메뉴 건너뛰기




Volumn 224, Issue 3, 2011, Pages 289-300

The roles of fascins in health and disease

Author keywords

actin; dendritic cell; filopodia; metastasis; microRNA; migration; neuron; photoreceptor; podosome; signalling; stereocilia

Indexed keywords

FASCIN; FASCIN 1; FASCIN 2; FASCIN 3; UNCLASSIFIED DRUG;

EID: 80955177507     PISSN: 00223417     EISSN: 10969896     Source Type: Journal    
DOI: 10.1002/path.2894     Document Type: Review
Times cited : (164)

References (116)
  • 1
    • 0034612995 scopus 로고    scopus 로고
    • Identification of distant homologues of fibroblast growth factors suggests a common ancestor for all beta-trefoil proteins
    • Ponting CP, Russell RB,. Identification of distant homologues of fibroblast growth factors suggests a common ancestor for all beta-trefoil proteins. J Mol Biol 2000; 302: 1041-1047.
    • (2000) J Mol Biol , vol.302 , pp. 1041-1047
    • Ponting, C.P.1    Russell, R.B.2
  • 2
    • 77954386574 scopus 로고    scopus 로고
    • Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein
    • Sedeh RS, Fedorov AA, Fedorov EV, et al., Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein. J Mol Biol 2010; 400: 589-604.
    • (2010) J Mol Biol , vol.400 , pp. 589-604
    • Sedeh, R.S.1    Fedorov, A.A.2    Fedorov, E.V.3
  • 3
    • 0029760018 scopus 로고    scopus 로고
    • Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch
    • DOI 10.1021/bi960789j
    • Hanakam F, Gerisch G, Lotz S, et al., Binding of hisactophilin I and II to lipid membranes is controlled by a pH-dependent myristoyl-histidine switch. Biochemistry 1996; 35: 11036-11044. (Pubitemid 26301166)
    • (1996) Biochemistry , vol.35 , Issue.34 , pp. 11036-11044
    • Hanakam, F.1    Gerisch, G.2    Lotz, S.3    Alt, T.4    Seelig, A.5
  • 5
    • 0142073731 scopus 로고    scopus 로고
    • Interaction of fascin and protein kinase Cα: A novel intersection in cell adhesion and motility
    • DOI 10.1093/emboj/cdg521
    • Anilkumar N, Parsons M, Monk R, et al., Interaction of fascin and protein kinase Cα: a novel intersection in cell adhesion and motility. EMBO J 2003; 22: 5390-5402. (Pubitemid 37279949)
    • (2003) EMBO Journal , vol.22 , Issue.20 , pp. 5390-5402
    • Anilkumar, N.1    Parsons, M.2    Monk, R.3    Ng, T.4    Adams, J.C.5
  • 7
    • 53349097707 scopus 로고    scopus 로고
    • Rac regulates the interaction of fascin with protein kinase C in cell migration
    • Parsons M, Adams JC,. Rac regulates the interaction of fascin with protein kinase C in cell migration. J Cell Sci 2008; 121: 2805-2813.
    • (2008) J Cell Sci , vol.121 , pp. 2805-2813
    • Parsons, M.1    Adams, J.C.2
  • 8
    • 0034655939 scopus 로고    scopus 로고
    • Characterization of human retinal fascin gene (FSCN2) at 17q25: Close physical linkage of fascin and cytoplasmic actin genes
    • DOI 10.1006/geno.2000.6156
    • Tubb BE, Bardien-Kruger S, Kashork CD, et al., Characterization of human retinal fascin gene (FSCN2) at 17q25: close physical linkage of fascin and cytoplasmic actin genes. Genomics 2000; 65: 146-156. (Pubitemid 30314422)
    • (2000) Genomics , vol.65 , Issue.2 , pp. 146-156
    • Tubb, B.E.1    Bardien-Kruger, S.2    Kashork, C.D.3    Shaffer, L.G.4    Ramagli, L.S.5    Xu, J.6    Siciliano, M.J.7    Bryan, J.8
  • 9
    • 0016537752 scopus 로고
    • Preparation and purification of polymerized actin from sea urchin egg extracts
    • Kane RE,. Preparation and purification of polymerized actin from sea urchin egg extracts. J Cell Biol 1975; 66: 305-315.
    • (1975) J Cell Biol , vol.66 , pp. 305-315
    • Kane, R.E.1
  • 10
    • 0018805959 scopus 로고
    • UBER DIE 'MALABSORPTIVE' DERMATITIS HERPETIFORMIS DUHRING. EINE KATAMNESTISCHE STUDIE UNTER BESONDERER BERUCKSICHTIGUNG DUNNDARM-BIOPTISCHER BEFUNDE
    • Otto HF, Sack J, Gebbers JO, et al., 'Malabsorptive' dermatitis herpetiformis. A study with particular regard to biopsy findings of the small intestine (author's translation). Virchows Arch A Pathol Anat Histol 1979; 383: 195-206. (Pubitemid 9223445)
    • (1979) Virchows Archiv - Abteilung A Pathologische Anatomie , vol.383 , Issue.2 , pp. 195-206
    • Otto, H.F.1    Sack, J.2    Gebbers, J.O.3
  • 11
    • 0019260574 scopus 로고
    • Redistribution of actin and fascin in sea urchin eggs after fertilization
    • Otto JJ, Kane RE, Bryan J,. Redistribution of actin and fascin in sea urchin eggs after fertilization. Cell Motil 1980; 1: 31-40. (Pubitemid 12233332)
    • (1980) Cell Motility , vol.1 , Issue.1 , pp. 31-40
    • Otto, J.J.1    Kane, R.E.2    Bryan, J.3
  • 12
    • 0023447718 scopus 로고
    • Comparison of a major heat-stable microtubule-associated protein in HeLa cells and 190-kDa microtubule-associated protein in bovine adrenal cortex
    • Murofushi H, Kotani S, Aizawa H, et al., Comparison of a major heat-stable microtubule-associated protein in HeLa cells and 190-kDa microtubule-associated protein in bovine adrenal cortex. J Biochem 1987; 102: 1101-1112.
    • (1987) J Biochem , vol.102 , pp. 1101-1112
    • Murofushi, H.1    Kotani, S.2    Aizawa, H.3
  • 13
    • 0026331943 scopus 로고
    • Structure and transcription of the singed locus of Drosophila melanogaster
    • Paterson J, O'Hare K,. Structure and transcription of the singed locus of Drosophila melanogaster. Genetics 1991; 129: 1073-1084.
    • (1991) Genetics , vol.129 , pp. 1073-1084
    • Paterson, J.1    O'Hare, K.2
  • 14
    • 0028269631 scopus 로고
    • Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension
    • Cant K, Knowles BA, Mooseker MS, et al., Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J Cell Biol 1994; 125: 369-380. (Pubitemid 24135950)
    • (1994) Journal of Cell Biology , vol.125 , Issue.2 , pp. 369-380
    • Cant, K.1    Knowles, B.A.2    Mooseker, M.S.3    Cooley, L.4
  • 15
    • 33748283557 scopus 로고    scopus 로고
    • Phenotypes of Drosophila brain neurons in primary culture reveal a role for fascin in neurite shape and trajectory
    • DOI 10.1523/JNEUROSCI.2106-06.2006
    • Kraft R, Escobar MM, Narro ML, et al., Phenotypes of Drosophila brain neurons in primary culture reveal a role for fascin in neurite shape and trajectory. J Neurosci 2006; 26: 8734-8747. (Pubitemid 44319409)
    • (2006) Journal of Neuroscience , vol.26 , Issue.34 , pp. 8734-8747
    • Kraft, R.1    Escobar, M.M.2    Narro, M.L.3    Kurtis, J.L.4    Efrat, A.5    Barnard, K.6    Restifo, L.L.7
  • 16
    • 69049098975 scopus 로고    scopus 로고
    • Fascin is required for blood cell migration during Drosophila embryogenesis
    • Zanet J, Stramer B, Millard T, et al., Fascin is required for blood cell migration during Drosophila embryogenesis. Development 2009; 136: 2557-2565.
    • (2009) Development , vol.136 , pp. 2557-2565
    • Zanet, J.1    Stramer, B.2    Millard, T.3
  • 17
    • 35848929056 scopus 로고    scopus 로고
    • Roles for Drosophila melanogaster myosin IB in maintenance of enterocyte brush-border structure and resistance to the bacterial pathogen Pseudomonas entomophila
    • DOI 10.1091/mbc.E07-02-0191
    • Hegan PS, Mermall V, Tilney LG, et al., Roles for Drosophila melanogaster myosin IB in maintenance of enterocyte brush-border structure and resistance to the bacterial pathogen Pseudomonas entomophila. Mol Biol Cell 2007; 18: 4625-4636. (Pubitemid 350060187)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4625-4636
    • Hegan, P.S.1    Mermall, V.2    Tilney, L.G.3    Mooseker, M.S.4
  • 18
    • 48749116068 scopus 로고    scopus 로고
    • Proper cellular reorganization during Drosophila spermatid individualization depends on actin structures composed of two domains, bundles and meshwork, that are differentially regulated and have different functions
    • Noguchi T, Lenartowska M, Rogat AD, et al., Proper cellular reorganization during Drosophila spermatid individualization depends on actin structures composed of two domains, bundles and meshwork, that are differentially regulated and have different functions. Mol Biol Cell 2008; 19: 2363-2372.
    • (2008) Mol Biol Cell , vol.19 , pp. 2363-2372
    • Noguchi, T.1    Lenartowska, M.2    Rogat, A.D.3
  • 19
    • 4744355682 scopus 로고    scopus 로고
    • Expression of fascin-1, the gene encoding the actin-bundling protein fascin-1, during mouse embryogenesis
    • DOI 10.1016/j.modgep.2004.04.012, PII S1567133X04000687
    • De Arcangelis A, Georges-Labouesse E, Adams JC,. Expression of fascin-1, the gene encoding the actin-bundling protein fascin-1, during mouse embryogenesis. Gene Expr Patterns 2004; 4: 637-643. (Pubitemid 39307527)
    • (2004) Gene Expression Patterns , vol.4 , Issue.6 , pp. 637-643
    • De Arcangelis, A.1    Georges-Labouesse, E.2    Adams, J.C.3
  • 20
    • 38649099381 scopus 로고    scopus 로고
    • Fascin expression in human embryonic, fetal, and normal adult tissue
    • Zhang FR, Tao LH, Shen ZY, et al., Fascin expression in human embryonic, fetal, and normal adult tissue. J Histochem Cytochem 2008; 56: 193-199.
    • (2008) J Histochem Cytochem , vol.56 , pp. 193-199
    • Zhang, F.R.1    Tao, L.H.2    Shen, Z.Y.3
  • 21
    • 67749096260 scopus 로고    scopus 로고
    • Fascin1 is dispensable for mouse development but is favorable for neonatal survival
    • Yamakita Y, Matsumura F, Yamashiro S,. Fascin1 is dispensable for mouse development but is favorable for neonatal survival. Cell Motil Cytoskeleton 2009; 66: 524-534.
    • (2009) Cell Motil Cytoskeleton , vol.66 , pp. 524-534
    • Yamakita, Y.1    Matsumura, F.2    Yamashiro, S.3
  • 22
    • 0035140487 scopus 로고    scopus 로고
    • Role of the actin bundling protein fascin in growth cone morphogenesis: Localization in filopodia and lamellipodia
    • DOI 10.1002/10 97-016 9(2001 02)48:2<1 09::AID-CM1 002>3.0.CO;2-G
    • Cohan CS, Welnhofer EA, Zhao L, et al., Role of the actin bundling protein fascin in growth cone morphogenesis: localization in filopodia and lamellipodia. Cell Motil Cytoskeleton 2001; 48: 109-120. (Pubitemid 32116358)
    • (2001) Cell Motility and the Cytoskeleton , vol.48 , Issue.2 , pp. 109-120
    • Cohan, C.S.1    Welnhofer, E.A.2    Zhao, L.3    Matsumura, F.4    Yamashiro, S.5
  • 23
    • 0034698675 scopus 로고    scopus 로고
    • Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42
    • DOI 10.1083/jcb.150.4.807
    • Adams JC, Schwartz MA,. Stimulation of fascin spikes by thrombospondin-1 is mediated by the GTPases Rac and Cdc42. J Cell Biol 2000; 150: 807-822. (Pubitemid 30663417)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 807-822
    • Adams, J.C.1    Schwartz, M.A.2
  • 24
    • 67651211499 scopus 로고    scopus 로고
    • Disruption of the cytoskeleton during Semaphorin 3A induced growth cone collapse correlates with differences in actin organization and associated binding proteins
    • Brown JA, Bridgman PC,. Disruption of the cytoskeleton during Semaphorin 3A induced growth cone collapse correlates with differences in actin organization and associated binding proteins. Dev Neurobiol 2009; 69: 633-646.
    • (2009) Dev Neurobiol , vol.69 , pp. 633-646
    • Brown, J.A.1    Bridgman, P.C.2
  • 26
    • 0032522837 scopus 로고    scopus 로고
    • The actin-bundling protein fascin is involved in the formation of dendritic processes in maturing epidermal Langerhans cells
    • Ross R, Ross XL, Schwing J, et al., The actin-bundling protein fascin is involved in the formation of dendritic processes in maturing epidermal Langerhans cells. J Immunol 1998; 160: 3776-3782. (Pubitemid 28176080)
    • (1998) Journal of Immunology , vol.160 , Issue.8 , pp. 3776-3782
    • Ross, R.1    Ross, X.-L.2    Schwing, J.3    Langin, T.4    Reske-Kunz, A.B.5
  • 27
    • 0033778649 scopus 로고    scopus 로고
    • Expression of the actin-bundling protein fascin in cultured human dendritic cells correlates with dendritic morphology and cell differentiation
    • Ross R, Jonuleit H, Bros M, et al., Expression of the actin-bundling protein fascin in cultured human dendritic cells correlates with dendritic morphology and cell differentiation. J Invest Dermatol 2000; 115: 658-663.
    • (2000) J Invest Dermatol , vol.115 , pp. 658-663
    • Ross, R.1    Jonuleit, H.2    Bros, M.3
  • 28
    • 0035160514 scopus 로고    scopus 로고
    • Fascin is involved in the antigen presentation activity of mature dendritic cells
    • Al-Alwan MM, Rowden G, Lee TD, et al., Fascin is involved in the antigen presentation activity of mature dendritic cells. J Immunol 2001; 166: 338-345. (Pubitemid 32038450)
    • (2001) Journal of Immunology , vol.166 , Issue.1 , pp. 338-345
    • Al-Alwan, M.M.1    Rowden, G.2    Lee, T.D.G.3    West, K.A.4
  • 29
    • 28444468824 scopus 로고    scopus 로고
    • Effects of UVB on fascin expression in dendritic cells and Langerhans cells
    • DOI 10.1016/j.jdermsci.2005.05.004, PII S0923181105001441
    • Sugihara A, Okamoto H, Horio T,. Effects of UVB on fascin expression in dendritic cells and Langerhans cells. J Dermatol Sci 2005; 40: 177-185. (Pubitemid 41728965)
    • (2005) Journal of Dermatological Science , vol.40 , Issue.3 , pp. 177-185
    • Sugihara, A.1    Okamoto, H.2    Horio, T.3
  • 31
    • 34248399632 scopus 로고    scopus 로고
    • Liver X receptors regulate dendritic cell phenotype and function through blocked induction of the actin-bundling protein fascin
    • DOI 10.1182/blood-2006-08-043422
    • Geyeregger R, Zeyda M, Bauer W, et al., Liver X receptors regulate dendritic cell phenotype and function through blocked induction of the actin-bundling protein fascin. Blood 2007; 109: 4288-4295. (Pubitemid 46743395)
    • (2007) Blood , vol.109 , Issue.10 , pp. 4288-4295
    • Geyeregger, R.1    Zeyda, M.2    Bauer, W.3    Kriehuber, E.4    Saemann, M.D.5    Zlabinger, G.J.6    Maurer, D.7    Stulnig, T.M.8
  • 32
    • 77950564432 scopus 로고    scopus 로고
    • MicroRNA control of podosome formation in vascular smooth muscle cells in vivo and in vitro
    • Quintavalle M, Elia L, Condorelli G, et al., MicroRNA control of podosome formation in vascular smooth muscle cells in vivo and in vitro. J Cell Biol 2010; 189: 13-22.
    • (2010) J Cell Biol , vol.189 , pp. 13-22
    • Quintavalle, M.1    Elia, L.2    Condorelli, G.3
  • 33
    • 77049108859 scopus 로고    scopus 로고
    • The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion
    • Li A, Dawson JC, Forero-Vargas M, et al., The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr Biol 2010; 20: 339-345.
    • (2010) Curr Biol , vol.20 , pp. 339-345
    • Li, A.1    Dawson, J.C.2    Forero-Vargas, M.3
  • 34
    • 0022535995 scopus 로고
    • Intracellular localization of the 55-kD actin-bundling protein in cultured cells: Spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin
    • Yamashiro-Matsumura S, Matsumura F,. Intracellular localization of the 55-kD actin-bundling protein in cultured cells: spatial relationships with actin, alpha-actinin, tropomyosin, and fimbrin. J Cell Biol 1986; 103: 631-640. (Pubitemid 16055056)
    • (1986) Journal of Cell Biology , vol.103 , Issue.2 , pp. 631-640
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 35
    • 0030785343 scopus 로고    scopus 로고
    • Characterization of cell-matrix adhesion requirements for the formation of fascin microspikes
    • Adams JC,. Characterization of cell-matrix adhesion requirements for the formation of fascin microspikes. Mol Biol Cell 1997; 8: 2345-2363. (Pubitemid 27469392)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.11 , pp. 2345-2363
    • Adams, J.C.1
  • 36
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: Filopodia contribute to the construction of contractile bundles in the lamella
    • DOI 10.1083/jcb.200709134
    • Nemethova M, Auinger S, Small JV,. Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J Cell Biol 2008; 180: 1233-1244. (Pubitemid 351468477)
    • (2008) Journal of Cell Biology , vol.180 , Issue.6 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 37
    • 0032500661 scopus 로고    scopus 로고
    • Regulation of actin binding and actin bundling activities of fascin by caldesmon coupled with tropomyosin
    • DOI 10.1074/jbc.273.41.26991
    • Ishikawa R, Yamashiro S, Kohama K, et al., Regulation of actin binding and actin bundling activities of fascin by caldesmon coupled with tropomyosin. J Biol Chem 1998; 273: 26991-26997. (Pubitemid 28471722)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.41 , pp. 26991-26997
    • Ishikawa, R.1    Yamashiro, S.2    Kohama, K.3    Matsumura, F.4
  • 38
    • 78650056157 scopus 로고    scopus 로고
    • Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actin-binding proteins to actin filaments
    • Creed SJ, Desouza M, Bamburg JR, et al., Tropomyosin isoform 3 promotes the formation of filopodia by regulating the recruitment of actin-binding proteins to actin filaments. Exp Cell Res 2011; 317: 249-261.
    • (2011) Exp Cell Res , vol.317 , pp. 249-261
    • Creed, S.J.1    Desouza, M.2    Bamburg, J.R.3
  • 39
    • 0031559882 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a photoreceptor cell-specific actin-bundling protein: Retinal fascin
    • DOI 10.1016/S0014-5793(97)01021-1, PII S0014579397010211
    • Saishin Y, Shimada S, Morimura H, et al., Isolation of a cDNA encoding a photoreceptor cell-specific actin-bundling protein: retinal fascin. FEBS Lett 1997; 414: 381-386. (Pubitemid 27389400)
    • (1997) FEBS Letters , vol.414 , Issue.2 , pp. 381-386
    • Saishin, Y.1    Shimada, S.2    Morimura, H.3    Sato, K.4    Ishimoto, I.5    Tano, Y.6    Tohyama, M.7
  • 41
    • 34047259668 scopus 로고    scopus 로고
    • Retina-specific protein fascin 2 is an actin cross-linker associated with actin bundles in photoreceptor inner segments and calycal processes
    • DOI 10.1167/iovs.06-0763
    • Lin-Jones J, Burnside B,. Retina-specific protein fascin 2 is an actin cross-linker associated with actin bundles in photoreceptor inner segments and calycal processes. Invest Ophthalmol Vis Sci 2007; 48: 1380-1388. (Pubitemid 351261438)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.3 , pp. 1380-1388
    • Lin-Jones, J.1    Burnside, B.2
  • 42
    • 0036349350 scopus 로고    scopus 로고
    • Testis fascin (FSCN3): A novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head
    • Tubb B, Mulholland DJ, Vogl W, et al., Testis fascin (FSCN3): a novel paralog of the actin-bundling protein fascin expressed specifically in the elongate spermatid head. Exp Cell Res 2002; 275: 92-109.
    • (2002) Exp Cell Res , vol.275 , pp. 92-109
    • Tubb, B.1    Mulholland, D.J.2    Vogl, W.3
  • 43
    • 76649131265 scopus 로고    scopus 로고
    • Analysis of proteomic changes associated with sperm capacitation through the combined use of IPG-strip pre-fractionation followed by RP chromatography LC-MS/MS analysis
    • Baker MA, Reeves G, Hetherington L, et al., Analysis of proteomic changes associated with sperm capacitation through the combined use of IPG-strip pre-fractionation followed by RP chromatography LC-MS/MS analysis. Proteomics 2010; 10: 482-495.
    • (2010) Proteomics , vol.10 , pp. 482-495
    • Baker, M.A.1    Reeves, G.2    Hetherington, L.3
  • 44
    • 64549140740 scopus 로고    scopus 로고
    • Fascin-1 promoter activity is regulated by CREB and the aryl hydrocarbon receptor in human carcinoma cells
    • Hashimoto Y, Loftis DW, Adams JC,. Fascin-1 promoter activity is regulated by CREB and the aryl hydrocarbon receptor in human carcinoma cells. PLoS One 2009; 4: e5130.
    • (2009) PLoS One , vol.4
    • Hashimoto, Y.1    Loftis, D.W.2    Adams, J.C.3
  • 45
    • 0042591370 scopus 로고    scopus 로고
    • The human fascin gene promoter is highly active in mature dendritic cells due to a stage-specific enhancer
    • Bros M, Ross XL, Pautz A, et al., The human fascin gene promoter is highly active in mature dendritic cells due to a stage-specific enhancer. J Immunol 2003; 171: 1825-1834. (Pubitemid 36966465)
    • (2003) Journal of Immunology , vol.171 , Issue.4 , pp. 1825-1834
    • Bros, M.1    Ross, X.-L.2    Pautz, A.3    Reske-Kunz, A.B.4    Ross, R.5
  • 46
    • 18844395839 scopus 로고    scopus 로고
    • Minor expression of fascin-1 gene (FSCN1) in NTera2 cells depleted of CREB-binding protein
    • DOI 10.1016/j.neulet.2005.02.027, PII S030439400500203X
    • Megiorni F, Indovina P, Mora B, et al., Minor expression of fascin-1 gene (FSCN1) in NTera2 cells depleted of CREB-binding protein. Neurosci Lett 2005; 381: 169-174. (Pubitemid 40693163)
    • (2005) Neuroscience Letters , vol.381 , Issue.1-2 , pp. 169-174
    • Megiorni, F.1    Indovina, P.2    Mora, B.3    Mazzilli, M.C.4
  • 47
    • 77649271930 scopus 로고    scopus 로고
    • MiR-145 and miR-133a function as tumour suppressors and directly regulate FSCN1 expression in bladder cancer
    • Chiyomaru T, Enokida H, Tatarano S, et al., miR-145 and miR-133a function as tumour suppressors and directly regulate FSCN1 expression in bladder cancer. Br J Cancer 2010; 102: 883-891.
    • (2010) Br J Cancer , vol.102 , pp. 883-891
    • Chiyomaru, T.1    Enokida, H.2    Tatarano, S.3
  • 48
    • 77956181723 scopus 로고    scopus 로고
    • MiR-145, miR-133a and miR-133b: Tumor-suppressive miRNAs target FSCN1 in esophageal squamous cell carcinoma
    • Kano M, Seki N, Kikkawa N, et al,: miR-145, miR-133a and miR-133b: tumor-suppressive miRNAs target FSCN1 in esophageal squamous cell carcinoma. Int J Cancer 2010; 127: 2804-2814.
    • (2010) Int J Cancer , vol.127 , pp. 2804-2814
    • Kano, M.1    Seki, N.2    Kikkawa, N.3
  • 49
    • 78649993667 scopus 로고    scopus 로고
    • Micro-RNA signature of the epithelial-mesenchymal transition in endometrial carcinosarcoma
    • Castilla MA, Moreno-Bueno G, Romero-Perez L, et al., Micro-RNA signature of the epithelial-mesenchymal transition in endometrial carcinosarcoma. J Pathol 2011; 223: 72-80.
    • (2011) J Pathol , vol.223 , pp. 72-80
    • Castilla, M.A.1    Moreno-Bueno, G.2    Romero-Perez, L.3
  • 50
    • 35848950225 scopus 로고    scopus 로고
    • Dual actin-bundling and protein kinase C-binding activities of fascin regulate carcinoma cell migration downstream of Rac and contribute to metastasis
    • DOI 10.1091/mbc.E07-02-0157
    • Hashimoto Y, Parsons M, Adams JC,. Dual actin-bundling and protein kinase C-binding activities of fascin regulate carcinoma cell migration downstream of Rac and contribute to metastasis. Mol Biol Cell 2007; 18: 4591-4602. (Pubitemid 350060184)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4591-4602
    • Hashimoto, Y.1    Parsons, M.2    Adams, J.C.3
  • 51
    • 0038798665 scopus 로고    scopus 로고
    • Neurotrophin-induced melanoma cell migration is mediated through the actin-bundling protein fascin
    • DOI 10.1038/sj.onc.1206561
    • Shonukan O, Bagayogo I, McCrea P, et al., Neurotrophin-induced melanoma cell migration is mediated through the actin-bundling protein fascin. Oncogene 2003; 22: 3616-3623. (Pubitemid 36765321)
    • (2003) Oncogene , vol.22 , Issue.23 , pp. 3616-3623
    • Shonukan, T.1    Bagayogo, I.2    McCrea, P.D.3    Chao, M.4    Hempstead, B.5
  • 52
    • 33344461843 scopus 로고    scopus 로고
    • Cytoplasmic domain of protocadherin-α enhances homophilic interactions and recognizes cytoskeletal elements
    • DOI 10.1002/neu.20228
    • Triana-Baltzer GB, Blank M,. Cytoplasmic domain of protocadherin-alpha enhances homophilic interactions and recognizes cytoskeletal elements. J Neurobiol 2006; 66: 393-407. (Pubitemid 43291288)
    • (2006) Journal of Neurobiology , vol.66 , Issue.4 , pp. 393-407
    • Triana-Baltzer, G.B.1    Blank, M.2
  • 53
    • 69949167051 scopus 로고    scopus 로고
    • Rab35 controls actin bundling by recruiting fascin as an effector protein
    • Zhang J, Fonovic M, Suyama K, et al., Rab35 controls actin bundling by recruiting fascin as an effector protein. Science 2009; 325: 1250-1254.
    • (2009) Science , vol.325 , pp. 1250-1254
    • Zhang, J.1    Fonovic, M.2    Suyama, K.3
  • 54
    • 15844362435 scopus 로고    scopus 로고
    • Phosphorylation of human fascin inhibits its actin binding and bundling activities
    • DOI 10.1074/jbc.271.21.12632
    • Yamakita Y, Ono S, Matsumura F, et al., Phosphorylation of human fascin inhibits its actin binding and bundling activities. J Biol Chem 1996; 271: 12632-12638. (Pubitemid 26163336)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.21 , pp. 12632-12638
    • Yamakita, Y.1    Ono, S.2    Matsumura, F.3    Yamashiro, S.4
  • 55
    • 0032741306 scopus 로고    scopus 로고
    • Cell-matrix adhesions differentially regulate fascin phosphorylation
    • Adams JC, Clelland JD, Collett GD, et al., Cell-matrix adhesions differentially regulate fascin phosphorylation. Mol Biol Cell 1999; 10: 4177-4190.
    • (1999) Mol Biol Cell , vol.10 , pp. 4177-4190
    • Adams, J.C.1    Clelland, J.D.2    Collett, G.D.3
  • 56
    • 36849001517 scopus 로고    scopus 로고
    • Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration
    • DOI 10.1002/jcp.21184
    • Bachy S, Letourneur F, Rousselle P,. Syndecan-1 interaction with the LG4/5 domain in laminin-332 is essential for keratinocyte migration. J Cell Physiol 2008; 214: 238-249. (Pubitemid 350220078)
    • (2008) Journal of Cellular Physiology , vol.214 , Issue.1 , pp. 238-249
    • Bachy, S.1    Letourneur, F.2    Rousselle, P.3
  • 58
    • 0036010596 scopus 로고    scopus 로고
    • Fascins, and their roles in cell structure and function
    • DOI 10.1002/bies.10070
    • Kureishy N, Sapountzi V, Prag S, et al., Fascins, and their roles in cell structure and function. Bioessays 2002; 24: 350-361. (Pubitemid 34305690)
    • (2002) BioEssays , vol.24 , Issue.4 , pp. 350-361
    • Kureishy, N.1    Sapountzi, V.2    Prag, S.3    Anilkumar, N.4    Adams, J.C.5
  • 59
    • 77956198670 scopus 로고    scopus 로고
    • Actin cross-link assembly and disassembly mechanics for alpha-actinin and fascin
    • Courson DS, Rock RS,. Actin cross-link assembly and disassembly mechanics for alpha-actinin and fascin. J Biol Chem 2010; 285: 26350-26357.
    • (2010) J Biol Chem , vol.285 , pp. 26350-26357
    • Courson, D.S.1    Rock, R.S.2
  • 61
    • 0030040876 scopus 로고    scopus 로고
    • Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones
    • Sasaki Y, Hayashi K, Shirao T, et al., Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J Neurochem 1996; 66: 980-988. (Pubitemid 26065894)
    • (1996) Journal of Neurochemistry , vol.66 , Issue.3 , pp. 980-988
    • Sasaki, Y.1    Hayashi, K.2    Shirao, T.3    Ishikawa, R.4    Kohama, K.5
  • 62
    • 0037067679 scopus 로고    scopus 로고
    • Functional synergy of actin filament cross-linking proteins
    • DOI 10.1074/jbc.M202609200
    • Tseng Y, Schafer BW, Almo SC, et al., Functional synergy of actin filament cross-linking proteins. J Biol Chem 2002; 277: 25609-25616. (Pubitemid 34951878)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.28 , pp. 25609-25616
    • Tseng, Y.1    Schafer, B.W.2    Almo, S.C.3    Wirtz, D.4
  • 63
    • 77957334369 scopus 로고    scopus 로고
    • The stepping pattern of myosin X is adapted for processive motility on bundled actin
    • Ricca BL, Rock RS,. The stepping pattern of myosin X is adapted for processive motility on bundled actin. Biophys J 2010; 99: 1818-1826.
    • (2010) Biophys J , vol.99 , pp. 1818-1826
    • Ricca, B.L.1    Rock, R.S.2
  • 64
    • 36549035377 scopus 로고    scopus 로고
    • A Cytoskeletal Demolition Worker: Myosin II Acts as an Actin Depolymerization Agent
    • DOI 10.1016/j.jmb.2007.09.066, PII S002228360701265X
    • Haviv L, Gillo D, Backouche F, et al., A cytoskeletal demolition worker: myosin II acts as an actin depolymerization agent. J Mol Biol 2008; 375: 325-330. (Pubitemid 350192474)
    • (2008) Journal of Molecular Biology , vol.375 , Issue.2 , pp. 325-330
    • Haviv, L.1    Gillo, D.2    Backouche, F.3    Bernheim-Groswasser, A.4
  • 65
    • 77954237525 scopus 로고    scopus 로고
    • Unconventional processive mechanics of non-muscle myosin IIB
    • Norstrom MF, Smithback PA, Rock RS,. Unconventional processive mechanics of non-muscle myosin IIB. J Biol Chem 2010; 285: 26326-26334.
    • (2010) J Biol Chem , vol.285 , pp. 26326-26334
    • Norstrom, M.F.1    Smithback, P.A.2    Rock, R.S.3
  • 68
    • 54749151462 scopus 로고    scopus 로고
    • Arp2/3 branched actin network mediates filopodia-like bundles formation in vitro
    • Ideses Y, Brill-Karniely Y, Haviv L, et al., Arp2/3 branched actin network mediates filopodia-like bundles formation in vitro. PLoS One 2008; 3: e3297.
    • (2008) PLoS One , vol.3
    • Ideses, Y.1    Brill-Karniely, Y.2    Haviv, L.3
  • 69
    • 77951977342 scopus 로고    scopus 로고
    • Electron tomography reveals unbranched networks of actin filaments in lamellipodia
    • Urban E, Jacob S, Nemethova M, et al., Electron tomography reveals unbranched networks of actin filaments in lamellipodia. Nature Cell Biol 2010; 12: 429-435.
    • (2010) Nature Cell Biol , vol.12 , pp. 429-435
    • Urban, E.1    Jacob, S.2    Nemethova, M.3
  • 70
    • 54849437256 scopus 로고    scopus 로고
    • The filamentous actin cross-linking/bundling activity of mammalian formins
    • Esue O, Harris ES, Higgs HN, et al., The filamentous actin cross-linking/bundling activity of mammalian formins. J Mol Biol 2008; 384: 324-334.
    • (2008) J Mol Biol , vol.384 , pp. 324-334
    • Esue, O.1    Harris, E.S.2    Higgs, H.N.3
  • 71
    • 77956537388 scopus 로고    scopus 로고
    • Self-assembly of filopodia-like structures on supported lipid bilayers
    • Lee K, Gallop JL, Rambani K, et al., Self-assembly of filopodia-like structures on supported lipid bilayers. Science 2010; 329: 1341-1345.
    • (2010) Science , vol.329 , pp. 1341-1345
    • Lee, K.1    Gallop, J.L.2    Rambani, K.3
  • 74
    • 0034609766 scopus 로고    scopus 로고
    • C-erbB-2/HER-2 upregulates fascin, an actin-bundling protein associated with cell motility, in human breast cancer cell lines
    • Grothey A, Hashizume R, Ji H, et al., C-erbB-2/HER-2 upregulates fascin, an actin-bundling protein associated with cell motility, in human breast cancer cell lines. Oncogene 2000; 19: 4864-4875.
    • (2000) Oncogene , vol.19 , pp. 4864-4875
    • Grothey, A.1    Hashizume, R.2    Ji, H.3
  • 75
    • 11344285907 scopus 로고    scopus 로고
    • The expression of fascin, an actin-bundling motility protein, correlates with hormone receptor-negative breast cancer and a more aggressive clinical course
    • Yoder BJ, Tso E, Skacel M, et al., The expression of fascin, an actin-bundling motility protein, correlates with hormone receptor-negative breast cancer and a more aggressive clinical course. Clin Cancer Res 2005; 11: 186-192. (Pubitemid 40075794)
    • (2005) Clinical Cancer Research , vol.11 , Issue.1 , pp. 186-192
    • Yoder, B.J.1    Tso, E.2    Skacel, M.3    Pettay, J.4    Tarr, S.5    Budd, T.6    Tubbs, R.R.7    Adams, J.C.8    Hicks, D.G.9
  • 76
    • 63149085638 scopus 로고    scopus 로고
    • Fascin regulates prostate cancer cell invasion and is associated with metastasis and biochemical failure in prostate cancer
    • Darnel AD, Behmoaram E, Vollmer RT, et al., Fascin regulates prostate cancer cell invasion and is associated with metastasis and biochemical failure in prostate cancer. Clin Cancer Res 2009; 15: 1376-1383.
    • (2009) Clin Cancer Res , vol.15 , pp. 1376-1383
    • Darnel, A.D.1    Behmoaram, E.2    Vollmer, R.T.3
  • 79
    • 70350335625 scopus 로고    scopus 로고
    • Effects of small interfering RNAs targeting fascin on gene expression in oral cancer cells
    • Chen SF, Lin CY, Chang YC, et al., Effects of small interfering RNAs targeting fascin on gene expression in oral cancer cells. J Oral Pathol Med 2009; 38: 722-730.
    • (2009) J Oral Pathol Med , vol.38 , pp. 722-730
    • Chen, S.F.1    Lin, C.Y.2    Chang, Y.C.3
  • 80
    • 77953676348 scopus 로고    scopus 로고
    • Effects of small interfering RNAs targeting fascin on human esophageal squamous cell carcinoma cell lines
    • Ortiz CM, Ito T, Hashimoto Y, et al., Effects of small interfering RNAs targeting fascin on human esophageal squamous cell carcinoma cell lines. Diagn Pathol 2010; 5: 41.
    • (2010) Diagn Pathol , vol.5 , pp. 41
    • Ortiz, C.M.1    Ito, T.2    Hashimoto, Y.3
  • 83
    • 77249102098 scopus 로고    scopus 로고
    • Galectin-3 increases gastric cancer cell motility by up-regulating fascin-1 expression
    • Kim SJ, Choi IJ, Cheong TC, et al., Galectin-3 increases gastric cancer cell motility by up-regulating fascin-1 expression. Gastroenterology 2010; 138: 1035-1045.
    • (2010) Gastroenterology , vol.138 , pp. 1035-1045
    • Kim, S.J.1    Choi, I.J.2    Cheong, T.C.3
  • 84
    • 77951116071 scopus 로고    scopus 로고
    • Migrastatin analogues target fascin to block tumour metastasis
    • Chen L, Yang S, Jakoncic J, et al., Migrastatin analogues target fascin to block tumour metastasis. Nature 2010; 464: 1062-1066.
    • (2010) Nature , vol.464 , pp. 1062-1066
    • Chen, L.1    Yang, S.2    Jakoncic, J.3
  • 87
    • 27944500223 scopus 로고    scopus 로고
    • Fascin expression in 90 patients with glioblastoma multiforme
    • DOI 10.1016/j.anndiagpath.2005.07.005, PII S1092913405001115
    • Roma AA, Prayson RA,. Fascin expression in 90 patients with glioblastoma multiforme. Ann Diagn Pathol 2005; 9: 307-311. (Pubitemid 41676877)
    • (2005) Annals of Diagnostic Pathology , vol.9 , Issue.6 , pp. 307-311
    • Roma, A.A.1    Prayson, R.A.2
  • 88
    • 39049136505 scopus 로고    scopus 로고
    • The role of fascin in the migration and invasiveness of malignant glioma cells
    • DOI 10.1593/neo.07909
    • Hwang JH, Smith CA, Salhia B, et al., The role of fascin in the migration and invasiveness of malignant glioma cells. Neoplasia 2008; 10: 149-159. (Pubitemid 351240881)
    • (2008) Neoplasia , vol.10 , Issue.2 , pp. 149-159
    • Jeong, H.H.1    Smith, C.A.2    Salhia, B.3    Rutka, J.T.4
  • 90
    • 39749159026 scopus 로고    scopus 로고
    • Proteomic analysis of stargazer mutant mouse neuronal proteins involved in absence seizure
    • DOI 10.1111/j.1471-4159.2007.05100.x
    • Ryu MJ, Lee C, Kim J, et al., Proteomic analysis of stargazer mutant mouse neuronal proteins involved in absence seizure. J Neurochem 2008; 104: 1260-1270. (Pubitemid 351293351)
    • (2008) Journal of Neurochemistry , vol.104 , Issue.5 , pp. 1260-1270
    • Ryu, M.-J.1    Lee, C.2    Kim, J.3    Shin, H.-S.4    Yu, M.-H.5
  • 91
    • 36949032159 scopus 로고    scopus 로고
    • Dysregulation of growth factor receptor-bound protein 2 and fascin in hippocampus of mice polytransgenic for chromosome 21 structures
    • DOI 10.1002/hipo.20351
    • Shin JH, Guedj F, Delabar JM, et al., Dysregulation of growth factor receptor-bound protein 2 and fascin in hippocampus of mice polytransgenic for chromosome 21 structures. Hippocampus 2007; 17: 1180-1192. (Pubitemid 350244234)
    • (2007) Hippocampus , vol.17 , Issue.12 , pp. 1180-1192
    • Shin, J.-H.1    Guedj, F.2    Delabar, J.-M.3    Lubec, G.4
  • 92
    • 38149046578 scopus 로고    scopus 로고
    • Ubiquitin proteasome-mediated synaptic reorganization: A novel mechanism underlying rapid ischemic tolerance
    • Meller R, Thompson SJ, Lusardi TA, et al., Ubiquitin proteasome-mediated synaptic reorganization: a novel mechanism underlying rapid ischemic tolerance. J Neurosci 2008; 28: 50-59.
    • (2008) J Neurosci , vol.28 , pp. 50-59
    • Meller, R.1    Thompson, S.J.2    Lusardi, T.A.3
  • 93
    • 0035990482 scopus 로고    scopus 로고
    • Actin-binding protein fascin expression in skin neoplasia
    • Goncharuk VN, Ross JS, Carlson JA,. Actin-binding protein fascin expression in skin neoplasia. J Cutan Pathol 2002; 29: 430-438.
    • (2002) J Cutan Pathol , vol.29 , pp. 430-438
    • Goncharuk, V.N.1    Ross, J.S.2    Carlson, J.A.3
  • 94
    • 69849106727 scopus 로고    scopus 로고
    • Fascin expression in melanocytic lesions of the skin
    • Yildiz L, Kefeli M, Aydin O, et al., Fascin expression in melanocytic lesions of the skin. Eur J Dermatol 2009; 19: 445-450.
    • (2009) Eur J Dermatol , vol.19 , pp. 445-450
    • Yildiz, L.1    Kefeli, M.2    Aydin, O.3
  • 95
    • 77952815978 scopus 로고    scopus 로고
    • Fascin, cortactin and survivin expression of melanocytic neoplasms and association with clinicopathological parameters and anatomic locations in Chinese people
    • Gao HW, Yu CP, Lee HS, et al., Fascin, cortactin and survivin expression of melanocytic neoplasms and association with clinicopathological parameters and anatomic locations in Chinese people. Eur J Dermatol 2010; 20: 293-301.
    • (2010) Eur J Dermatol , vol.20 , pp. 293-301
    • Gao, H.W.1    Yu, C.P.2    Lee, H.S.3
  • 96
    • 70350488083 scopus 로고    scopus 로고
    • Comparative proteomic analysis of mouse melanoma cell line B16, a metastatic descendant B16F10, and B16 overexpressing the metastasis-associated tyrosine phosphatase PRL-3
    • Kim SH, Kim Y, Kim M, et al., Comparative proteomic analysis of mouse melanoma cell line B16, a metastatic descendant B16F10, and B16 overexpressing the metastasis-associated tyrosine phosphatase PRL-3. Oncol Res 2009; 17: 601-612.
    • (2009) Oncol Res , vol.17 , pp. 601-612
    • Kim, S.H.1    Kim, Y.2    Kim, M.3
  • 98
    • 0242611651 scopus 로고    scopus 로고
    • Autosomal Dominant Macular Degeneration Associated With 208delG Mutation in the FSCN2 Gene
    • DOI 10.1001/archopht.121.11.1613
    • Wada Y, Abe T, Itabashi T, et al., Autosomal dominant macular degeneration associated with 208delG mutation in the FSCN2 gene. Arch Ophthalmol 2003; 121: 1613-1620. (Pubitemid 37392369)
    • (2003) Archives of Ophthalmology , vol.121 , Issue.11 , pp. 1613-1620
    • Wada, Y.1    Abe, T.2    Itabashi, T.3    Sato, H.4    Kawamura, M.5    Tamai, M.6
  • 100
    • 33847738565 scopus 로고    scopus 로고
    • The 208delG mutation in FSCN2 does not associate with retinal degeneration in Chinese individuals
    • DOI 10.1167/iovs.06-0669
    • Zhang Q, Li S, Xiao X, et al., The 208delG mutation in FSCN2 does not associate with retinal degeneration in Chinese individuals. Invest Ophthalmol Vis Sci 2007; 48: 530-533. (Pubitemid 351260681)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.2 , pp. 530-533
    • Zhang, Q.1    Li, S.2    Xiao, X.3    Jia, X.4    Guo, X.5
  • 102
    • 34147096482 scopus 로고    scopus 로고
    • Identification of photoreceptor genes affected by PRPF31 mutations associated with autosomal dominant retinitis pigmentosa
    • DOI 10.1016/j.nbd.2006.08.026, PII S0969996106001975
    • Mordes D, Yuan L, Xu L, et al., Identification of photoreceptor genes affected by PRPF31 mutations associated with autosomal dominant retinitis pigmentosa. Neurobiol Dis 2007; 26: 291-300. (Pubitemid 46561333)
    • (2007) Neurobiology of Disease , vol.26 , Issue.2 , pp. 291-300
    • Mordes, D.1    Yuan, L.2    Xu, L.3    Kawada, M.4    Molday, R.S.5    Wu, J.Y.6
  • 103
    • 79951782264 scopus 로고    scopus 로고
    • How the genetics of deafness illuminates auditory physiology
    • Richardson GP, Boutet de Monvel J, Petit C,. How the genetics of deafness illuminates auditory physiology. Annu Rev Physiol 2011; 73: 20.1-20.24.
    • (2011) Annu Rev Physiol , vol.73 , pp. 201-2024
    • Richardson, G.P.1    Boutet De Monvel, J.2    Petit, C.3
  • 104
    • 77954847853 scopus 로고    scopus 로고
    • The R109H variant of fascin-2, a developmentally regulated actin crosslinker in hair-cell stereocilia, underlies early-onset hearing loss of DBA/2J mice
    • Shin JB, Longo-Guess CM, Gagnon LH, et al., The R109H variant of fascin-2, a developmentally regulated actin crosslinker in hair-cell stereocilia, underlies early-onset hearing loss of DBA/2J mice. J Neurosci 2010; 30: 9683-9694.
    • (2010) J Neurosci , vol.30 , pp. 9683-9694
    • Shin, J.B.1    Longo-Guess, C.M.2    Gagnon, L.H.3
  • 106
    • 58049196780 scopus 로고    scopus 로고
    • MTORC1-dependent and -independent regulation of stem cell renewal, differentiation, and mobilization
    • Gan B, Sahin E, Jiang S, et al., mTORC1-dependent and -independent regulation of stem cell renewal, differentiation, and mobilization. Proc Natl Acad Sci U S A 2008; 105: 19384-19389.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19384-19389
    • Gan, B.1    Sahin, E.2    Jiang, S.3
  • 108
    • 0028936379 scopus 로고
    • The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm
    • Hanakam F, Eckerskorn C, Lottspeich F, et al., The pH-sensitive actin-binding protein hisactophilin of Dictyostelium exists in two isoforms which both are myristoylated and distributed between plasma membrane and cytoplasm. J Biol Chem 1995; 270: 596-602.
    • (1995) J Biol Chem , vol.270 , pp. 596-602
    • Hanakam, F.1    Eckerskorn, C.2    Lottspeich, F.3
  • 109
    • 0029156887 scopus 로고
    • F actin bundles in Drosophila bristles. I. Two filament cross-links are involved in bundling
    • Tilney LG, Tilney MS, Guild GM,. F actin bundles in Drosophila bristles. I. Two filament cross-links are involved in bundling. J Cell Biol 1995; 130: 629-638.
    • (1995) J Cell Biol , vol.130 , pp. 629-638
    • Tilney, L.G.1    Tilney, M.S.2    Guild, G.M.3
  • 111
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: Molecular architecture and cellular functions
    • DOI 10.1038/nrm2406, PII NRM2406
    • Mattila PK, Lappalainen P,. Filopodia: molecular architecture and cellular functions. Nature Rev Mol Cell Biol 2008; 9: 446-454. (Pubitemid 351733400)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.6 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 112
    • 0029015719 scopus 로고
    • Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin-1: Implications for the anti-adhesive activities of thrombospondin-1
    • Adams JC,. Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin-1: implications for the anti-adhesive activities of thrombospondin-1. J Cell Sci 1995; 108: 1977-1990.
    • (1995) J Cell Sci , vol.108 , pp. 1977-1990
    • Adams, J.C.1
  • 113
    • 0036591974 scopus 로고    scopus 로고
    • Trimeric assembly of the C-terminal region of thrombospondin-1 or thrombospondin-2 is necessary for cell spreading and fascin spike organisation
    • Anilkumar N, Annis DS, Mosher DF, et al., Trimeric assembly of the C-terminal region of thrombospondin-1 or thrombospondin-2 is necessary for cell spreading and fascin spike organisation. J Cell Sci 2002; 115: 2357-2366. (Pubitemid 34752979)
    • (2002) Journal of Cell Science , vol.115 , Issue.11 , pp. 2357-2366
    • Anilkumar, N.1    Annis, D.S.2    Mosher, D.F.3    Adams, J.C.4
  • 114
    • 0035911954 scopus 로고    scopus 로고
    • A role for syndecan-1 in coupling fascin spike formation by thrombospondin-1
    • DOI 10.1083/jcb.152.6.1169
    • Adams JC, Kureishy N, Taylor AL,. A role for syndecan-1 in coupling fascin spike formation by thrombospondin-1. J Cell Biol 2001; 152: 1169-1182. (Pubitemid 34280175)
    • (2001) Journal of Cell Biology , vol.152 , Issue.6 , pp. 1169-1182
    • Adams, J.C.1    Kureishy, N.2    Taylor, A.L.3
  • 115
    • 0030851834 scopus 로고    scopus 로고
    • Cell-adhesive responses to Tenascin-C splice variants involve formation of fascin microspikes
    • Fischer D, Tucker RP, Chiquet-Ehrismann R, et al., Cell-adhesive responses to tenascin-C splice variants involve formation of fascin microspikes. Mol Biol Cell 1997; 8: 2055-2075. (Pubitemid 27451120)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.10 , pp. 2055-2075
    • Fischer, D.1    Tucker, R.P.2    Chiquet-Ehrismann, R.3    Adams, J.C.4
  • 116
    • 0036218155 scopus 로고    scopus 로고
    • Induction of fascin spikes in breast cancer cells by activation of the insulin-like growth factor-I receptor
    • DOI 10.1016/S1357-2725(01)00160-1, PII S1357272501001601
    • Guvakova MA, Boettiger D, Adams JC,. Induction of fascin spikes in breast cancer cells by activation of the insulin-like growth factor-I receptor. Int J Biochem Cell Biol 2002; 34: 685-698. (Pubitemid 34270721)
    • (2002) International Journal of Biochemistry and Cell Biology , vol.34 , Issue.6 , pp. 685-698
    • Guvakova, M.A.1    Boettiger, D.2    Adams, J.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.