메뉴 건너뛰기




Volumn 18, Issue 9, 2013, Pages 496-504

Regulation of cytoskeletal dynamics by phospholipase D and phosphatidic acid

Author keywords

Actin; Cytoskeleton; Microtubules; Phosphatidic acid; Phospholipase D; Signaling

Indexed keywords

ANIMALIA;

EID: 84883295137     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2013.04.005     Document Type: Review
Times cited : (104)

References (89)
  • 1
    • 33745000523 scopus 로고    scopus 로고
    • Visualization of cellulose synthase demonstrates functional association with microtubules
    • Paredez A.R., et al. Visualization of cellulose synthase demonstrates functional association with microtubules. Science 2006, 312:1491-1495.
    • (2006) Science , vol.312 , pp. 1491-1495
    • Paredez, A.R.1
  • 2
    • 67650079304 scopus 로고    scopus 로고
    • Arabidopsis cortical microtubules position cellulose synthase delivery to the plasma membrane and interact with cellulose synthase trafficking compartments
    • Gutierrez R., et al. Arabidopsis cortical microtubules position cellulose synthase delivery to the plasma membrane and interact with cellulose synthase trafficking compartments. Nat. Cell Biol. 2009, 11:797-806.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 797-806
    • Gutierrez, R.1
  • 3
    • 0038518182 scopus 로고    scopus 로고
    • Sustained microtubule treadmilling in Arabidopsis cortical arrays
    • Shaw S.L., et al. Sustained microtubule treadmilling in Arabidopsis cortical arrays. Science 2003, 300:1715-1718.
    • (2003) Science , vol.300 , pp. 1715-1718
    • Shaw, S.L.1
  • 4
    • 33745966640 scopus 로고    scopus 로고
    • Microtubule dynamics and organization in the plant cortical array
    • Ehrhardt D.W., Shaw S.L. Microtubule dynamics and organization in the plant cortical array. Annu. Rev. Plant Biol. 2006, 57:859-875.
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 859-875
    • Ehrhardt, D.W.1    Shaw, S.L.2
  • 5
    • 44649191103 scopus 로고    scopus 로고
    • Microtubules, MAPs and plant directional cell expansion
    • Sedbrook J.C., Kaloriti D. Microtubules, MAPs and plant directional cell expansion. Trends Plant Sci. 2008, 13:303-310.
    • (2008) Trends Plant Sci. , vol.13 , pp. 303-310
    • Sedbrook, J.C.1    Kaloriti, D.2
  • 6
    • 60849130414 scopus 로고    scopus 로고
    • Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array
    • Staiger C.J., et al. Actin filament dynamics are dominated by rapid growth and severing activity in the Arabidopsis cortical array. J. Cell Biol. 2009, 184:269-280.
    • (2009) J. Cell Biol. , vol.184 , pp. 269-280
    • Staiger, C.J.1
  • 7
    • 77956900248 scopus 로고    scopus 로고
    • Strategies of actin reorganisation in plant cells
    • Smertenko A.P., et al. Strategies of actin reorganisation in plant cells. J. Cell Sci. 2010, 123:3019-3028.
    • (2010) J. Cell Sci. , vol.123 , pp. 3019-3028
    • Smertenko, A.P.1
  • 8
    • 77951831907 scopus 로고    scopus 로고
    • Regulation of actin dynamics by actin-binding proteins in pollen
    • Staiger C.J., et al. Regulation of actin dynamics by actin-binding proteins in pollen. J. Exp. Bot. 2010, 61:1969-1986.
    • (2010) J. Exp. Bot. , vol.61 , pp. 1969-1986
    • Staiger, C.J.1
  • 9
    • 6044230998 scopus 로고    scopus 로고
    • MAPs in plant cells: delineating microtubule growth dynamics and organization
    • Sedbrook J.C. MAPs in plant cells: delineating microtubule growth dynamics and organization. Curr. Opin. Plant Biol. 2004, 7:632-640.
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 632-640
    • Sedbrook, J.C.1
  • 10
    • 33749860518 scopus 로고    scopus 로고
    • Actin dynamics: old friends with new stories
    • Staiger C.J., Blanchoin L. Actin dynamics: old friends with new stories. Curr. Opin. Plant Biol. 2006, 9:554-562.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 554-562
    • Staiger, C.J.1    Blanchoin, L.2
  • 11
    • 33847337003 scopus 로고    scopus 로고
    • Microtubule-associated proteins in higher plants
    • Hamada T. Microtubule-associated proteins in higher plants. J. Plant Res. 2007, 120:79-98.
    • (2007) J. Plant Res. , vol.120 , pp. 79-98
    • Hamada, T.1
  • 12
    • 84886248412 scopus 로고    scopus 로고
    • The cytoskeleton and signal transduction: role and regulation of plant actin- and microtubule-binding proteins
    • Hussey P.J., Hashimoto T. The cytoskeleton and signal transduction: role and regulation of plant actin- and microtubule-binding proteins. Annu. Plant Rev. 2008, 33:244-272.
    • (2008) Annu. Plant Rev. , vol.33 , pp. 244-272
    • Hussey, P.J.1    Hashimoto, T.2
  • 13
    • 3042664547 scopus 로고    scopus 로고
    • Tansley review: the role of the actin cytoskeleton in plant cell signaling
    • Drøbak B.K., et al. Tansley review: the role of the actin cytoskeleton in plant cell signaling. New Phytol. 2004, 163:13-30.
    • (2004) New Phytol. , vol.163 , pp. 13-30
    • Drøbak, B.K.1
  • 14
    • 33747887420 scopus 로고    scopus 로고
    • The role of phospholipase D in plant stress responses
    • Bargmann B.O., Munnik T. The role of phospholipase D in plant stress responses. Curr. Opin. Plant Biol. 2006, 9:515-522.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 515-522
    • Bargmann, B.O.1    Munnik, T.2
  • 15
    • 79955461974 scopus 로고    scopus 로고
    • Molecular, cellular and physiological responses to phosphatidic acid formation in plants
    • Testerink C., Munnik T. Molecular, cellular and physiological responses to phosphatidic acid formation in plants. J. Exp. Bot. 2011, 62:2349-2361.
    • (2011) J. Exp. Bot. , vol.62 , pp. 2349-2361
    • Testerink, C.1    Munnik, T.2
  • 16
    • 0038271908 scopus 로고    scopus 로고
    • Phosphatidic acid produced by phospholipase D is required for tobacco pollen tube growth
    • Potocký M., et al. Phosphatidic acid produced by phospholipase D is required for tobacco pollen tube growth. Planta 2003, 217:122-130.
    • (2003) Planta , vol.217 , pp. 122-130
    • Potocký, M.1
  • 17
    • 20044394532 scopus 로고    scopus 로고
    • c and membrane secretion
    • c and membrane secretion. J. Exp. Bot. 2005, 416:1665-1674.
    • (2005) J. Exp. Bot. , vol.416 , pp. 1665-1674
    • Monteiro, D.1
  • 18
    • 10744221592 scopus 로고    scopus 로고
    • A protein kinase target of a PDK1 signaling pathway is involved in root hair growth in Arabidopsis
    • Anthony R.G., et al. A protein kinase target of a PDK1 signaling pathway is involved in root hair growth in Arabidopsis. EMBO J. 2004, 23:572-581.
    • (2004) EMBO J. , vol.23 , pp. 572-581
    • Anthony, R.G.1
  • 19
    • 0038442830 scopus 로고    scopus 로고
    • Modulation of phospholipid signaling by GLABRA2 in root-hair pattern formation
    • Ohashi Y., et al. Modulation of phospholipid signaling by GLABRA2 in root-hair pattern formation. Science 2003, 300:1427-1430.
    • (2003) Science , vol.300 , pp. 1427-1430
    • Ohashi, Y.1
  • 20
    • 84879982145 scopus 로고    scopus 로고
    • Microtubules, signalling and abiotic stress
    • Nick P. Microtubules, signalling and abiotic stress. Plant J. 2013, 10.1111/tpj.12102.
    • (2013) Plant J.
    • Nick, P.1
  • 21
    • 4143112376 scopus 로고    scopus 로고
    • Isolation and identification of phosphatidic acid targets from plants
    • Testerink C., et al. Isolation and identification of phosphatidic acid targets from plants. Plant J. 2004, 39:527-536.
    • (2004) Plant J. , vol.39 , pp. 527-536
    • Testerink, C.1
  • 22
    • 23044460008 scopus 로고    scopus 로고
    • Phosphatidic acid: a multifunctional stress signaling lipid in plants
    • Testerink C., Munnik T. Phosphatidic acid: a multifunctional stress signaling lipid in plants. Trends Plant Sci. 2005, 10:368-375.
    • (2005) Trends Plant Sci. , vol.10 , pp. 368-375
    • Testerink, C.1    Munnik, T.2
  • 23
    • 84874618106 scopus 로고    scopus 로고
    • Identification of novel candidate phosphatidic acid binding proteins involved in salt stress response of Arabidopsis thaliana roots
    • McLoughlin F., et al. Identification of novel candidate phosphatidic acid binding proteins involved in salt stress response of Arabidopsis thaliana roots. Biochem. J. 2013, 450:573-581.
    • (2013) Biochem. J. , vol.450 , pp. 573-581
    • McLoughlin, F.1
  • 24
    • 0034708158 scopus 로고    scopus 로고
    • Membrane traffic: do cones mark sites of fission?
    • Barr F.A., Shorter J. Membrane traffic: do cones mark sites of fission?. Curr. Biol. 2000, 10:R141-R144.
    • (2000) Curr. Biol. , vol.10
    • Barr, F.A.1    Shorter, J.2
  • 25
    • 74949105152 scopus 로고    scopus 로고
    • Phosphatidic acid: an electrostatic/hydrogen-bond switch
    • Springer-Verlag, T. Munnik (Ed.)
    • Kooijman E.E., Testerink C. Phosphatidic acid: an electrostatic/hydrogen-bond switch. Lipid Signaling in Plants (Plant Cell Monographs) 2010, 203-222. Springer-Verlag. T. Munnik (Ed.).
    • (2010) Lipid Signaling in Plants (Plant Cell Monographs) , pp. 203-222
    • Kooijman, E.E.1    Testerink, C.2
  • 26
    • 74949089275 scopus 로고    scopus 로고
    • Phosphatidic acid phosphatases in seed plants
    • Springer-Verlag, T. Munnik (Ed.)
    • Nakamura Y., Ohta H. Phosphatidic acid phosphatases in seed plants. Lipid Signaling in Plants (Plant Cell Monographs) 2010, 131-141. Springer-Verlag. T. Munnik (Ed.).
    • (2010) Lipid Signaling in Plants (Plant Cell Monographs) , pp. 131-141
    • Nakamura, Y.1    Ohta, H.2
  • 27
    • 33645983977 scopus 로고    scopus 로고
    • Signalling diacylglycerol pyrophosphate, a new phosphatidic acid metabolite
    • van Schooten B., et al. Signalling diacylglycerol pyrophosphate, a new phosphatidic acid metabolite. Biochim. Biophys. Acta 2006, 1761:151-159.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 151-159
    • van Schooten, B.1
  • 28
    • 0037199955 scopus 로고    scopus 로고
    • Profiling membrane lipids in plant stress responses. Role of phospholipase Dα in freezing-induced lipid changes in Arabidopsis
    • Welti R., et al. Profiling membrane lipids in plant stress responses. Role of phospholipase Dα in freezing-induced lipid changes in Arabidopsis. J. Biol. Chem. 2002, 277:31994-32002.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31994-32002
    • Welti, R.1
  • 29
    • 0038662612 scopus 로고    scopus 로고
    • Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid
    • Kooijman E.E., et al. Modulation of membrane curvature by phosphatidic acid and lysophosphatidic acid. Traffic 2003, 4:162-174.
    • (2003) Traffic , vol.4 , pp. 162-174
    • Kooijman, E.E.1
  • 30
    • 34249685982 scopus 로고    scopus 로고
    • An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins
    • Kooijman E.E., et al. An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins. J. Biol. Chem. 2007, 282:11356-11364.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11356-11364
    • Kooijman, E.E.1
  • 31
    • 77956111722 scopus 로고    scopus 로고
    • Phosphatidic acid is a pH biosensor that links membrane biogenesis to metabolism
    • Young B.P., et al. Phosphatidic acid is a pH biosensor that links membrane biogenesis to metabolism. Proc. Natl. Acad. Sci. U.S.A. 2010, 329:1085-1088.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.329 , pp. 1085-1088
    • Young, B.P.1
  • 32
    • 82455188329 scopus 로고    scopus 로고
    • Putting the pH into phosphatidic acid signaling
    • Shin J.J.H., Loewen C.J.R. Putting the pH into phosphatidic acid signaling. BMC Biol. 2011, 9:85.
    • (2011) BMC Biol. , vol.9 , pp. 85
    • Shin, J.J.H.1    Loewen, C.J.R.2
  • 33
    • 0842341454 scopus 로고    scopus 로고
    • Phosphatidic acid induces actin polymerization by activating protein kinases in soybean cells
    • Lee S., et al. Phosphatidic acid induces actin polymerization by activating protein kinases in soybean cells. Mol. Cells 2003, 15:313-319.
    • (2003) Mol. Cells , vol.15 , pp. 313-319
    • Lee, S.1
  • 34
    • 28644433762 scopus 로고    scopus 로고
    • Differential effects of two phospholipase D inhibitors, 1-butanol and N-acylethanolamine, on in vivo cytoskeletal organization and Arabidopsis seedling growth
    • Motes C.M., et al. Differential effects of two phospholipase D inhibitors, 1-butanol and N-acylethanolamine, on in vivo cytoskeletal organization and Arabidopsis seedling growth. Protoplasma 2005, 226:109-123.
    • (2005) Protoplasma , vol.226 , pp. 109-123
    • Motes, C.M.1
  • 35
    • 33745359833 scopus 로고    scopus 로고
    • Heterodimeric capping protein from Arabidopsis is regulated by phosphatidic acid
    • Huang S., et al. Heterodimeric capping protein from Arabidopsis is regulated by phosphatidic acid. Mol. Biol. Cell 2006, 17:1946-1958.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1946-1958
    • Huang, S.1
  • 36
    • 55549106486 scopus 로고    scopus 로고
    • The involvement of phospholipases C and D in the asymmetric division of subsidiary cell mother cells of Zea mays
    • Apostolakos P., et al. The involvement of phospholipases C and D in the asymmetric division of subsidiary cell mother cells of Zea mays. Cell Motil. Cytoskeleton 2008, 65:863-875.
    • (2008) Cell Motil. Cytoskeleton , vol.65 , pp. 863-875
    • Apostolakos, P.1
  • 37
    • 77950954186 scopus 로고    scopus 로고
    • Mutual regulation of plant phospholipase D and the actin cytoskeleton
    • Pleskot R., et al. Mutual regulation of plant phospholipase D and the actin cytoskeleton. Plant J. 2010, 62:494-507.
    • (2010) Plant J. , vol.62 , pp. 494-507
    • Pleskot, R.1
  • 38
    • 84868136934 scopus 로고    scopus 로고
    • Turnover of phosphatidic acid through distinct signalling pathways affects multiple aspects of pollen tube growth in tobacco
    • Pleskot R., et al. Turnover of phosphatidic acid through distinct signalling pathways affects multiple aspects of pollen tube growth in tobacco. Front. Plant Sci. 2012, 3:54.
    • (2012) Front. Plant Sci. , vol.3 , pp. 54
    • Pleskot, R.1
  • 39
    • 84868154444 scopus 로고    scopus 로고
    • Capping protein modulates the dynamic behavior of actin filaments in response to phosphatidic acid in Arabidopsis
    • Li J., et al. Capping protein modulates the dynamic behavior of actin filaments in response to phosphatidic acid in Arabidopsis. Plant Cell 2012, 24:3742-3754.
    • (2012) Plant Cell , vol.24 , pp. 3742-3754
    • Li, J.1
  • 40
    • 0037445874 scopus 로고    scopus 로고
    • Evolutionary conservation of physical and functional interactions between phospholipase D and actin
    • Kusner D.J., et al. Evolutionary conservation of physical and functional interactions between phospholipase D and actin. Arch. Biochem. Biophys. 2003, 412:231-241.
    • (2003) Arch. Biochem. Biophys. , vol.412 , pp. 231-241
    • Kusner, D.J.1
  • 41
    • 48949106158 scopus 로고    scopus 로고
    • New insights into mechanism and regulation of actin capping protein
    • Cooper J.A., Sept D. New insights into mechanism and regulation of actin capping protein. Int. Rev. Cell Mol. Biol. 2008, 267:183-206.
    • (2008) Int. Rev. Cell Mol. Biol. , vol.267 , pp. 183-206
    • Cooper, J.A.1    Sept, D.2
  • 42
    • 84870709983 scopus 로고    scopus 로고
    • Structural insights into the inhibition of actin-capping protein by interactions with phosphatidic acid and phosphatidylinositol (4,5)-bisphosphate
    • Pleskot R., et al. Structural insights into the inhibition of actin-capping protein by interactions with phosphatidic acid and phosphatidylinositol (4,5)-bisphosphate. PLoS Comput. Biol. 2012, 8:e1002765.
    • (2012) PLoS Comput. Biol. , vol.8
    • Pleskot, R.1
  • 43
    • 0242666072 scopus 로고    scopus 로고
    • Arabidopsis capping protein (AtCP) is a heterodimer that regulates assembly at the barbed ends of actin filaments
    • Huang S., et al. Arabidopsis capping protein (AtCP) is a heterodimer that regulates assembly at the barbed ends of actin filaments. J. Biol. Chem. 2003, 278:44832-44842.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44832-44842
    • Huang, S.1
  • 44
    • 34247173028 scopus 로고    scopus 로고
    • Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein
    • Kim Y., et al. Structure/function analysis of the interaction of phosphatidylinositol 4,5-bisphosphate with actin-capping protein. J. Biol. Chem. 2007, 282:5871-5879.
    • (2007) J. Biol. Chem. , vol.282 , pp. 5871-5879
    • Kim, Y.1
  • 45
    • 34948838501 scopus 로고    scopus 로고
    • Single molecule kinetic analysis of actin filament capping: polyphosphoinositides do not dissociate capping proteins
    • Kuhn J.R., Pollard T.D. Single molecule kinetic analysis of actin filament capping: polyphosphoinositides do not dissociate capping proteins. J. Biol. Chem. 2007, 282:28014-28024.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28014-28024
    • Kuhn, J.R.1    Pollard, T.D.2
  • 46
    • 72749108450 scopus 로고    scopus 로고
    • Quantification and cluster analysis of actin cytoskeletal structures in plant cells: role of actin bundling in stomatal movement during diurnal cycles in Arabidopsis guard cells
    • Higaki T., et al. Quantification and cluster analysis of actin cytoskeletal structures in plant cells: role of actin bundling in stomatal movement during diurnal cycles in Arabidopsis guard cells. Plant J. 2010, 61:156-165.
    • (2010) Plant J. , vol.61 , pp. 156-165
    • Higaki, T.1
  • 47
    • 82755161219 scopus 로고    scopus 로고
    • Arabidopsis actin depolymerizing factor 4 modulates the stochastic dynamic behavior of actin filaments in the cortical array of epidermal cells
    • Henty J.L., et al. Arabidopsis actin depolymerizing factor 4 modulates the stochastic dynamic behavior of actin filaments in the cortical array of epidermal cells. Plant Cell 2011, 23:3711-3726.
    • (2011) Plant Cell , vol.23 , pp. 3711-3726
    • Henty, J.L.1
  • 48
    • 68949091932 scopus 로고    scopus 로고
    • Phosphatidic acid regulation of phosphatidylinositol 4-phosphate 5-kinases
    • Cockcroft S. Phosphatidic acid regulation of phosphatidylinositol 4-phosphate 5-kinases. Biochim. Biophys. Acta 2009, 1791:905-912.
    • (2009) Biochim. Biophys. Acta , vol.1791 , pp. 905-912
    • Cockcroft, S.1
  • 49
    • 20444362713 scopus 로고    scopus 로고
    • Characterization and comparative analysis of Arabidopsis phosphatidylinositol phosphate 5-kinase 10 reveals differences in Arabidopsis and human phosphatidylinositol phosphate kinases
    • Perera I.Y., et al. Characterization and comparative analysis of Arabidopsis phosphatidylinositol phosphate 5-kinase 10 reveals differences in Arabidopsis and human phosphatidylinositol phosphate kinases. FEBS Lett. 2005, 579:3427-3432.
    • (2005) FEBS Lett. , vol.579 , pp. 3427-3432
    • Perera, I.Y.1
  • 50
    • 0034695461 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion
    • Raucher D., et al. Phosphatidylinositol 4,5-bisphosphate functions as a second messenger that regulates cytoskeleton-plasma membrane adhesion. Cell 2000, 100:221-228.
    • (2000) Cell , vol.100 , pp. 221-228
    • Raucher, D.1
  • 51
    • 0036844844 scopus 로고    scopus 로고
    • Regulation of the pollen-specific actin-depolymerizing factor LlADF1
    • Allwood E.G., et al. Regulation of the pollen-specific actin-depolymerizing factor LlADF1. Plant Cell 2002, 14:2915-2927.
    • (2002) Plant Cell , vol.14 , pp. 2915-2927
    • Allwood, E.G.1
  • 52
    • 34547658952 scopus 로고    scopus 로고
    • ACTIN BINDING PROTEIN29 from Lilium pollen plays an important role in dynamic actin remodeling
    • Xiang Y., et al. ACTIN BINDING PROTEIN29 from Lilium pollen plays an important role in dynamic actin remodeling. Plant Cell 2007, 19:1930-1946.
    • (2007) Plant Cell , vol.19 , pp. 1930-1946
    • Xiang, Y.1
  • 53
    • 74949100104 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides
    • Saarikangas J., et al. Regulation of the actin cytoskeleton-plasma membrane interplay by phosphoinositides. Physiol. Rev. 2010, 90:259-289.
    • (2010) Physiol. Rev. , vol.90 , pp. 259-289
    • Saarikangas, J.1
  • 54
    • 0344417107 scopus 로고    scopus 로고
    • Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth
    • Kost B., et al. Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J. Cell Biol. 1999, 145:317-330.
    • (1999) J. Cell Biol. , vol.145 , pp. 317-330
    • Kost, B.1
  • 55
    • 34249662680 scopus 로고    scopus 로고
    • A novel ROP/RAC effector links cell polarity, root-meristem maintenance, and vesicle trafficking
    • Lavy M., et al. A novel ROP/RAC effector links cell polarity, root-meristem maintenance, and vesicle trafficking. Curr. Biol. 2007, 17:947-952.
    • (2007) Curr. Biol. , vol.17 , pp. 947-952
    • Lavy, M.1
  • 56
    • 79251560962 scopus 로고    scopus 로고
    • Phosphatidylinositol-4,5-bisphosphate influences Nt-Rac5-mediated cell expansion in pollen tubes of Nicotiana tabacum
    • Ischebeck T., et al. Phosphatidylinositol-4,5-bisphosphate influences Nt-Rac5-mediated cell expansion in pollen tubes of Nicotiana tabacum. Plant J. 2011, 65:453-468.
    • (2011) Plant J. , vol.65 , pp. 453-468
    • Ischebeck, T.1
  • 57
    • 79959926844 scopus 로고    scopus 로고
    • Rho proteins of plants - functional cycle and regulation of cytoskeletal dynamics
    • Mucha E., et al. Rho proteins of plants - functional cycle and regulation of cytoskeletal dynamics. Eur. J. Cell Biol. 2011, 90:934-943.
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 934-943
    • Mucha, E.1
  • 58
    • 84866111156 scopus 로고    scopus 로고
    • Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry breaking
    • Oda Y., Fukuda H. Initiation of cell wall pattern by a Rho- and microtubule-driven symmetry breaking. Science 2012, 337:1333-1336.
    • (2012) Science , vol.337 , pp. 1333-1336
    • Oda, Y.1    Fukuda, H.2
  • 59
    • 84883291358 scopus 로고    scopus 로고
    • Endocytic signaling in leaves and roots: same rules different players
    • Craddock C., Yang Z. Endocytic signaling in leaves and roots: same rules different players. Front. Plant Sci. 2012, 3:219.
    • (2012) Front. Plant Sci. , vol.3 , pp. 219
    • Craddock, C.1    Yang, Z.2
  • 60
    • 0344514831 scopus 로고    scopus 로고
    • Phospholipase D activation correlates with microtubule reorganization in living plant cells
    • Dhonukshe P., et al. Phospholipase D activation correlates with microtubule reorganization in living plant cells. Plant Cell 2003, 15:2666-2679.
    • (2003) Plant Cell , vol.15 , pp. 2666-2679
    • Dhonukshe, P.1
  • 61
    • 0041742201 scopus 로고    scopus 로고
    • The effects of the phospholipase D-antagonist 1-butanol on seedling development and microtubule organisation in Arabidopsis
    • Gardiner J., et al. The effects of the phospholipase D-antagonist 1-butanol on seedling development and microtubule organisation in Arabidopsis. Plant Cell Physiol. 2003, 44:687-696.
    • (2003) Plant Cell Physiol. , vol.44 , pp. 687-696
    • Gardiner, J.1
  • 62
  • 63
    • 33747819473 scopus 로고    scopus 로고
    • N-Butanol induces depolymerization of microtubules in vivo and in vitro
    • Hirase A., et al. n-Butanol induces depolymerization of microtubules in vivo and in vitro. Plant Cell Physiol. 2006, 47:1004-1009.
    • (2006) Plant Cell Physiol. , vol.47 , pp. 1004-1009
    • Hirase, A.1
  • 64
    • 84871910179 scopus 로고    scopus 로고
    • Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis
    • Zhang Q., et al. Phosphatidic acid regulates microtubule organization by interacting with MAP65-1 in response to salt stress in Arabidopsis. Plant Cell 2012, 24:4555-4576.
    • (2012) Plant Cell , vol.24 , pp. 4555-4576
    • Zhang, Q.1
  • 65
    • 33746826849 scopus 로고    scopus 로고
    • Macrotubule-dependent protoplast volume regulation in plasmolysed root-tip cells of Triticum turgidum: involvement of phospholipase D
    • Komis G., et al. Macrotubule-dependent protoplast volume regulation in plasmolysed root-tip cells of Triticum turgidum: involvement of phospholipase D. New Phytol. 2006, 171:737-750.
    • (2006) New Phytol. , vol.171 , pp. 737-750
    • Komis, G.1
  • 66
    • 0030452396 scopus 로고    scopus 로고
    • Isolation of a 90-kD microtubule-associated protein from tobacco membranes
    • Marc J., et al. Isolation of a 90-kD microtubule-associated protein from tobacco membranes. Plant Cell 1996, 8:2127-2138.
    • (1996) Plant Cell , vol.8 , pp. 2127-2138
    • Marc, J.1
  • 67
    • 0034802757 scopus 로고    scopus 로고
    • A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane
    • Gardiner J.C., et al. A 90-kD phospholipase D from tobacco binds to microtubules and the plasma membrane. Plant Cell 2001, 13:2143-2158.
    • (2001) Plant Cell , vol.13 , pp. 2143-2158
    • Gardiner, J.C.1
  • 68
    • 59849119837 scopus 로고    scopus 로고
    • Arabidopsis phospholipase Dδ as an initiator of cytoskeleton-mediated signalling to fundamental cellular processes
    • Ho A.Y.Y., et al. Arabidopsis phospholipase Dδ as an initiator of cytoskeleton-mediated signalling to fundamental cellular processes. Funct. Plant Biol. 2009, 36:190-198.
    • (2009) Funct. Plant Biol. , vol.36 , pp. 190-198
    • Ho, A.Y.Y.1
  • 69
    • 77950941733 scopus 로고    scopus 로고
    • Phospholipase D family interactions with the cytoskeleton: isoform δ promotes plasma membrane anchoring of cortical microtubules
    • Andreeva Z., et al. Phospholipase D family interactions with the cytoskeleton: isoform δ promotes plasma membrane anchoring of cortical microtubules. Funct. Plant Biol. 2009, 36:600-612.
    • (2009) Funct. Plant Biol. , vol.36 , pp. 600-612
    • Andreeva, Z.1
  • 70
    • 52649171957 scopus 로고    scopus 로고
    • Developmental reorientation of transverse cortical microtubules to longitudinal directions: a role for actomyosin-based streaming and partial microtubule-membrane detachment
    • Sainsbury F., et al. Developmental reorientation of transverse cortical microtubules to longitudinal directions: a role for actomyosin-based streaming and partial microtubule-membrane detachment. Plant J. 2008, 56:116-131.
    • (2008) Plant J. , vol.56 , pp. 116-131
    • Sainsbury, F.1
  • 71
    • 4043123335 scopus 로고    scopus 로고
    • The Arabidopsis microtubule-associated protein AtMAP65-1: molecular analysis of its microtubule bundling activity
    • Smertenko A.P., et al. The Arabidopsis microtubule-associated protein AtMAP65-1: molecular analysis of its microtubule bundling activity. Plant Cell 2004, 16:2035-2047.
    • (2004) Plant Cell , vol.16 , pp. 2035-2047
    • Smertenko, A.P.1
  • 72
    • 14744280248 scopus 로고    scopus 로고
    • In vivo dynamics and differential microtubule-binding activities of MAP65 proteins
    • Van Damme D., et al. In vivo dynamics and differential microtubule-binding activities of MAP65 proteins. Plant Physiol. 2004, 136:3956-3967.
    • (2004) Plant Physiol. , vol.136 , pp. 3956-3967
    • Van Damme, D.1
  • 73
    • 26944469613 scopus 로고    scopus 로고
    • Two microtubule-associated proteins of the Arabidopsis MAP65 family function differently on microtubules
    • Mao T., et al. Two microtubule-associated proteins of the Arabidopsis MAP65 family function differently on microtubules. Plant Physiol. 2005, 138:654-662.
    • (2005) Plant Physiol. , vol.138 , pp. 654-662
    • Mao, T.1
  • 74
    • 79959828598 scopus 로고    scopus 로고
    • Microtubule-associated proteins MAP65-1 and MAP65-2 positively regulate axial cell growth in etiolated Arabidopsis hypocotyls
    • Lucas J.R., et al. Microtubule-associated proteins MAP65-1 and MAP65-2 positively regulate axial cell growth in etiolated Arabidopsis hypocotyls. Plant Cell 2011, 23:1889-1903.
    • (2011) Plant Cell , vol.23 , pp. 1889-1903
    • Lucas, J.R.1
  • 75
    • 48249089753 scopus 로고    scopus 로고
    • Phospholipase Dα3 is involved in the hyperosmotic response in Arabidopsis
    • Hong Y., et al. Phospholipase Dα3 is involved in the hyperosmotic response in Arabidopsis. Plant Cell 2008, 20:803-816.
    • (2008) Plant Cell , vol.20 , pp. 803-816
    • Hong, Y.1
  • 76
    • 58449085005 scopus 로고    scopus 로고
    • Multiple PLDs required for high salinity and water deficit tolerance in plants
    • Bargmann B.O.R., et al. Multiple PLDs required for high salinity and water deficit tolerance in plants. Plant Cell Physiol. 2009, 50:78-89.
    • (2009) Plant Cell Physiol. , vol.50 , pp. 78-89
    • Bargmann, B.O.R.1
  • 77
    • 77958586850 scopus 로고    scopus 로고
    • Phosphatidic acid mediates salt stress response by regulation of MPK6 in Arabidopsis thaliana
    • Yu L., et al. Phosphatidic acid mediates salt stress response by regulation of MPK6 in Arabidopsis thaliana. New Phytol. 2010, 188:762-773.
    • (2010) New Phytol. , vol.188 , pp. 762-773
    • Yu, L.1
  • 78
    • 36248939596 scopus 로고    scopus 로고
    • Salt tolerance requires cortical microtubule reorganization in Arabidopsis
    • Wang C., et al. Salt tolerance requires cortical microtubule reorganization in Arabidopsis. Plant Cell Physiol. 2007, 48:1534-1547.
    • (2007) Plant Cell Physiol. , vol.48 , pp. 1534-1547
    • Wang, C.1
  • 79
    • 80055015202 scopus 로고    scopus 로고
    • Salt stress-induced disassembly of Arabidopsis cortical microtubule arrays involves 26S proteasome-dependent degradation of SPIRAL1
    • Wang S., et al. Salt stress-induced disassembly of Arabidopsis cortical microtubule arrays involves 26S proteasome-dependent degradation of SPIRAL1. Plant Cell 2011, 23:3412-3427.
    • (2011) Plant Cell , vol.23 , pp. 3412-3427
    • Wang, S.1
  • 80
    • 13544258103 scopus 로고    scopus 로고
    • Inhibition of muscarinic receptor-linked phospholipase D activation by association with tubulin
    • Chae Y.C., et al. Inhibition of muscarinic receptor-linked phospholipase D activation by association with tubulin. J. Biol. Chem. 2005, 280:3723-3730.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3723-3730
    • Chae, Y.C.1
  • 81
    • 33646061961 scopus 로고    scopus 로고
    • Signaling functions of phosphatidic acid
    • Wang X., et al. Signaling functions of phosphatidic acid. Prog. Lipid Res. 2006, 45:250-278.
    • (2006) Prog. Lipid Res. , vol.45 , pp. 250-278
    • Wang, X.1
  • 82
  • 83
    • 42149093290 scopus 로고    scopus 로고
    • Crossed-wires: interactions and cross-talk between the microtubule and microfilament networks in plants
    • Springer, P. Nick (Ed.)
    • Collings D.A. Crossed-wires: interactions and cross-talk between the microtubule and microfilament networks in plants. Plant Microtubules, Development and Flexibility 2008, 47-82. Springer. P. Nick (Ed.).
    • (2008) Plant Microtubules, Development and Flexibility , pp. 47-82
    • Collings, D.A.1
  • 84
    • 84864408366 scopus 로고    scopus 로고
    • Prieurianin/endosidin 1 is an actin stabilizing small molecule identified from chemical genetic screen for circadian clock effectors in Arabidopsis thaliana
    • Tóth R., et al. Prieurianin/endosidin 1 is an actin stabilizing small molecule identified from chemical genetic screen for circadian clock effectors in Arabidopsis thaliana. Plant J. 2012, 71:338-352.
    • (2012) Plant J. , vol.71 , pp. 338-352
    • Tóth, R.1
  • 85
    • 34248173036 scopus 로고    scopus 로고
    • Actin-filament stochastic dynamics mediated by ADF/cofilin
    • Michelot A., et al. Actin-filament stochastic dynamics mediated by ADF/cofilin. Curr. Biol. 2007, 17:825-833.
    • (2007) Curr. Biol. , vol.17 , pp. 825-833
    • Michelot, A.1
  • 86
    • 0029878720 scopus 로고    scopus 로고
    • VMD: visual molecular dynamics
    • Humphrey W., et al. VMD: visual molecular dynamics. J. Mol. Graph. 1996, 14:33-38.
    • (1996) J. Mol. Graph. , vol.14 , pp. 33-38
    • Humphrey, W.1
  • 87
    • 0036421146 scopus 로고    scopus 로고
    • Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle
    • Chen L.F., et al. Molecular modeling of averaged rigor crossbridges from tomograms of insect flight muscle. J. Struct. Biol. 2002, 138:92-104.
    • (2002) J. Struct. Biol. , vol.138 , pp. 92-104
    • Chen, L.F.1
  • 88
    • 77953221109 scopus 로고    scopus 로고
    • Practical modeling of molecular systems with symmetries
    • Grudinin S., Redon S. Practical modeling of molecular systems with symmetries. J. Comput. Chem. 2010, 31:1799-1814.
    • (2010) J. Comput. Chem. , vol.31 , pp. 1799-1814
    • Grudinin, S.1    Redon, S.2
  • 89
    • 39449115394 scopus 로고    scopus 로고
    • I-TASSER server for protein 3D structure prediction
    • Zhang Y. I-TASSER server for protein 3D structure prediction. BMC Bioinformatics 2008, 9:40.
    • (2008) BMC Bioinformatics , vol.9 , pp. 40
    • Zhang, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.