메뉴 건너뛰기




Volumn 230, Issue 3-4, 2007, Pages 171-182

The function of actin-binding proteins in pollen tube growth

Author keywords

Actin cytoskeleton; Actin depolymerising factor; Formin; Pollen tube growth; Profilin; Villin gelsolin fragmin

Indexed keywords

ACTIN BINDING PROTEIN;

EID: 34247555357     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-006-0231-x     Document Type: Article
Times cited : (83)

References (125)
  • 1
    • 0035876055 scopus 로고    scopus 로고
    • Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase
    • Allwood EG, Smertenko AP, Hussey PJ (2001) Phosphorylation of plant actin-depolymerising factor by calmodulin-like domain protein kinase. FEBS Lett 499: 97-100
    • (2001) FEBS Lett , vol.499 , pp. 97-100
    • Allwood, E.G.1    Smertenko, A.P.2    Hussey, P.J.3
  • 3
    • 0023850804 scopus 로고
    • Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains
    • Andre E, Lottspeich F, Schleicher M, Noegel A (1988) Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains. J Biol Chem 263: 722-727
    • (1988) J Biol Chem , vol.263 , pp. 722-727
    • Andre, E.1    Lottspeich, F.2    Schleicher, M.3    Noegel, A.4
  • 4
    • 33645870695 scopus 로고    scopus 로고
    • Plant formins come of age: Something special about cross-walls
    • Baluška F, Hlavačka A (2005) Plant formins come of age: something special about cross-walls. New Phytol 168: 499-503
    • (2005) New Phytol , vol.168 , pp. 499-503
    • Baluška, F.1    Hlavačka, A.2
  • 5
    • 0034669149 scopus 로고    scopus 로고
    • Root hair formation: F-actin-dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges
    • Baluška F, Salaj J, Mathur J, Braun M, Jasper F, Samaj J, Chua NH, Barlow PW, Volkmann D (2000) Root hair formation: F-actin-dependent tip growth is initiated by local assembly of profilin-supported F-actin meshworks accumulated within expansin-enriched bulges. Dev Biol 227: 618-632
    • (2000) Dev Biol , vol.227 , pp. 618-632
    • Baluška, F.1    Salaj, J.2    Mathur, J.3    Braun, M.4    Jasper, F.5    Samaj, J.6    Chua, N.H.7    Barlow, P.W.8    Volkmann, D.9
  • 6
    • 0033280237 scopus 로고    scopus 로고
    • Proteins of the ADF/cofilin family: Essential regulators of actin dynamics
    • Bamburg JR (1999) Proteins of the ADF/cofilin family: essential regulators of actin dynamics. Annu Rev Cell Dev Biol 15: 185-230
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 185-230
    • Bamburg, J.R.1
  • 7
    • 0034121194 scopus 로고    scopus 로고
    • Characterization of the Arabidopsis formin-like protein AFH1 and its interacting protein
    • Banno H, Chua NH (2000) Characterization of the Arabidopsis formin-like protein AFH1 and its interacting protein. Plant Cell Physiol 41: 617-626
    • (2000) Plant Cell Physiol , vol.41 , pp. 617-626
    • Banno, H.1    Chua, N.H.2
  • 8
    • 26244433180 scopus 로고    scopus 로고
    • Basu D, Le J, El-Essal SEl-D, Huang S, Zhang C, Mallery EL, Koliantz G, Staiger CJ, Szymanski DB (2005) DISTORTED3/SCAR2 is a putative Arabidopsis WAVE complex subunit that activated the Arp2/3 complex and is required for epidermal morphogenesis. Plant Cell 17: 502-524
    • Basu D, Le J, El-Essal SEl-D, Huang S, Zhang C, Mallery EL, Koliantz G, Staiger CJ, Szymanski DB (2005) DISTORTED3/SCAR2 is a putative Arabidopsis WAVE complex subunit that activated the Arp2/3 complex and is required for epidermal morphogenesis. Plant Cell 17: 502-524
  • 9
    • 0039699925 scopus 로고    scopus 로고
    • Redistribution of actin, profilin and phosphatidylinositol-4,5-bisphosphate in growing and maturing root hairs
    • Braun M, Baluška F, von Witsch M, Menzel D (1999) Redistribution of actin, profilin and phosphatidylinositol-4,5-bisphosphate in growing and maturing root hairs. Planta 209: 435-443
    • (1999) Planta , vol.209 , pp. 435-443
    • Braun, M.1    Baluška, F.2    von Witsch, M.3    Menzel, D.4
  • 10
    • 0344975376 scopus 로고
    • Villin: The major microfilament-associated protein of the intestinal microvillus
    • Bretscher A, Weber K (1979) Villin: the major microfilament-associated protein of the intestinal microvillus. Proc Natl Acad Sci USA 76: 2321-2325
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 2321-2325
    • Bretscher, A.1    Weber, K.2
  • 11
    • 19944396800 scopus 로고    scopus 로고
    • Actin polymerization promotes the reversal of streaming in the apex of pollen tubes
    • Cardenas L, Lovy-Wheeler A,Wilsen KL, Hepler PK (2005) Actin polymerization promotes the reversal of streaming in the apex of pollen tubes. Cell Motil Cytoskeleton 61: 112-127
    • (2005) Cell Motil Cytoskeleton , vol.61 , pp. 112-127
    • Cardenas, L.1    Lovy-Wheeler, A.2    Wilsen, K.L.3    Hepler, P.K.4
  • 12
    • 0031580210 scopus 로고    scopus 로고
    • Control of actin dynamics in cell motility
    • Carlier MF, Pantaloni D (1997) Control of actin dynamics in cell motility. J Mol Biol 269: 459-467
    • (1997) J Mol Biol , vol.269 , pp. 459-467
    • Carlier, M.F.1    Pantaloni, D.2
  • 14
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson L, Nystrom LE, Sundkvist I, Markey F, Lindberg U (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J Mol Biol 115: 465-483
    • (1977) J Mol Biol , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 15
    • 0028053435 scopus 로고
    • Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene
    • Castrillon D, Wassermann S (1994) Diaphanous is required for cytokinesis in Drosophila and shares domains of similarity with the products of the limb deformity gene. Development 120: 3367-3377
    • (1994) Development , vol.120 , pp. 3367-3377
    • Castrillon, D.1    Wassermann, S.2
  • 16
    • 0036741550 scopus 로고    scopus 로고
    • The regulation of actin organization by actin depolymerizing factor in elongating pollen tubes
    • Chen CY, Wong EI, Vidali L, Estavillo A, Hepler PK, Wu HM, Cheung AY (2002) The regulation of actin organization by actin depolymerizing factor in elongating pollen tubes. Plant Cell 14: 2175-2190
    • (2002) Plant Cell , vol.14 , pp. 2175-2190
    • Chen, C.Y.1    Wong, E.I.2    Vidali, L.3    Estavillo, A.4    Hepler, P.K.5    Wu, H.M.6    Cheung, A.Y.7
  • 17
    • 0037256774 scopus 로고    scopus 로고
    • Actin-depolymerizing factor mediates Rac/Rop GTPase-regulated pollen tube growth
    • Chen CYH, Cheung AY, Wu HM (2003) Actin-depolymerizing factor mediates Rac/Rop GTPase-regulated pollen tube growth. Plant Cell 15: 237-249
    • (2003) Plant Cell , vol.15 , pp. 237-249
    • Chen, C.Y.H.1    Cheung, A.Y.2    Wu, H.M.3
  • 18
    • 0842291746 scopus 로고    scopus 로고
    • Overexpression of an Arabidopsis formin stimulates supernumerary actin cable formation from pollen tube cell membrane
    • Cheung AY, Wu HM (2004) Overexpression of an Arabidopsis formin stimulates supernumerary actin cable formation from pollen tube cell membrane. Plant Cell 16: 257-269
    • (2004) Plant Cell , vol.16 , pp. 257-269
    • Cheung, A.Y.1    Wu, H.M.2
  • 20
    • 0033648030 scopus 로고    scopus 로고
    • Cvrčková F (2000) Are plant formins integral membrane proteins? Genome Biol 1: research001
    • Cvrčková F (2000) Are plant formins integral membrane proteins? Genome Biol 1: research001
  • 21
    • 9444255105 scopus 로고    scopus 로고
    • Formin homology 2 domains occur in multiple contexts in angiosperms
    • Cvrčková F, Novotný M, Picková D, Žarský V (2004) Formin homology 2 domains occur in multiple contexts in angiosperms. BMC Genomics 5: 44
    • (2004) BMC Genomics , vol.5 , pp. 44
    • Cvrčková, F.1    Novotný, M.2    Picková, D.3    Žarský, V.4
  • 22
    • 0036835889 scopus 로고    scopus 로고
    • Formins: Intermediates in signal-transduction cascades that affect cytoskeletal reorganization
    • Deeks MJ, Hussey PJ, Davies B (2002) Formins: intermediates in signal-transduction cascades that affect cytoskeletal reorganization. Trends Plant Sci 7: 1360-1385
    • (2002) Trends Plant Sci , vol.7 , pp. 1360-1385
    • Deeks, M.J.1    Hussey, P.J.2    Davies, B.3
  • 23
    • 33645864068 scopus 로고    scopus 로고
    • Arabidopsis group I formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression
    • Deeks MJ, Cvrčková F, Machesky LM, Mikitová V, Ketelaar T, Žarský V, Davies B, Hussey PJ (2005) Arabidopsis group I formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression. New Phytol 168: 529-540
    • (2005) New Phytol , vol.168 , pp. 529-540
    • Deeks, M.J.1    Cvrčková, F.2    Machesky, L.M.3    Mikitová, V.4    Ketelaar, T.5    Žarský, V.6    Davies, B.7    Hussey, P.J.8
  • 25
    • 33645731661 scopus 로고    scopus 로고
    • BRICK1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabidopsis
    • Djakovic S, Dyachok J, Burke M, Frank MJ, Smith LG (2006) BRICK1/HSPC300 functions with SCAR and the ARP2/3 complex to regulate epidermal cell shape in Arabidopsis. Development 133: 1091-1100
    • (2006) Development , vol.133 , pp. 1091-1100
    • Djakovic, S.1    Dyachok, J.2    Burke, M.3    Frank, M.J.4    Smith, L.G.5
  • 26
    • 0028105664 scopus 로고
    • Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin
    • Drøbak BK, Watkins PAC, Valenta R, Dove SK, Lloyd CW, Staiger CJ (1994) Inhibition of plant plasma membrane phosphoinositide phospholipase C by the actin-binding protein, profilin. Plant J 6: 389-400
    • (1994) Plant J , vol.6 , pp. 389-400
    • Drøbak, B.K.1    Watkins, P.A.C.2    Valenta, R.3    Dove, S.K.4    Lloyd, C.W.5    Staiger, C.J.6
  • 28
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A (2002) Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 4: 32-41
    • (2002) Nat Cell Biol , vol.4 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 29
    • 0038445654 scopus 로고    scopus 로고
    • Formins: Signaling effectors for assembly and polarization of actin filaments
    • Evangelista M, Zigmond S, Boone C (2003) Formins: signaling effectors for assembly and polarization of actin filaments. J Cell Sci 116: 2603-2611
    • (2003) J Cell Sci , vol.116 , pp. 2603-2611
    • Evangelista, M.1    Zigmond, S.2    Boone, C.3
  • 32
    • 0035975991 scopus 로고    scopus 로고
    • Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division
    • Feierbach B, Chang F (2001) Roles of the fission yeast formin for3p in cell polarity, actin cable formation and symmetric cell division. Curr Biol 11: 1656-1665
    • (2001) Curr Biol , vol.11 , pp. 1656-1665
    • Feierbach, B.1    Chang, F.2
  • 33
    • 0033535048 scopus 로고    scopus 로고
    • Growing pollen tubes possess a constitutive alkaline band in the clear zone and a growth-dependent acidic tip
    • Feijó JA, Sainhas J, Hackett GR, Kunkel JG, Hepler PK (1999) Growing pollen tubes possess a constitutive alkaline band in the clear zone and a growth-dependent acidic tip. J Cell Biol 144: 483-496
    • (1999) J Cell Biol , vol.144 , pp. 483-496
    • Feijó, J.A.1    Sainhas, J.2    Hackett, G.R.3    Kunkel, J.G.4    Hepler, P.K.5
  • 34
    • 0033006993 scopus 로고    scopus 로고
    • Cytokinesis in eukaryotes: A mechanistic comparison
    • Field C, Li R, Oegema K (1999) Cytokinesis in eukaryotes: a mechanistic comparison. Curr Opin Cell Biol 11: 68-90
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 68-90
    • Field, C.1    Li, R.2    Oegema, K.3
  • 35
    • 9244240976 scopus 로고    scopus 로고
    • Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVE
    • Frank M, Egile C, Dyachok J, Djakovic S, Nolasco M, Li R, Smith LC (2004) Activation of Arp2/3 complex-dependent actin polymerization by plant proteins distantly related to Scar/WAVE. Proc Natl Acad Sci USA 101: 16379-16384
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16379-16384
    • Frank, M.1    Egile, C.2    Dyachok, J.3    Djakovic, S.4    Nolasco, M.5    Li, R.6    Smith, L.C.7
  • 36
    • 0032698958 scopus 로고    scopus 로고
    • Signaling and the modulation of pollen tube growth
    • Franklin-Tong VE (1999) Signaling and the modulation of pollen tube growth. Plant cell 11: 727-738
    • (1999) Plant cell , vol.11 , pp. 727-738
    • Franklin-Tong, V.E.1
  • 38
    • 0035809915 scopus 로고    scopus 로고
    • GTPase dependent dynamics of tip localized F-actin controls tip growth in pollen tubes
    • Fu Y, Wu G, Yang Z (2001) GTPase dependent dynamics of tip localized F-actin controls tip growth in pollen tubes. J Cell Biol 152: 1019-1032
    • (2001) J Cell Biol , vol.152 , pp. 1019-1032
    • Fu, Y.1    Wu, G.2    Yang, Z.3
  • 39
    • 0034095607 scopus 로고    scopus 로고
    • The cytoskeleton in plant and fungal cell tip growth
    • Geitmann A, Emons AM (2000) The cytoskeleton in plant and fungal cell tip growth. J Microsc 198: 218-245
    • (2000) J Microsc , vol.198 , pp. 218-245
    • Geitmann, A.1    Emons, A.M.2
  • 40
  • 41
    • 0033397748 scopus 로고    scopus 로고
    • Latrunculin B has different effects on pollen germination and tube growth
    • Gibbon BC, Kovar DR, Staiger CJ (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
  • 42
    • 0019088749 scopus 로고
    • Calcium control of the intestinal microvillus cytoskeleton: Its implications for the regulation of microfilament organizations
    • Glenney JR, Bretscher A,Weber K (1980) Calcium control of the intestinal microvillus cytoskeleton: its implications for the regulation of microfilament organizations. Proc Natl Acad Sci USA 77: 6458-6462
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 6458-6462
    • Glenney, J.R.1    Bretscher, A.2    Weber, K.3
  • 44
    • 0032443967 scopus 로고    scopus 로고
    • Interaction of maize actin-depolymerising factor with actin and phosphoinositides and its inhibition of plant phospholipase C
    • Gungabissoon RA, Jiang C-J, Drøbak BK, Maciver SK, Hussey PJ (1998) Interaction of maize actin-depolymerising factor with actin and phosphoinositides and its inhibition of plant phospholipase C. Plant J 16: 689-696
    • (1998) Plant J , vol.16 , pp. 689-696
    • Gungabissoon, R.A.1    Jiang, C.-J.2    Drøbak, B.K.3    Maciver, S.K.4    Hussey, P.J.5
  • 45
    • 0027439319 scopus 로고
    • Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
    • Hawkins M, Pope B, Maciver SK, Weeds AG (1993) Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments. Biochemistry 32: 9985-9993
    • (1993) Biochemistry , vol.32 , pp. 9985-9993
    • Hawkins, M.1    Pope, B.2    Maciver, S.K.3    Weeds, A.G.4
  • 46
    • 0027494863 scopus 로고
    • Analysis of the interactions of actin depolymerizing factor with G- and F-actin
    • Hayden SM, Miller PS, Brauweiler A, Bamburg JR (1993) Analysis of the interactions of actin depolymerizing factor with G- and F-actin. Biochemistry 32: 9994-10004
    • (1993) Biochemistry , vol.32 , pp. 9994-10004
    • Hayden, S.M.1    Miller, P.S.2    Brauweiler, A.3    Bamburg, J.R.4
  • 49
    • 0030771772 scopus 로고    scopus 로고
    • Profilin revealed in pollen nuclei: Immunoelectron microscopy of high-pressure frozen Ledebouria socialis Roth (Hyacinthaceae)
    • Hess MW, Valenta R (1997) Profilin revealed in pollen nuclei: immunoelectron microscopy of high-pressure frozen Ledebouria socialis Roth (Hyacinthaceae). Sex Plant Reprod 10: 283-287
    • (1997) Sex Plant Reprod , vol.10 , pp. 283-287
    • Hess, M.W.1    Valenta, R.2
  • 50
    • 0030138167 scopus 로고    scopus 로고
    • The Arabidopis 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 Arabidopis 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
  • 51
    • 2542452087 scopus 로고    scopus 로고
    • A gelsolin-like protein from Papaver rhoeas pollen (PrABP80) stimulates calcium-regulated severing and depolymerization of actin filaments
    • Huang S, Blanchoin L, Chaudhry F, Franklin-Tong VE, Staiger CJ (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
    • (2004) J Biol Chem , vol.279 , pp. 23364-23375
    • Huang, S.1    Blanchoin, L.2    Chaudhry, F.3    Franklin-Tong, V.E.4    Staiger, C.J.5
  • 53
    • 27644538028 scopus 로고    scopus 로고
    • Oscillatory ROP GTPase activation leads the oscillatory polarized growth of pollen tubes
    • Hwang JU, Gu Ying, Lee YJ, Yang Z (2005) Oscillatory ROP GTPase activation leads the oscillatory polarized growth of pollen tubes. Mol Biol Cell 16: 5385-5399
    • (2005) Mol Biol Cell , vol.16 , pp. 5385-5399
    • Hwang, J.U.1    Ying, G.2    Lee, Y.J.3    Yang, Z.4
  • 56
    • 0033197668 scopus 로고    scopus 로고
    • The Arabidopsis actin-related protein2 (AtARP2) promoter directs expression in xylem precursor cells and pollen
    • Klahre U, Chua NH (1999) The Arabidopsis actin-related protein2 (AtARP2) promoter directs expression in xylem precursor cells and pollen. Plant Mol Biol 41: 65-73
    • (1999) Plant Mol Biol , vol.41 , pp. 65-73
    • Klahre, U.1    Chua, N.H.2
  • 57
    • 0033759043 scopus 로고    scopus 로고
    • Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis
    • Klahre U, Friederich E, Kost B, Louvard D, Chua NH (2000) Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis. Plant Physiol 122: 35-47
    • (2000) Plant Physiol , vol.122 , pp. 35-47
    • Klahre, U.1    Friederich, E.2    Kost, B.3    Louvard, D.4    Chua, N.H.5
  • 58
    • 0032213954 scopus 로고    scopus 로고
    • A GFP-mouse talin fusion protein labels plant actin filaments in vivo and visualizes the actin cytoskeleton in growing pollen tubes
    • Kost B, Spielhofer P, Chua NH (1998) A GFP-mouse talin fusion protein labels plant actin filaments in vivo and visualizes the actin cytoskeleton in growing pollen tubes. Plant J 16: 393-401
    • (1998) Plant J , vol.16 , pp. 393-401
    • Kost, B.1    Spielhofer, P.2    Chua, N.H.3
  • 59
    • 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, Lemichez E, Spielhofer P, Hong Y, Tolias K, Carpenter C, Chua NH (1999) Rac homologues and compartmentalized phosphatidylinositol 4,5-bisphosphate act in a common pathway to regulate polar pollen tube growth. J Cell Biol 145: 317-330
    • (1999) J Cell Biol , vol.145 , pp. 317-330
    • Kost, B.1    Lemichez, E.2    Spielhofer, P.3    Hong, Y.4    Tolias, K.5    Carpenter, C.6    Chua, N.H.7
  • 60
    • 0034067715 scopus 로고    scopus 로고
    • Maize profilin isoforms are functionally distinct
    • Kovar DR, Drøbak BK, Staiger CJ (2000) Maize profilin isoforms are functionally distinct. Plant Cell 12: 583-598
    • (2000) Plant Cell , vol.12 , pp. 583-598
    • Kovar, D.R.1    Drøbak, B.K.2    Staiger, C.J.3
  • 61
    • 0035882162 scopus 로고    scopus 로고
    • The characterization of ligand-specific maize (Zea mays) profilin mutants
    • Kovar DR, Drøbak BK, Collings DA, Staiger CJ (2001) The characterization of ligand-specific maize (Zea mays) profilin mutants. Biochem J 358: 49-57
    • (2001) Biochem J , vol.358 , pp. 49-57
    • Kovar, D.R.1    Drøbak, B.K.2    Collings, D.A.3    Staiger, C.J.4
  • 62
    • 0022487183 scopus 로고
    • Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain
    • Kwiatkowski DJ, Stossel TP, Orkin SH, Mole JE, Colten HR, Yin HL (1986) Plasma and cytoplasmic gelsolins are encoded by a single gene and contain a duplicated actin-binding domain. Nature 323: 455-458
    • (1986) Nature , vol.323 , pp. 455-458
    • Kwiatkowski, D.J.1    Stossel, T.P.2    Orkin, S.H.3    Mole, J.E.4    Colten, H.R.5    Yin, H.L.6
  • 63
    • 0043202969 scopus 로고    scopus 로고
    • The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F, Higgs HN (2003) The mouse formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13: 1335-1340
    • (2003) Curr Biol , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 64
    • 0043011658 scopus 로고    scopus 로고
    • The putative Arabidopsis Arp2/3 complex controls leaf cell morphogenesis
    • Li S, Blanchoin L, Yang Z, Lord EM (2003) The putative Arabidopsis Arp2/3 complex controls leaf cell morphogenesis. Plant Physiol 132: 2034-2044
    • (2003) Plant Physiol , vol.132 , pp. 2034-2044
    • Li, S.1    Blanchoin, L.2    Yang, Z.3    Lord, E.M.4
  • 65
    • 0034794331 scopus 로고    scopus 로고
    • Circular F-actin bundles and a G-actin gradient in pollen and pollen tubes of Lilium davidii
    • Li Y, Zee S-Y, Liu Y-M, Huang B-Q, Yen L-F (2001) Circular F-actin bundles and a G-actin gradient in pollen and pollen tubes of Lilium davidii. Planta 213: 722-730
    • (2001) Planta , vol.213 , pp. 722-730
    • Li, Y.1    Zee, S.-Y.2    Liu, Y.-M.3    Huang, B.-Q.4    Yen, L.-F.5
  • 68
    • 18044372483 scopus 로고    scopus 로고
    • Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube
    • Lovy-Wheeler A, Wilsen KL, Baskin TI, Hepler PK (2005) Enhanced fixation reveals the apical cortical fringe of actin filaments as a consistent feature of the pollen tube. Planta 221: 95-104
    • (2005) Planta , vol.221 , pp. 95-104
    • Lovy-Wheeler, A.1    Wilsen, K.L.2    Baskin, T.I.3    Hepler, P.K.4
  • 69
    • 0035163855 scopus 로고    scopus 로고
    • Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast
    • Lu J, Pollard TD (2001) Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol Biol Cell 12: 1161-1175
    • (2001) Mol Biol Cell , vol.12 , pp. 1161-1175
    • Lu, J.1    Pollard, T.D.2
  • 70
    • 0030707797 scopus 로고    scopus 로고
    • Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous
    • Lynch ED, Lee MK, Morrow JE, Welcsh PL, León PE, King MC (1997) Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science 278: 1315-1318
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1    Lee, M.K.2    Morrow, J.E.3    Welcsh, P.L.4    León, P.E.5    King, M.C.6
  • 71
    • 0036264824 scopus 로고    scopus 로고
    • Maciver SK, Hussey PJ (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3: reviews3007
    • Maciver SK, Hussey PJ (2002) The ADF/cofilin family: actin-remodeling proteins. Genome Biol 3: reviews3007
  • 72
    • 17844390343 scopus 로고    scopus 로고
    • The ARP2/3 complex: Giving plant cells a leading edge
    • Mathur J (2005) The ARP2/3 complex: giving plant cells a leading edge. BioEssays 27: 377-387
    • (2005) BioEssays , vol.27 , pp. 377-387
    • Mathur, J.1
  • 73
    • 0018578513 scopus 로고
    • Identification and organization of the components in the isolated microvillus cytoskeleton
    • Matsudaira PT, Burgess DR (1979) Identification and organization of the components in the isolated microvillus cytoskeleton. J Cell Biol 83: 667-673
    • (1979) J Cell Biol , vol.83 , pp. 667-673
    • Matsudaira, P.T.1    Burgess, D.R.2
  • 74
    • 0033588258 scopus 로고    scopus 로고
    • ADF/cofilin weakens lateral contacts in the actin filament
    • McGough A, Chiu W (1999) ADF/cofilin weakens lateral contacts in the actin filament. J Mol Biol 291: 513-519
    • (1999) J Mol Biol , vol.291 , pp. 513-519
    • McGough, A.1    Chiu, W.2
  • 75
    • 1942454810 scopus 로고    scopus 로고
    • Profilin inhibits pollen tube growth through actin-binding, but not poly-L-proline-binding
    • McKenna ST, Vidali L, Hepler PK (2004) Profilin inhibits pollen tube growth through actin-binding, but not poly-L-proline-binding. Planta 218: 906-915
    • (2004) Planta , vol.218 , pp. 906-915
    • McKenna, S.T.1    Vidali, L.2    Hepler, P.K.3
  • 76
    • 0036006050 scopus 로고    scopus 로고
    • Arabidopsis contains ancient classes of differentially expressed actin related protein genes
    • McKinney EC, Kandasamy MK, Meagher RB (2002) Arabidopsis contains ancient classes of differentially expressed actin related protein genes. Plant Physiol 128: 997-1007
    • (2002) Plant Physiol , vol.128 , pp. 997-1007
    • McKinney, E.C.1    Kandasamy, M.K.2    Meagher, R.B.3
  • 79
    • 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
  • 80
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with Gactin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mockrin SC, Korn ED (1980) Acanthamoeba profilin interacts with Gactin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry 19: 5359-5362
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 82
    • 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
  • 84
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin beta 4
    • Pantaloni D, Carlier MF (1993) How profilin promotes actin filament assembly in the presence of thymosin beta 4. Cell 75: 1007-1014
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 85
    • 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
  • 86
    • 0036909561 scopus 로고    scopus 로고
    • Structure and function of the Arp2/3 complex
    • Pollard TD, Beltzner CC (2002) Structure and function of the Arp2/3 complex. Curr Opin Struct Biol 12: 768-774
    • (2002) Curr Opin Struct Biol , vol.12 , pp. 768-774
    • Pollard, T.D.1    Beltzner, C.C.2
  • 87
    • 0021766640 scopus 로고
    • Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation
    • Pollard TD, Cooper JA (1984) Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation. Biochemistry 23: 6631-6641
    • (1984) Biochemistry , vol.23 , pp. 6631-6641
    • Pollard, T.D.1    Cooper, J.A.2
  • 90
    • 0029263357 scopus 로고
    • A Zea mays pollen cDNA encoding a putative actin-depolymerizing factor
    • Rozycka M, Khan S, Lopez I, Greenland AJ, Hussey PJ (1995) A Zea mays pollen cDNA encoding a putative actin-depolymerizing factor. Plant Physiol 107: 1011-1012
    • (1995) Plant Physiol , vol.107 , pp. 1011-1012
    • Rozycka, M.1    Khan, S.2    Lopez, I.3    Greenland, A.J.4    Hussey, P.J.5
  • 91
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot I, Klee SK, Pellman D (2002a) Yeast formins regulate cell polarity by controlling the assembly of actin cables. Nat Cell Biol 4: 42-50
    • (2002) Nat Cell Biol , vol.4 , pp. 42-50
    • Sagot, I.1    Klee, S.K.2    Pellman, D.3
  • 93
    • 0024231233 scopus 로고
    • Actin-binding proteins are conserved from slime molds to man
    • Schleicher M, Andre E, Hartmann H, Noegel AA (1988) Actin-binding proteins are conserved from slime molds to man. Dev Genet 9: 521-530
    • (1988) Dev Genet , vol.9 , pp. 521-530
    • Schleicher, M.1    Andre, E.2    Hartmann, H.3    Noegel, A.A.4
  • 94
    • 0032053115 scopus 로고    scopus 로고
    • Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity
    • Smertenko AP, Jiang CJ, Simmons NJ, Weeds AG, Dersavies DR, Hussey PJ (1998) Ser6 in the maize actin-depolymerizing factor, ZmADF3, is phosphorylated by a calcium-stimulated protein kinase and is essential for the control of functional activity. Plant J 14: 187-194
    • (1998) Plant J , vol.14 , pp. 187-194
    • Smertenko, A.P.1    Jiang, C.J.2    Simmons, N.J.3    Weeds, A.G.4    Dersavies, D.R.5    Hussey, P.J.6
  • 97
    • 0036801753 scopus 로고    scopus 로고
    • Signal-mediated depolymerization of actin in pollen during the self-incompatibility response
    • Snowman BN, Kovar DR, Shevchenko G, Franklin-Tong VE, Staiger CJ (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
  • 98
  • 101
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multifunctional actin regulatory protein
    • Sun HQ, Yamamoto M, Mejillano M, Yin HL (1999) Gelsolin, a multifunctional actin regulatory protein. J Biol Chem 274: 33179-33182
    • (1999) J Biol Chem , vol.274 , pp. 33179-33182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 102
    • 11844299718 scopus 로고    scopus 로고
    • Breaking the WAVE complex: The point of Arabidopsis trichomes
    • Szymanski DB (2005) Breaking the WAVE complex: the point of Arabidopsis trichomes. Curr Opin Plant Biol 8: 1-10
    • (2005) Curr Opin Plant Biol , vol.8 , pp. 1-10
    • Szymanski, D.B.1
  • 103
    • 33544459386 scopus 로고    scopus 로고
    • Regulation of gelsolin to plant actin filaments and its distribution on pollen
    • Tao Z, Ren H (2003) Regulation of gelsolin to plant actin filaments and its distribution on pollen. Sci China 46: 379-388
    • (2003) Sci China , vol.46 , pp. 379-388
    • Tao, Z.1    Ren, H.2
  • 105
    • 0034020244 scopus 로고    scopus 로고
    • The role of plant villin in the organization of the actin cytoskeleton, cytoplasmic streaming and the architecture of the transvacuolar strand in root hair cells of Hydrocharis
    • Tominaga M, Yokota E, Vidali L, Sonobe S, Hepler PK, Shimmen T (2000) The role of plant villin in the organization of the actin cytoskeleton, cytoplasmic streaming and the architecture of the transvacuolar strand in root hair cells of Hydrocharis. Planta 210: 836-843
    • (2000) Planta , vol.210 , pp. 836-843
    • Tominaga, M.1    Yokota, E.2    Vidali, L.3    Sonobe, S.4    Hepler, P.K.5    Shimmen, T.6
  • 106
    • 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 Cytoskeleton 36: 323-338
    • (1997) Cell Motil Cytoskeleton , vol.36 , pp. 323-338
    • Vidali, L.1    Hepler, P.K.2
  • 107
    • 0035047583 scopus 로고    scopus 로고
    • Actin and pollen tube growth
    • Vidali L, Hepler PK (2001) Actin and pollen tube growth. Protoplasma 215: 64-76
    • (2001) Protoplasma , vol.215 , pp. 64-76
    • Vidali, L.1    Hepler, P.K.2
  • 108
    • 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
  • 109
    • 0032415374 scopus 로고    scopus 로고
    • Profilin is associated with the plasma membrane in microspores and pollen
    • von Witsch M, BalusÇka F, Staiger CJ, Volkmann D (1998) Profilin is associated with the plasma membrane in microspores and pollen. Eur J Cell Biol 77: 303-312
    • (1998) Eur J Cell Biol , vol.77 , pp. 303-312
    • von Witsch, M.1    BalusÇka, F.2    Staiger, C.J.3    Volkmann, D.4
  • 110
    • 0025007616 scopus 로고
    • Formins': Proteins deduced from the alternative transcripts of the limb deformity gene
    • Woychik RP, Maas RL, Zeller R, Vogt TF, Leder P (1990) 'Formins': proteins deduced from the alternative transcripts of the limb deformity gene. Nature 346: 850-853
    • (1990) Nature , vol.346 , pp. 850-853
    • Woychik, R.P.1    Maas, R.L.2    Zeller, R.3    Vogt, T.F.4    Leder, P.5
  • 111
    • 33646755630 scopus 로고    scopus 로고
    • Identification of gelsolin by western blotting in maize pollen
    • Wu W, Yan LF (1997) Identification of gelsolin by western blotting in maize pollen. Chin Sci Bull 42: 1784-1786
    • (1997) Chin Sci Bull , vol.42 , pp. 1784-1786
    • Wu, W.1    Yan, L.F.2
  • 112
    • 33749666297 scopus 로고    scopus 로고
    • Dynamic organization of actin cytoskeleton during the polarity formation and germination of pollen protoplasts
    • Xu X, Zi H, Sun Y, Ren H (2004) Dynamic organization of actin cytoskeleton during the polarity formation and germination of pollen protoplasts. Chin Sci Bull 16: 1702-1706
    • (2004) Chin Sci Bull , vol.16 , pp. 1702-1706
    • Xu, X.1    Zi, H.2    Sun, Y.3    Ren, H.4
  • 113
  • 114
    • 0036304481 scopus 로고    scopus 로고
    • Determining the differences in actin binding by human ADF and cofilin
    • Yeoh S, Pope B, Mannherz HG, Weeds A (2002) Determining the differences in actin binding by human ADF and cofilin. J Mol Biol 315: 911-925
    • (2002) J Mol Biol , vol.315 , pp. 911-925
    • Yeoh, S.1    Pope, B.2    Mannherz, H.G.3    Weeds, A.4
  • 115
    • 26944466154 scopus 로고    scopus 로고
    • Cloning and functional characterization of a formin-like protein (AtFH8) from Arabidopsis
    • Yi K, Guo C, Chen D, Zhao B, Yang B, Ren H (2005) Cloning and functional characterization of a formin-like protein (AtFH8) from Arabidopsis. Plant Physiol 138: 1071-1082
    • (2005) Plant Physiol , vol.138 , pp. 1071-1082
    • Yi, K.1    Guo, C.2    Chen, D.3    Zhao, B.4    Yang, B.5    Ren, H.6
  • 117
    • 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
  • 118
    • 0002417240 scopus 로고    scopus 로고
    • Characterization of native actin-binding proteins from pollen. Myosin and the actin-binding proteins, 135-ABP and 115-ABP
    • Staiger CJ, Baluška F, Volkmann D, Barlow P eds, Kluwer Academic, Dordrecht, pp
    • Yokota E, Shimmen T (2000) Characterization of native actin-binding proteins from pollen. Myosin and the actin-binding proteins, 135-ABP and 115-ABP. In: Staiger CJ, Baluška F, Volkmann D, Barlow P (eds) Actin: a dynamic framework for multiple plant cell functions. Kluwer Academic, Dordrecht, pp 103-118
    • (2000) Actin: A dynamic framework for multiple plant cell functions , pp. 103-118
    • Yokota, E.1    Shimmen, T.2
  • 119
    • 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
  • 122
    • 0022403777 scopus 로고
    • pH control of actin polymerization by cofilin
    • Yonezawa N, Nishida E, Sakai H (1985) pH control of actin polymerization by cofilin. J Biol Chem 260: 14410-14412
    • (1985) J Biol Chem , vol.260 , pp. 14410-14412
    • Yonezawa, N.1    Nishida, E.2    Sakai, H.3
  • 123
    • 0025277362 scopus 로고
    • Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides
    • Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H (1990) Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 265: 8382-8386
    • (1990) J Biol Chem , vol.265 , pp. 8382-8386
    • Yonezawa, N.1    Nishida, E.2    Iida, K.3    Yahara, I.4    Sakai, H.5
  • 124
    • 0025651999 scopus 로고
    • gCap39, a calcium ionand polyphosphoinositide-regulated actin capping protein
    • Yu FX, Johnston PA, Sudhof TC, Yin HL (1990) gCap39, a calcium ionand polyphosphoinositide-regulated actin capping protein. Science 250: 1413-1415
    • (1990) Science , vol.250 , pp. 1413-1415
    • Yu, F.X.1    Johnston, P.A.2    Sudhof, T.C.3    Yin, H.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.