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Volumn 49, Issue 8, 2007, Pages 1183-1191

The villin/gelsolin/fragmin superfamily proteins in plants

Author keywords

Actin binding protein; Actincyto skeleton; Villin gelsolin fragmin

Indexed keywords

BIOCHEMISTRY; HOMOLOGY; PLANT; PROTEIN;

EID: 34547883183     PISSN: 16729072     EISSN: 17447909     Source Type: Journal    
DOI: 10.1111/j.1672-9072.2007.00546.x     Document Type: Review
Times cited : (19)

References (52)
  • 1
    • 0036721401 scopus 로고    scopus 로고
    • The epithelial cell cytoskeleton and intracellular trafficking: III. How villin is involved in the actin cytoskeleton dynamics in intestinal cells?
    • Athman R, Louvard D, Robine S (2002). The epithelial cell cytoskeleton and intracellular trafficking: III. How villin is involved in the actin cytoskeleton dynamics in intestinal cells? Am. J. Physiol. Gastrointest. Liver Physiol. 283, 496-502.
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.283 , pp. 496-502
    • Athman, R.1    Louvard, D.2    Robine, S.3
  • 2
    • 0030829385 scopus 로고    scopus 로고
    • The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation
    • Burtnick LD, Koepf EK, Grimes J, Jones EY, Stuart DI, McLaughlin PJ et al. (1997). The crystal structure of plasma gelsolin: Implications for actin severing, capping, and nucleation. Cell 90, 661-670.
    • (1997) Cell , vol.90 , pp. 661-670
    • Burtnick, L.D.1    Koepf, E.K.2    Grimes, J.3    Jones, E.Y.4    Stuart, D.I.5    McLaughlin, P.J.6
  • 3
    • 0027496510 scopus 로고
    • The drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in caenorhabditis elegans and humans
    • Campbell HD, Schimansky T, Claudianos C, Ozsarac N, Kasprzak AB, Cotsell JN et al. (1993). The drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in caenorhabditis elegans and humans. Proc. Natl. Acad. Sci. USA 90, 11386-11390.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11386-11390
    • Campbell, H.D.1    Schimansky, T.2    Claudianos, C.3    Ozsarac, N.4    Kasprzak, A.B.5    Cotsell, J.N.6
  • 4
    • 0036923313 scopus 로고    scopus 로고
    • The calcium activation of gelsolin: Insights from the 3A structure of the G4-G6/actin complex
    • Choe H, Burtnic LD, Mejillano M, Yin HL, Robinson RC, Choe S (2002). The calcium activation of gelsolin: Insights from the 3A structure of the G4-G6/actin complex. J. Mol. Biol. 324, 691-702.
    • (2002) J. Mol. Biol. , vol.324 , pp. 691-702
    • Choe, H.1    Burtnic, L.D.2    Mejillano, M.3    Yin, H.L.4    Robinson, R.C.5    Choe, S.6
  • 5
    • 0035399959 scopus 로고    scopus 로고
    • How is actin polymerization nucleated in vivo?
    • Condeelis J (2001). How is actin polymerization nucleated in vivo? Trends Cell Biol. 11, 288-93.
    • (2001) Trends Cell Biol. , vol.11 , pp. 288-293
    • Condeelis, J.1
  • 6
    • 0029843044 scopus 로고    scopus 로고
    • Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin-binding site and structural features of the domain
    • Doering DS, Matsudaira P (1996). Cysteine scanning mutagenesis at 40 of 76 positions in villin headpiece maps the F-actin-binding site and structural features of the domain. Biochemistry 35, 12677-12685.
    • (1996) Biochemistry , vol.35 , pp. 12677-12685
    • Doering, D.S.1    Matsudaira, P.2
  • 7
    • 0021136824 scopus 로고
    • Actin polymerization. The effect of brevin on filament size and rate of polymerization
    • Doi Y, Frieden C (1984). Actin polymerization. The effect of brevin on filament size and rate of polymerization. J. Biol. Chem. 259, 11868-11875.
    • (1984) J. Biol. Chem. , vol.259 , pp. 11868-11875
    • Doi, Y.1    Frieden, C.2
  • 9
    • 0034494327 scopus 로고    scopus 로고
    • Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins
    • Ebert F, Guillen N, Leippe M, Tannich E (2000). Molecular cloning and cellular localization of an unusual bipartite Entamoeba histolytica polypeptide with similarity to actin binding proteins. Mol. Biochem. Parasitol. 111, 459-464.
    • (2000) Mol. Biochem. Parasitol. , vol.111 , pp. 459-464
    • Ebert, F.1    Guillen, N.2    Leippe, M.3    Tannich, E.4
  • 11
    • 0034937550 scopus 로고    scopus 로고
    • Root hairs as a model system for studying plant cell growth
    • Foreman J, Dolan L (2001). Root hairs as a model system for studying plant cell growth. Ann. Bot. 88, 1-7.
    • (2001) Ann. Bot. , vol.88 , pp. 1-7
    • Foreman, J.1    Dolan, L.2
  • 12
    • 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
  • 13
    • 0020685135 scopus 로고
    • Ligand-induced conformational changes in villin, a calcium-controlled actin-modulating protein
    • Hesterberg LK, Weber K (1983). Ligand-induced conformational changes in villin, a calcium-controlled actin-modulating protein. J. Biol. Chem. 258, 359-364.
    • (1983) J. Biol. Chem. , vol.258 , pp. 359-364
    • Hesterberg, L.K.1    Weber, K.2
  • 14
    • 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
  • 15
    • 27244456193 scopus 로고    scopus 로고
    • Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization
    • Huang S, Robinson RC, Gao LY, Matsumoto T, Brunet A, Blanchoin L et al. (2005). Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization. Plant Cell 17, 486-501.
    • (2005) Plant Cell , vol.17 , pp. 486-501
    • Huang, S.1    Robinson, R.C.2    Gao, L.Y.3    Matsumoto, T.4    Brunet, A.5    Blanchoin, L.6
  • 16
    • 0023199043 scopus 로고
    • Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin
    • Janmey PA, Iida K, Yin HL, Stossel TP (1987). Polyphosphoinositide micelles and polyphosphoinositide-containing vesicles dissociate endogenous gelsolin-actin complexes and promote actin assembly from the fast-growing end of actin filaments blocked by gelsolin. J. Biol. Chem. 262, 12228-12236.
    • (1987) J. Biol. Chem. , vol.262 , pp. 12228-12236
    • Janmey, P.A.1    Iida, K.2    Yin, H.L.3    Stossel, T.P.4
  • 17
    • 33750029727 scopus 로고    scopus 로고
    • Evolutionary conservation and regulation of particular alternative splicing events in plant SR proteins
    • Kalyna M, Lopato S, Voronin V, Barta A (2006). Evolutionary conservation and regulation of particular alternative splicing events in plant SR proteins. Nucleic Acids Res. 34, 4395-4405.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4395-4405
    • Kalyna, M.1    Lopato, S.2    Voronin, V.3    Barta, A.4
  • 21
    • 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
  • 22
    • 1642576026 scopus 로고    scopus 로고
    • Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin
    • Kumar N, Zhao P, Tomar A, Galea CA, Khurana S (2004). Functional dissection and molecular characterization of calcium-sensitive actin-capping and actin-depolymerizing sites in villin. J. Biol.Chem. 279, 3096-3110.
    • (2004) J. Biol.Chem. , vol.279 , pp. 3096-3110
    • Kumar, N.1    Zhao, P.2    Tomar, A.3    Galea, C.A.4    Khurana, S.5
  • 23
    • 0026078290 scopus 로고
    • Domain structure in actin-binding proteins: Expression and functional characterization of truncated severin
    • Ludwig Eichinger, Angelika A, Noegel, Schleicher M (1991). Domain structure in actin-binding proteins: Expression and functional characterization of truncated severin. J. Cell Biol. 112, 665-676.
    • (1991) J. Cell Biol. , vol.112 , pp. 665-676
    • Eichinger, L.1    Noegel, A.A.2    Schleicher, M.3
  • 24
    • 0031879577 scopus 로고    scopus 로고
    • Determination of the gelsolin binding site on f-actin: Implications for severing and capping
    • McGough A, Chiu W, Way M (1998). Determination of the gelsolin binding site on f-actin: Implications for severing and capping. Biophys. J. 74, 764-772.
    • (1998) Biophys. J. , vol.74 , pp. 764-772
    • McGough, A.1    Chiu, W.2    Way, M.3
  • 25
    • 0141761142 scopus 로고    scopus 로고
    • The gelsolin family of actin regulatory proteins: Modular structures, versatile functions
    • McGough AM, Staiger CJ, Min JK, Simonetti KD (2003). The gelsolin family of actin regulatory proteins: Modular structures, versatile functions. FEBS Lett. 552, 75-81.
    • (2003) FEBS Lett. , vol.552 , pp. 75-81
    • McGough, A.M.1    Staiger, C.J.2    Min, J.K.3    Simonetti, K.D.4
  • 26
    • 0027251071 scopus 로고
    • Structure of gelsolin segment 1-actin complex and the mechanism of filament severing
    • McLaughlin PJ, Gooch JT, Mannherz HG, Weeds AG (1993). Structure of gelsolin segment 1-actin complex and the mechanism of filament severing. Nature 364, 685-692.
    • (1993) Nature , vol.364 , pp. 685-692
    • McLaughlin, P.J.1    Gooch, J.T.2    Mannherz, H.G.3    Weeds, A.G.4
  • 27
    • 21244441158 scopus 로고    scopus 로고
    • Identification of a villin-related tobacco protein as a novel cross-reactive plant allergen
    • Mittermann I, Voronin V, Heberle-Bors E, Valenta R (2005). Identification of a villin-related tobacco protein as a novel cross-reactive plant allergen. FEBS Lett. 579, 3807-3813.
    • (2005) FEBS Lett. , vol.579 , pp. 3807-3813
    • Mittermann, I.1    Voronin, V.2    Heberle-Bors, E.3    Valenta, R.4
  • 28
    • 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
  • 29
    • 0030831613 scopus 로고    scopus 로고
    • Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily
    • Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ (1997). Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. J. Biol.Chem. 139, 1255-1269.
    • (1997) J. Biol.Chem. , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 30
    • 0026089715 scopus 로고
    • Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. Implications of capping and severing mechanisms
    • Pope B, Way M, Weeds AG (1991). Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. Implications of capping and severing mechanisms. FEBS Lett. 280, 70-74.
    • (1991) FEBS Lett. , vol.280 , pp. 70-74
    • Pope, B.1    Way, M.2    Weeds, A.G.3
  • 35
    • 33751206848 scopus 로고    scopus 로고
    • Vesicular trafficking, cytoskeleton and signalling in root hairs and pollen tubes
    • Samaj J, Muller J, Beck M, Bohm N, Menzel D (2006). Vesicular trafficking, cytoskeleton and signalling in root hairs and pollen tubes. Trends Plant Sci. 11, 594-600.
    • (2006) Trends Plant Sci. , vol.11 , pp. 594-600
    • Samaj, J.1    Muller, J.2    Beck, M.3    Bohm, N.4    Menzel, D.5
  • 37
    • 33749860518 scopus 로고    scopus 로고
    • Actin dynamics: Old friends with new stories
    • Staiger CJ, Blanchoin L (2006). Actin dynamics: Old friends with new stories. Curr. Opin. Plant Biol. 9, 554-562.
    • (2006) Curr. Opin. Plant Biol. , vol.9 , pp. 554-562
    • Staiger, C.J.1    Blanchoin, L.2
  • 39
    • 0001027292 scopus 로고    scopus 로고
    • Gelsolin, a multi-functional actin regulatory protein
    • Sun HQ, Yamamoto M, Mejillano M, Yin HL (1999). Gelsolin, a multi-functional actin regulatory protein. J. Biol. Chem. 274, 3179-3182.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3179-3182
    • Sun, H.Q.1    Yamamoto, M.2    Mejillano, M.3    Yin, H.L.4
  • 40
    • 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
  • 41
    • 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
  • 42
    • 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
  • 43
    • 0033395843 scopus 로고    scopus 로고
    • The 135-kDa actin-bundling protein from Lilium longiflorum pollen is the plant homolog 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 homolog 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
  • 44
    • 0024318706 scopus 로고
    • Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis
    • Way M, Gooch J, Pope B, Weeds AG (1989). Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis. J. Cell Biol. 109, 593-605.
    • (1989) J. Cell Biol. , vol.109 , pp. 593-605
    • Way, M.1    Gooch, J.2    Pope, B.3    Weeds, A.G.4
  • 45
    • 33646484347 scopus 로고    scopus 로고
    • Genomewide comparative analysis of alternative splicing in plants
    • Wang BB, Brendel V (2006). Genomewide comparative analysis of alternative splicing in plants. Proc. Natl. Acad. Sci. USA 103, 7175-7180.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7175-7180
    • Wang, B.B.1    Brendel, V.2
  • 46
    • 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
  • 48
    • 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
  • 49
    • 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
  • 50
    • 0242569607 scopus 로고    scopus 로고
    • Plant 115-kDa actin-filament bundling protein, P-115-ABP, is a homolog of plant villin and widely distributed in cells
    • Yokota E, Vidali L, Tominaga M, Tahara H, Orii H, Morizane Y et al. (2003). Plant 115-kDa actin-filament bundling protein, P-115-ABP, is a homolog of plant villin and widely distributed in cells. Plant Cell Physiol. l44, 1088-1099.
    • (2003) Plant Cell Physiol. , vol.144 , pp. 1088-1099
    • Yokota, E.1    Vidali, L.2    Tominaga, M.3    Tahara, H.4    Orii, H.5    Morizane, Y.6
  • 52
    • 0026752622 scopus 로고
    • Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin
    • Yu FX, Sun HQ, Janmeyg PA, Ying HL (1992). Identification of a polyphosphoinositide-binding sequence in an actin monomer-binding domain of gelsolin. J. Biol. Chem. 267, 14616-14621.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14616-14621
    • Yu, F.X.1    Sun, H.Q.2    Janmeyg, P.A.3    Ying, H.L.4


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