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Volumn 70, Issue 11, 2013, Pages 775-795

The expanding superfamily of gelsolin homology domain proteins

Author keywords

Actin; Flightless; Gelsolin; Supervillin; Villin

Indexed keywords

ACTIN; COFILIN; DALTEPARIN; GELSOLIN; VILLIN;

EID: 84888139863     PISSN: 19493584     EISSN: 19493592     Source Type: Journal    
DOI: 10.1002/cm.21149     Document Type: Article
Times cited : (38)

References (64)
  • 2
    • 0023661298 scopus 로고
    • The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin
    • Ampe C, Vandekerckhove J. 1987. The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin. EMBO J 6:4149-4157.
    • (1987) EMBO J , vol.6 , pp. 4149-4157
    • Ampe, C.1    Vandekerckhove, J.2
  • 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
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • Arabidopsis Genome Initiative
    • Arabidopsis Genome Initiative. 2000. Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 408:796-815.
    • (2000) Nature , vol.408 , pp. 796-815
  • 6
    • 70349785050 scopus 로고    scopus 로고
    • How to arm a supervillin: designing F-actin binding activity into supervillin headpiece
    • Brown JW, Vardar-Ulu D, McKnight CJ. 2009. How to arm a supervillin: designing F-actin binding activity into supervillin headpiece. J Mol Biol 393:608-618.
    • (2009) J Mol Biol , vol.393 , pp. 608-618
    • Brown, J.W.1    Vardar-Ulu, D.2    McKnight, C.J.3
  • 8
    • 3543012019 scopus 로고    scopus 로고
    • Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF
    • Burtnick LD, Urosev D, Irobi E, Narayan K, Robinson RC. 2004. Structure of the N-terminal half of gelsolin bound to actin: roles in severing, apoptosis and FAF. EMBO J 23:2713-2722.
    • (2004) EMBO J , vol.23 , pp. 2713-2722
    • Burtnick, L.D.1    Urosev, D.2    Irobi, E.3    Narayan, K.4    Robinson, R.C.5
  • 9
    • 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, Young IG, de Couet HG, Miklos GL. 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    Young, I.G.7    de Couet, H.G.8    Miklos, G.L.9
  • 10
    • 0031570341 scopus 로고    scopus 로고
    • Genomic structure, evolution, and expression of human FLII, a gelsolin and leucine-rich-repeat family member: overlap with LLGL
    • Campbell HD, Fountain S, Young IG, Claudianos C, Hoheisel JD, Chen KS, Lupski JR. 1997. Genomic structure, evolution, and expression of human FLII, a gelsolin and leucine-rich-repeat family member: overlap with LLGL. Genomics 42:46-54.
    • (1997) Genomics , vol.42 , pp. 46-54
    • Campbell, H.D.1    Fountain, S.2    Young, I.G.3    Claudianos, C.4    Hoheisel, J.D.5    Chen, K.S.6    Lupski, J.R.7
  • 11
    • 0036923313 scopus 로고    scopus 로고
    • The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex
    • Choe H, Burtnick 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    Burtnick, L.D.2    Mejillano, M.3    Yin, H.L.4    Robinson, R.C.5    Choe, S.6
  • 13
    • 0028898938 scopus 로고
    • The novel flightless-I gene brings together two gene families, actin-binding proteins related to gelsolin and leucine-rich-repeat proteins involved in Ras signal transduction
    • Claudianos C, Campbell HD. 1995. The novel flightless-I gene brings together two gene families, actin-binding proteins related to gelsolin and leucine-rich-repeat proteins involved in Ras signal transduction. Mol Biol Evol 12:405-414.
    • (1995) Mol Biol Evol , vol.12 , pp. 405-414
    • Claudianos, C.1    Campbell, H.D.2
  • 17
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar RC. 2004. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 18
    • 34548839356 scopus 로고    scopus 로고
    • Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders
    • George SP, Wang Y, Mathew S, Srinivasan K, Khurana S. 2007. Dimerization and actin-bundling properties of villin and its role in the assembly of epithelial cell brush borders. J Biol Chem 282:26528-26541.
    • (2007) J Biol Chem , vol.282 , pp. 26528-26541
    • George, S.P.1    Wang, Y.2    Mathew, S.3    Srinivasan, K.4    Khurana, S.5
  • 19
    • 0038446802 scopus 로고    scopus 로고
    • Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton
    • Gloss A, Rivero F, Khaire N, Muller R, Loomis WF, Schleicher M, Noegel AA. 2003. Villidin, a novel WD-repeat and villin-related protein from Dictyostelium, is associated with membranes and the cytoskeleton. Mol Biol Cell 14:2716-2727.
    • (2003) Mol Biol Cell , vol.14 , pp. 2716-2727
    • Gloss, A.1    Rivero, F.2    Khaire, N.3    Muller, R.4    Loomis, W.F.5    Schleicher, M.6    Noegel, A.A.7
  • 20
    • 74549125386 scopus 로고    scopus 로고
    • SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building
    • Gouy M, Guindon S, Gascuel O. 2010. SeaView version 4: A multiplatform graphical user interface for sequence alignment and phylogenetic tree building. Mol Biol Evol 27:221-224.
    • (2010) Mol Biol Evol , vol.27 , pp. 221-224
    • Gouy, M.1    Guindon, S.2    Gascuel, O.3
  • 23
    • 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
  • 26
    • 0141426434 scopus 로고    scopus 로고
    • From the first to the second domain of gelsolin: a common path on the surface of actin?
    • Irobi E, Burtnick LD, Urosev D, Narayan K, Robinson RC. 2003. From the first to the second domain of gelsolin: a common path on the surface of actin? FEBS Lett 552:86-90.
    • (2003) FEBS Lett , vol.552 , pp. 86-90
    • Irobi, E.1    Burtnick, L.D.2    Urosev, D.3    Narayan, K.4    Robinson, R.C.5
  • 27
    • 0031588601 scopus 로고    scopus 로고
    • Sequence analysis of a 685-kb genomic region on chromosome 3p22-p21.3 that is homozygously deleted in a lung carcinoma cell line
    • Ishikawa S, Kai M, Tamari M, Takei Y, Takeuchi K, Bandou H, Yamane Y, Ogawa M, Nakamura Y. 1997. Sequence analysis of a 685-kb genomic region on chromosome 3p22-p21.3 that is homozygously deleted in a lung carcinoma cell line. DNA Res 4:35-43.
    • (1997) DNA Res , vol.4 , pp. 35-43
    • Ishikawa, S.1    Kai, M.2    Tamari, M.3    Takei, Y.4    Takeuchi, K.5    Bandou, H.6    Yamane, Y.7    Ogawa, M.8    Nakamura, Y.9
  • 28
    • 35248829189 scopus 로고    scopus 로고
    • Duplicated gelsolin family genes in zebrafish: a novel scinderin-like gene (scinla) encodes the major corneal crystallin
    • Jia S, Omelchenko M, Garland D, Vasiliou V, Kanungo J, Spencer M, Wolf Y, Koonin E, Piatigorsky J. 2007. Duplicated gelsolin family genes in zebrafish: a novel scinderin-like gene (scinla) encodes the major corneal crystallin. Faseb J 21:3318-3328.
    • (2007) Faseb J , vol.21 , pp. 3318-3328
    • Jia, S.1    Omelchenko, M.2    Garland, D.3    Vasiliou, V.4    Kanungo, J.5    Spencer, M.6    Wolf, Y.7    Koonin, E.8    Piatigorsky, J.9
  • 29
    • 0037051973 scopus 로고    scopus 로고
    • Der f 16: a novel gelsolin-related molecule identified as an allergen from the house dust mite, Dermatophagoides farinae
    • Kawamoto S, Suzuki T, Aki T, Katsutani T, Tsuboi S, Shigeta S, Ono K. 2002. Der f 16: a novel gelsolin-related molecule identified as an allergen from the house dust mite, Dermatophagoides farinae. FEBS Lett 516:234-238.
    • (2002) FEBS Lett , vol.516 , pp. 234-238
    • Kawamoto, S.1    Suzuki, T.2    Aki, T.3    Katsutani, T.4    Tsuboi, S.5    Shigeta, S.6    Ono, K.7
  • 30
    • 54449085163 scopus 로고    scopus 로고
    • Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats
    • Klaavuniemi T, Yamashiro S, Ono S. 2008. Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats. J Biol Chem 283:26071-26080.
    • (2008) J Biol Chem , vol.283 , pp. 26071-26080
    • Klaavuniemi, T.1    Yamashiro, S.2    Ono, S.3
  • 31
    • 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 122:35-48.
    • (2000) Plant Physiol , vol.122 , pp. 35-48
    • Klahre, U.1    Friederich, E.2    Kost, B.3    Louvard, D.4    Chua, N.H.5
  • 32
    • 0037693763 scopus 로고    scopus 로고
    • Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions
    • Kolappan S, Gooch JT, Weeds AG, McLaughlin PJ. 2003. Gelsolin domains 4-6 in active, actin-free conformation identifies sites of regulatory calcium ions. J Mol Biol 329:85-92.
    • (2003) J Mol Biol , vol.329 , pp. 85-92
    • Kolappan, S.1    Gooch, J.T.2    Weeds, A.G.3    McLaughlin, P.J.4
  • 33
    • 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
  • 34
    • 33845873289 scopus 로고    scopus 로고
    • Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation
    • Letunic I, Bork P. 2007. Interactive Tree Of Life (iTOL): an online tool for phylogenetic tree display and annotation. Bioinformatics 23:127-128.
    • (2007) Bioinformatics , vol.23 , pp. 127-128
    • Letunic, I.1    Bork, P.2
  • 35
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: recent updates to the protein domain annotation resource
    • Letunic I, Doerks T, Bork P. 2012. SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res 40:D302-D305.
    • (2012) Nucleic Acids Res , vol.40
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 36
    • 0031667298 scopus 로고    scopus 로고
    • Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins
    • Marks PW, Arai M, Bandura JL, Kwiatkowski DJ. 1998. Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins. J Cell Sci 111 (Pt 15):2129-2136.
    • (1998) J Cell Sci 111 (Pt , vol.15 , pp. 2129-2136
    • Marks, P.W.1    Arai, M.2    Bandura, J.L.3    Kwiatkowski, D.J.4
  • 37
    • 0030954481 scopus 로고    scopus 로고
    • Refined structure of villin 14T and a detailed comparison with other actin-severing domains
    • Markus MA, Matsudaira P, Wagner G. 1997. Refined structure of villin 14T and a detailed comparison with other actin-severing domains. Protein Sci 6:1197-1209.
    • (1997) Protein Sci , vol.6 , pp. 1197-1209
    • Markus, M.A.1    Matsudaira, P.2    Wagner, G.3
  • 38
    • 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
  • 39
    • 0028116599 scopus 로고
    • The human actin-regulatory protein cap G: gene structure and chromosome location
    • Mishra VS, Henske EP, Kwiatkowski DJ, Southwick FS. 1994. The human actin-regulatory protein cap G: gene structure and chromosome location. Genomics 23:560-565.
    • (1994) Genomics , vol.23 , pp. 560-565
    • Mishra, V.S.1    Henske, E.P.2    Kwiatkowski, D.J.3    Southwick, F.S.4
  • 42
    • 0028142460 scopus 로고
    • Differential expression of bovine adseverin in adrenal gland revealed by in situ hybridization
    • Nakamura S, Sakurai T, Nonomura Y. 1994. Differential expression of bovine adseverin in adrenal gland revealed by in situ hybridization. Cloning of a cDNA for adseverin. J Biol Chem 269:5890-5896.
    • (1994) Cloning of a cDNA for adseverin. J Biol Chem , vol.269 , pp. 5890-5896
    • Nakamura, S.1    Sakurai, T.2    Nonomura, Y.3
  • 44
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame C, Higgins DG, Heringa J. 2000. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J Mol Biol 302:205-217.
    • (2000) J Mol Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 45
    • 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 Cell Biol 139:1255-1269.
    • (1997) J Cell Biol , vol.139 , pp. 1255-1269
    • Pestonjamasp, K.N.1    Pope, R.K.2    Wulfkuhle, J.D.3    Luna, E.J.4
  • 46
    • 0026079365 scopus 로고
    • Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo
    • Prendergast GC, Ziff EB. 1991. Mbh 1: a novel gelsolin/severin-related protein which binds actin in vitro and exhibits nuclear localization in vivo. Embo J 10:757-766.
    • (1991) Embo J , vol.10 , pp. 757-766
    • Prendergast, G.C.1    Ziff, E.B.2
  • 47
    • 77949718257 scopus 로고    scopus 로고
    • FastTree 2-approximately maximum-likelihood trees for large alignments
    • Price MN, Dehal PS, Arkin AP. 2010. FastTree 2-approximately maximum-likelihood trees for large alignments. PLoS One 5:e9490.
    • (2010) PLoS One , vol.5
    • Price, M.N.1    Dehal, P.S.2    Arkin, A.P.3
  • 48
    • 84859436530 scopus 로고    scopus 로고
    • NCBI Reference Sequences (RefSeq): current status, new features and genome annotation policy
    • Pruitt KD, Tatusova T, Brown GR, Maglott DR. 2012. NCBI Reference Sequences (RefSeq): current status, new features and genome annotation policy. Nucleic Acids Res 40:D130-D135.
    • (2012) Nucleic Acids Res , vol.40
    • Pruitt, K.D.1    Tatusova, T.2    Brown, G.R.3    Maglott, D.R.4
  • 51
    • 34248176797 scopus 로고    scopus 로고
    • Mechanisms of COPII vesicle formation and protein sorting
    • Sato K, Nakano A. 2007. Mechanisms of COPII vesicle formation and protein sorting. FEBS Lett 581:2076-2082.
    • (2007) FEBS Lett , vol.581 , pp. 2076-2082
    • Sato, K.1    Nakano, A.2
  • 54
    • 0032951301 scopus 로고    scopus 로고
    • Phototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein
    • Stocker S, Hiery M, Marriott G. 1999. Phototactic migration of Dictyostelium cells is linked to a new type of gelsolin-related protein. Mol Biol Cell 10:161-178.
    • (1999) Mol Biol Cell , vol.10 , pp. 161-178
    • Stocker, S.1    Hiery, M.2    Marriott, G.3
  • 55
    • 0035868754 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis
    • Ulm R, Revenkova E, di Sansebastiano GP, Bechtold N, Paszkowski J. 2001. Mitogen-activated protein kinase phosphatase is required for genotoxic stress relief in Arabidopsis. Genes Dev 15:699-709.
    • (2001) Genes Dev , vol.15 , pp. 699-709
    • Ulm, R.1    Revenkova, E.2    di Sansebastiano, G.P.3    Bechtold, N.4    Paszkowski, J.5
  • 56
    • 0033579417 scopus 로고    scopus 로고
    • NMR structure of an F-actin-binding "headpiece" motif from villin
    • Vardar D, Buckley DA, Frank BS, McKnight CJ. 1999. NMR structure of an F-actin-binding "headpiece" motif from villin. J Mol Biol 294:1299-1310.
    • (1999) J Mol Biol , vol.294 , pp. 1299-1310
    • Vardar, D.1    Buckley, D.A.2    Frank, B.S.3    McKnight, C.J.4
  • 60
    • 0024293322 scopus 로고
    • Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats
    • Way M, Weeds A. 1988. Nucleotide sequence of pig plasma gelsolin. Comparison of protein sequence with human gelsolin and other actin-severing proteins shows strong homologies and evidence for large internal repeats. J Mol Biol 203:1127-1133.
    • (1988) J Mol Biol , vol.203 , pp. 1127-1133
    • Way, M.1    Weeds, A.2
  • 62
    • 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 PJ, 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
  • 63
    • 0025651999 scopus 로고
    • gCap39, a calcium ion- and polyphosphoinositide-regulated actin capping protein
    • Yu FX, Johnston PA, Sudhof TC, Yin HL. 1990. gCap39, a calcium ion- and 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


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