubules and F-actin. Plant J. 51, 406-418
    • (2007) Plant J , vol.51 , pp. 406-418
    • Huang, S.1    Jin, L.2    Du, J.3    Li, H.4    Zhao, Q.5    Ou, G.6    Ao, G.7    Yuan, M.8
  • 28
    • 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
  • 29
    • 34247555357 scopus 로고    scopus 로고
    • The function of actin-binding proteins in pollen tube growth
    • Ren, H., and Xiang, Y. (2007) The function of actin-binding proteins in pollen tube growth. Protoplasma 230, 171-182
    • (2007) Protoplasma , vol.230 , pp. 171-182
    • Ren, H.1    Xiang, Y.2
  • 30
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosintroponin 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 tropomyosintroponin 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
  • 31
    • 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
  • 32
    • 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
  • 33
    • 84871927481 scopus 로고    scopus 로고
    • Overexpression of profilin 3 affects cell elongation and F-actin organization in Arabidopsis thaliana
    • Fan, T. T., Zhai, H. H., Shi, W. W., Wang, J., Jia, H. L., Xiang, Y., and An, L. Z. (2013) Overexpression of profilin 3 affects cell elongation and F-actin organization in Arabidopsis thaliana. Plant Cell Rep. 32, 149-160
    • (2013) Plant Cell Rep , vol.32 , pp. 149-160
    • Fan, T.T.1    Zhai, H.H.2    Shi, W.W.3    Wang, J.4    Jia, H.L.5    Xiang, Y.6    An, L.Z.7
  • 34
    • 0042695874 scopus 로고    scopus 로고
    • The Arabidopsis SKP1-like genes present a spectrum of expression profiles
    • Marrocco, K., Lecureuil, A., Nicolas, P., and Guerche, P. (2003) The Arabidopsis SKP1-like genes present a spectrum of expression profiles. Plant Mol. Biol. 52, 715-727
    • (2003) Plant Mol. Biol , vol.52 , pp. 715-727
    • Marrocco, K.1    Lecureuil, A.2    Nicolas, P.3    Guerche, P.4
  • 35
    • 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
  • 36
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web. A case study using the Phyre server
    • Kelley, L. A., and Sternberg, M. J. (2009) Protein structure prediction on the Web. A case study using the Phyre server. Nat. Protocols 4, 363-371
    • (2009) Nat. Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 38
    • 0036183061 scopus 로고    scopus 로고
    • Conserved and nonconserved features of the folding pathway of hisactophilin, a β-trefoil protein
    • Liu, C., Gaspar, J. A., Wong, H. J., and Meiering, E. M. (2002) Conserved and nonconserved features of the folding pathway of hisactophilin, a β-trefoil protein. Protein Sci. 11, 669-679
    • (2002) Protein Sci , vol.11 , pp. 669-679
    • Liu, C.1    Gaspar, J.A.2    Wong, H.J.3    Meiering, E.M.4
  • 39
    • 3343012103 scopus 로고    scopus 로고
    • Hisactophilin is involved in osmoprotection in Dictyostelium
    • Pintsch, T., Zischka, H., and Schuster, S. C. (2002) Hisactophilin is involved in osmoprotection in Dictyostelium. BMC Biochem. 3, 10-17
    • (2002) BMC Biochem , vol.3 , pp. 10-17
    • Pintsch, T.1    Zischka, H.2    Schuster, S.C.3
  • 40
    • 0030929818 scopus 로고    scopus 로고
    • Hypothesis what is the diameter of the actin filament?
    • Grazi, E. (1997) Hypothesis what is the diameter of the actin filament? FEBS Lett. 405, 249-252
    • (1997) FEBS Lett , vol.405 , pp. 249-252
    • Grazi, E.1
  • 41
    • 33846371992 scopus 로고    scopus 로고
    • Molecular scale imaging of F-actin assemblies immobilized on a photopolymer surface
    • Ikawa, T., Hoshino, F., Watanabe, O., Li, Y., Pincus, P., and Safinya, C. R. (2007) Molecular scale imaging of F-actin assemblies immobilized on a photopolymer surface. Phys. Rev. Lett. 98, 018101-018104
    • (2007) Phys. Rev. Lett , vol.98 , pp. 018101-018104
    • Ikawa, T.1    Hoshino, F.2    Watanabe, O.3    Li, Y.4    Pincus, P.5    Safinya, C.R.6
  • 42
    • 0030843484 scopus 로고    scopus 로고
    • Actin depolymerizing factor (ADF/cofilin) enhances the rate of filament turnover. Implication in actin-based motility
    • 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
    • (1997) J. Cell Biol , vol.136 , 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
  • 43
    • 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


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