메뉴 건너뛰기




Volumn 160, Issue 6, 2003, Pages 951-962

Formation of filopodia-like bundles in vitro from a dendritic network

Author keywords

Actin; Arp2 3; Capping protein; Fascin; Filopodia

Indexed keywords

ACTIN; WISKOTT ALDRICH SYNDROME PROTEIN;

EID: 0345146913     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200208059     Document Type: Article
Times cited : (215)

References (51)
  • 7
    • 0035140487 scopus 로고    scopus 로고
    • Role of the actin bundling protein fascin in growth cone morphogenesis: Localization in filopodia and lamellipodia
    • Cohan, C.S., E.A. Welnhofer, L. Zhao, F. Matsumura, and S. Yamashiro. 2001. Role of the actin bundling protein fascin in growth cone morphogenesis: localization in filopodia and lamellipodia. Cell Motil. Cytoskeleton. 48:109-120.
    • (2001) Cell Motil. Cytoskeleton. , vol.48 , pp. 109-120
    • Cohan, C.S.1    Welnhofer, E.A.2    Zhao, L.3    Matsumura, F.4    Yamashiro, S.5
  • 8
    • 0033965314 scopus 로고    scopus 로고
    • Control of actin assembly and disassembly at filament ends
    • Cooper, J.A., and D.A. Schafer. 2000. Control of actin assembly and disassembly at filament ends. Curr. Opin. Cell Biol. 12:97-103.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 97-103
    • Cooper, J.A.1    Schafer, D.A.2
  • 9
    • 0028882496 scopus 로고
    • Actin filament barbed-end capping activity in neutrophil lysates: The role of capping protein-β2
    • DiNubile, M.J., L. Cassimeris, M. Joyce, and S.H. Zigmond. 1995. Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-β2. Mol. Biol. Cell 6:1659-1671.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1659-1671
    • DiNubile, M.J.1    Cassimeris, L.2    Joyce, M.3    Zigmond, S.H.4
  • 10
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile, C., T.P. Loisel, V. Laurent, R. Li, D. Pantaloni, P.J. Sansonetti, and M.F. Carlier. 1999. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146:1319-1332.
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.F.7
  • 11
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • Evangelista, M., D. Pruyne, D.C. Amberg, C. Boone, and A. Bretscher. 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
  • 12
    • 0035199154 scopus 로고    scopus 로고
    • Actin-based motility of intracellular microbial pathogens
    • table of contents
    • Goldberg, M.B. 2001. Actin-based motility of intracellular microbial pathogens. Microbiol. Mol. Biol. Rev. 65:595-626 (table of contents).
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 595-626
    • Goldberg, M.B.1
  • 13
    • 0034911925 scopus 로고    scopus 로고
    • Regulation of actin filament network formation through ARP2/3 complex: Activation by a diverse array of proteins
    • Higgs, H.N., and T.D. Pollard. 2001. Regulation of actin filament network formation through ARP2/3 complex: activation by a diverse array of proteins. Annu. Rev. Biochem. 70:649-676.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 649-676
    • Higgs, H.N.1    Pollard, T.D.2
  • 15
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert, H., P. Venier, A.C. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M.F. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.F.7
  • 16
    • 0020011022 scopus 로고
    • Vinculin and α-actinin: Interaction with actin and effect on microfilament network formation
    • Jockusch, B.M., and G. Isenberg. 1982. Vinculin and α-actinin: interaction with actin and effect on microfilament network formation. Cold Spring Harb. Symp. Quant. Biol. 46:613-623.
    • (1982) Cold Spring Harb. Symp. Quant. Biol. , vol.46 , pp. 613-623
    • Jockusch, B.M.1    Isenberg, G.2
  • 18
    • 0021711645 scopus 로고
    • Ultrastructural localization of α-actinin and filamin in cultured cells with the immunogold staining (IGS) method
    • Langanger, G., J. de Mey, M. Moeremans, G. Daneels, M. de Brabander, and J.V. Small. 1984. Ultrastructural localization of α-actinin and filamin in cultured cells with the immunogold staining (IGS) method. J. Cell Biol. 99:1324-1334.
    • (1984) J. Cell Biol. , vol.99 , pp. 1324-1334
    • Langanger, G.1    De Mey, J.2    Moeremans, M.3    Daneels, G.4    De Brabander, M.5    Small, J.V.6
  • 21
    • 0026437563 scopus 로고
    • Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity
    • Lewis, A.K., and P.C. Bridgman. 1992. Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity. J. Cell Biol. 119:1219-1243.
    • (1992) J. Cell Biol. , vol.119 , pp. 1219-1243
    • Lewis, A.K.1    Bridgman, P.C.2
  • 22
    • 0037097589 scopus 로고    scopus 로고
    • Arp2/3 complex is required for actin polymerization during platelet shape change
    • Li, Z., E.S. Kim, and E.L. Bearer. 2002. Arp2/3 complex is required for actin polymerization during platelet shape change. Blood. 99:4466-4474.
    • (2002) Blood , vol.99 , pp. 4466-4474
    • Li, Z.1    Kim, E.S.2    Bearer, E.L.3
  • 23
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • see comments
    • Loisel, T.P., R. Boujemaa, D. Pantaloni, and M.F. Carlier. 1999. Reconstitution of actin-based motility of Listeria and Shigella using pure proteins. Nature. 401: 613-616 (see comments).
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 24
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L.M., and R.H. Insall. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 25
    • 0037215933 scopus 로고    scopus 로고
    • Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5
    • Millard, T.H., B. Behrendt, S. Launay, K. Futterer, and L.M. Machesky. 2003. Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5. Cell Motil. Cytoskeleton. 54:81-90.
    • (2003) Cell Motil. Cytoskeleton. , vol.54 , pp. 81-90
    • Millard, T.H.1    Behrendt, B.2    Launay, S.3    Futterer, K.4    Machesky, L.M.5
  • 26
    • 0032825265 scopus 로고    scopus 로고
    • Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction
    • Mallavarapu, A., and T. Mitchison. 1999. Regulated actin cytoskeleton assembly at filopodium tips controls their extension and retraction. J. Cell Biol. 146: 1097-1106.
    • (1999) J. Cell Biol. , vol.146 , pp. 1097-1106
    • Mallavarapu, A.1    Mitchison, T.2
  • 27
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP
    • Miki, H., T. Sasaki, Y. Takai, and T. Takenawa. 1998. Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP. Nature. 391:93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 28
    • 0032568650 scopus 로고    scopus 로고
    • The interaction of Arp2/3 complex with actin: Nucleation, high affinity pointed end capping, and formation of branching networks of filaments
    • Mullins, R.D., J.A. Heuser, and T.D. Pollard. 1998. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. USA. 95: 6181-6186.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 29
    • 0026266161 scopus 로고
    • Cell cycle extracts
    • Murray, A.W. 1991. Cell cycle extracts. Methods Cell Biol. 36:581-605.
    • (1991) Methods Cell Biol. , vol.36 , pp. 581-605
    • Murray, A.W.1
  • 30
  • 31
    • 0035886026 scopus 로고    scopus 로고
    • Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin
    • Palmgren, S., P.J. Ojala, M.A. Wear, J.A. Cooper, and P. Lappalainen. 2001. Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin. J. Cell Biol. 155:251-260.
    • (2001) J. Cell Biol. , vol.155 , pp. 251-260
    • Palmgren, S.1    Ojala, P.J.2    Wear, M.A.3    Cooper, J.A.4    Lappalainen, P.5
  • 32
    • 0033771755 scopus 로고    scopus 로고
    • The Arp2/3 complex branches filament barbed ends: Functional antagonism with capping proteins
    • Pantaloni, D., R. Boujemaa, D. Didry, P. Gounon, and M.F. Carlier. 2000. The Arp2/3 complex branches filament barbed ends: functional antagonism with capping proteins. Nat. Cell Biol. 2:385-391.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 385-391
    • Pantaloni, D.1    Boujemaa, R.2    Didry, D.3    Gounon, P.4    Carlier, M.F.5
  • 35
    • 0036141585 scopus 로고    scopus 로고
    • Yeast formins regulate cell polarity by controlling the assembly of actin cables
    • Sagot, I., S.K. Klee, and D. Pellman. 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
  • 37
    • 0032555923 scopus 로고    scopus 로고
    • Stepwise reconstitution of interphase microtubule dynamics in permeabilized cells and comparison to dynamic mechanisms in intact cells
    • Saoudi, Y., R. Fotedar, A. Abrieu, M. Doree, J. Wehland, R.L. Margolis, and D. Job. 1998. Stepwise reconstitution of interphase microtubule dynamics in permeabilized cells and comparison to dynamic mechanisms in intact cells. J. Cell Biol. 142:1519-1532.
    • (1998) J. Cell Biol. , vol.142 , pp. 1519-1532
    • Saoudi, Y.1    Fotedar, R.2    Abrieu, A.3    Doree, M.4    Wehland, J.5    Margolis, R.L.6    Job, D.7
  • 38
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • Small, J.V., G. Isenberg, and J.E. Celis. 1978. Polarity of actin at the leading edge of cultured cells. Nature. 272:638-639.
    • (1978) Nature , vol.272 , pp. 638-639
    • Small, J.V.1    Isenberg, G.2    Celis, J.E.3
  • 39
    • 0028579772 scopus 로고
    • Visualization of actin filaments in keratocyte lamellipodia: Negative staining compared with freeze-drying
    • Small, J.V., M. Herzog, M. Haner, and U. Abei. 1994. Visualization of actin filaments in keratocyte lamellipodia: negative staining compared with freeze-drying, J. Struct. Biol. 113:135-141.
    • (1994) J. Struct. Biol. , vol.113 , pp. 135-141
    • Small, J.V.1    Herzog, M.2    Haner, M.3    Abei, U.4
  • 41
  • 42
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich, J.A., and S. Watt. 1971. The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J. Biol. Chem. 246:4866-4871.
    • (1971) J. Biol. Chem. , vol.246 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 43
    • 0031615095 scopus 로고    scopus 로고
    • Correlative light and electron microscopy of the cytoskeleton of cultured cells
    • Svitkina, T.M., and G.G. Borisy. 1998. Correlative light and electron microscopy of the cytoskeleton of cultured cells. Methods Enzymol. 298:570-592.
    • (1998) Methods Enzymol. , vol.298 , pp. 570-592
    • Svitkina, T.M.1    Borisy, G.G.2
  • 44
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina, T.M., and G.G. Borisy. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-1026.
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 45
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: Mechanism of cell body translocation
    • Svitkina, T.M., A.B. Verkhovsky, K.M. McQuade, and G.G. Borisy. 1997. Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J. Cell Biol. 139:397-415.
    • (1997) J. Cell Biol. , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 47
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L. monocyrogenes in cells and in cell-free extracts
    • Theriot, J.A., J. Rosenblatt, D.A. Portnoy, P.J. Goldschmidt-Clermont, and T.J. Mitchison. 1994. Involvement of profilin in the actin-based motility of L. monocyrogenes in cells and in cell-free extracts. Cell. 76:505-517.
    • (1994) Cell , vol.76 , pp. 505-517
    • Theriot, J.A.1    Rosenblatt, J.2    Portnoy, D.A.3    Goldschmidt-Clermont, P.J.4    Mitchison, T.J.5
  • 48
    • 0031694209 scopus 로고    scopus 로고
    • Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells
    • Yamashiro, S., Y. Yamakita, S. Ono, and F. Matsumura. 1998. Fascin, an actin-bundling protein, induces membrane protrusions and increases cell motility of epithelial cells. Mol. Biol. Cell. 9:993-1006.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 993-1006
    • Yamashiro, S.1    Yamakita, Y.2    Ono, S.3    Matsumura, F.4
  • 49
    • 0021827569 scopus 로고
    • Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells
    • Yamashiro-Matsumura, S., and F. Matsumura. 1985. Purification and characterization of an F-actin-bundling 55-kilodalton protein from HeLa cells. J. Biol. Chem. 260:5087-5097.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5087-5097
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 50
    • 0033587188 scopus 로고    scopus 로고
    • The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex
    • Yarar, D., W. To, A. Abo, and M.D. Welch. 1999. The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9:555-558.
    • (1999) Curr. Biol. , vol.9 , pp. 555-558
    • Yarar, D.1    To, W.2    Abo, A.3    Welch, M.D.4
  • 51
    • 0035846598 scopus 로고    scopus 로고
    • Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities
    • Zalevsky, J., L. Lempert, H. Kranitz, and R.D. Mullins. 2001. Different WASP family proteins stimulate different Arp2/3 complex-dependent actin-nucleating activities. Curr. Biol. 11:1903-1913.
    • (2001) Curr. Biol. , vol.11 , pp. 1903-1913
    • Zalevsky, J.1    Lempert, L.2    Kranitz, H.3    Mullins, R.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.