메뉴 건너뛰기




Volumn 95, Issue 6, 1998, Pages 741-748

Spatial control of actin filament assembly: Lessons from Listeria

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; SIGNAL PEPTIDE;

EID: 0032411699     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81697-9     Document Type: Review
Times cited : (94)

References (48)
  • 1
    • 0031830659 scopus 로고    scopus 로고
    • Mutations in Drosophila enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1 ) and EVH2 domains
    • Ahern-Djamali, S.M., Comer, A.R., Bachmann, C., Kastenmeier, A.S., Reddy, S.K., Beckerle, M.C., Walter, U., and Huffman, P.M. (1998). Mutations in Drosophila Enabled and rescue by human vasodilator-stimulated phosphoprotein (VASP) indicate important functional roles for Ena/VASP homology domain 1 (EVH1 ) and EVH2 domains. Mol. Biol. Cell 9, 2157-2171.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2157-2171
    • Ahern-Djamali, S.M.1    Comer, A.R.2    Bachmann, C.3    Kastenmeier, A.S.4    Reddy, S.K.5    Beckerle, M.C.6    Walter, U.7    Huffman, P.M.8
  • 3
    • 0031281898 scopus 로고    scopus 로고
    • Zyxin: Zinc fingers at sites of cell adhesion
    • Beckerle, M.C. (1997). Zyxin: zinc fingers at sites of cell adhesion. Bioessays 19, 949-957.
    • (1997) Bioessays , vol.19 , pp. 949-957
    • Beckerle, M.C.1
  • 4
    • 0029761645 scopus 로고    scopus 로고
    • The focal-adhesion vasodilator-stimulated phospho-protein (VASP) binds to the proline-rich domain in vinculin
    • Brindle, N.P.J., Holt, M.R., Davies, J.E., Price, C.J., and Critchley, D.R. (1996). The focal-adhesion vasodilator-stimulated phospho-protein (VASP) binds to the proline-rich domain in vinculin. Biochem. J. 318, 753-757.
    • (1996) Biochem. J. , vol.318 , pp. 753-757
    • Brindle, N.P.J.1    Holt, M.R.2    Davies, J.E.3    Price, C.J.4    Critchley, D.R.5
  • 5
    • 0031908252 scopus 로고    scopus 로고
    • EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells
    • Chan, A.Y., Raft, S., Bailly, M., Wyckoff, J.B., Segall, J.E., and Condeelis, J.S. (1998). EGF stimulates an increase in actin nucleation and filament number at the leading edge of the lamellipod in mammary adenocarcinoma cells. J. Cell Sci. 111, p. 204.
    • (1998) J. Cell Sci. , vol.111 , pp. 204
    • Chan, A.Y.1    Raft, S.2    Bailly, M.3    Wyckoff, J.B.4    Segall, J.E.5    Condeelis, J.S.6
  • 6
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of Rac-1 GDP/ GTP exchange by the vav proto-oncogene product
    • Crespo, P., Schuebel, K.E., Ostrom, A.A., Gutkind, J.S., and Bustelo, X.R. (1997). Phosphotyrosine-dependent activation of Rac-1 GDP/ GTP exchange by the vav proto-oncogene product. Nature 385, 169-172.
    • (1997) Nature , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 7
    • 0026577663 scopus 로고
    • A novel bacterial gene in listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin
    • Domann, E., Wehland, J., Rohde, M., Pistor, S., Hartl, M., Goebel, W., Leimeister-Wächter, M., Wuenschner, M., and Chakraborty, T. (1992). A novel bacterial gene in Listeria monocytogenes required for host cell microfilament interaction with homology to the proline-rich region of vinculin. EMBO J. 11, 1981-1990.
    • (1992) EMBO J. , vol.11 , pp. 1981-1990
    • Domann, E.1    Wehland, J.2    Rohde, M.3    Pistor, S.4    Hartl, M.5    Goebel, W.6    Leimeister-Wächter, M.7    Wuenschner, M.8    Chakraborty, T.9
  • 8
    • 0028985980 scopus 로고
    • Lack of β-1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts
    • Fassler, R., Pfaff, M., Murphy, J., Noegel, A.A., Johansson, S., Timpl, R., and Albrecht, R. (1995). Lack of β-1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts. J. Cell Biol. 128, 979-988.
    • (1995) J. Cell Biol. , vol.128 , pp. 979-988
    • Fassler, R.1    Pfaff, M.2    Murphy, J.3    Noegel, A.A.4    Johansson, S.5    Timpl, R.6    Albrecht, R.7
  • 9
    • 0029079119 scopus 로고
    • Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function
    • Friederich, E., Gouin, E., Hellio, R., Kocks, C., Cossart, P., and Louvard, D. (1995). Targeting of Listeria monocytogenes ActA protein to the plasma membrane as a tool to dissect both actin-based cell morphogenesis and ActA function. EMBO J. 14, 2731-2744.
    • (1995) EMBO J. , vol.14 , pp. 2731-2744
    • Friederich, E.1    Gouin, E.2    Hellio, R.3    Kocks, C.4    Cossart, P.5    Louvard, D.6
  • 10
    • 0027052435 scopus 로고
    • Retrovirally introduced antisense integrin RNA inhibits neuroblast migration in vivo
    • Galileo, D.S., Majors, J., Horwitz, A.F., and Sanes, J.R. (1992). Retrovirally introduced antisense integrin RNA inhibits neuroblast migration in vivo. Neuron 9, 1117-1131.
    • (1992) Neuron , vol.9 , pp. 1117-1131
    • Galileo, D.S.1    Majors, J.2    Horwitz, A.F.3    Sanes, J.R.4
  • 11
    • 0030592559 scopus 로고    scopus 로고
    • Mena, a relative of VASP and Drosophila enabled, is implicated in the control of microfilament dynamics
    • Gertler, F.B., Niebuhr, K., Reinhard, M., Wehland, J., and Soriano, P. (1996). Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics. Cell 87, 227-239.
    • (1996) Cell , vol.87 , pp. 227-239
    • Gertler, F.B.1    Niebuhr, K.2    Reinhard, M.3    Wehland, J.4    Soriano, P.5
  • 12
    • 0030828053 scopus 로고    scopus 로고
    • Structural and functional similarities between the human cytoskeletal protein, zyxin, and the ActA protein of Listeria monocytogenes
    • Golsteyn, R., Beckerle, M.C., Koay, T., Louvard, D., and Friederich, E. (1997). Structural and functional similarities between the human cytoskeletal protein, zyxin, and the ActA protein of Listeria monocytogenes. J. Cell Sci. 10, 1893-1906.
    • (1997) J. Cell Sci. , vol.10 , pp. 1893-1906
    • Golsteyn, R.1    Beckerle, M.C.2    Koay, T.3    Louvard, D.4    Friederich, E.5
  • 13
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J.H., Bokoch, G.M., Carpenter, C.L., Janmey, P.A., Taylor, L.A., Toker, A., and Stossel, T.P. (1995). Thrombin receptor ligation and activated Rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82, 643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 14
    • 0029985426 scopus 로고    scopus 로고
    • SH3 domain-dependent interaction of vav with the LIM-domain protein zyxin
    • Hobert, O., Schilling, J.W., Beckerle, M.C., Ullrich, A., and Jallal, B. (1996). SH3 domain-dependent interaction of vav with the LIM-domain protein zyxin. Oncogene 12, 1577-1581.
    • (1996) Oncogene , vol.12 , pp. 1577-1581
    • Hobert, O.1    Schilling, J.W.2    Beckerle, M.C.3    Ullrich, A.4    Jallal, B.5
  • 15
    • 0030851599 scopus 로고    scopus 로고
    • Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): Implications for actin-based Listeria motility
    • Kang, F., Laine, R.O., Rubb, J.R., Southwick, F.S., and Purich, D.L. (1997). Profilin interacts with the Gly-Pro-Pro-Pro-Pro-Pro sequences of vasodilator-stimulated phosphoprotein (VASP): implications for actin-based Listeria motility. Biochemistry 36, 8384-8392.
    • (1997) Biochemistry , vol.36 , pp. 8384-8392
    • Kang, F.1    Laine, R.O.2    Rubb, J.R.3    Southwick, F.S.4    Purich, D.L.5
  • 16
    • 0028786352 scopus 로고
    • Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba
    • Kelleher, J.F., Atkinson, S.J., and Pollard, T.D. (1995). Sequences, structural models, and cellular localization of the actin-related proteins Arp2 and Arp3 from Acanthamoeba. J. Cell Biol. 131, 385-397.
    • (1995) J. Cell Biol. , vol.131 , pp. 385-397
    • Kelleher, J.F.1    Atkinson, S.J.2    Pollard, T.D.3
  • 17
    • 0026515440 scopus 로고
    • Listeria monocytogenes-induced actin assembly requires the actA gene product, a surface protein
    • Kocks, C., Gouin, E., Tabouret, M., Berche, P., Ohayon, H., and Cossart, P. (1992). Listeria monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68, 521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 18
    • 0029591170 scopus 로고
    • The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocula and Escherichia coli respectively
    • Kocks, C., Marchand, J.B., Gouin, G., d'Hauteville, H., Sansonetti, P.J., Carlier, M.F., and Cossart, P. (1995). The unrelated surface proteins ActA of Listeria monocytogenes and IcsA of Shigella flexneri are sufficient to confer actin-based motility on Listeria innocula and Escherichia coli respectively. Mol. Microbiol. 18, 413-423.
    • (1995) Mol. Microbiol. , vol.18 , pp. 413-423
    • Kocks, C.1    Marchand, J.B.2    Gouin, G.3    D'Hauteville, H.4    Sansonetti, P.J.5    Carlier, M.F.6    Cossart, P.7
  • 19
    • 0029609261 scopus 로고
    • The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator
    • Lasa, I., David, V., Gouin, E., Marchand, J.P., and Cossart, P. (1995). The amino-terminal part of ActA is critical for the actin-based motility of Listeria monocytogenes; the central proline-rich region acts as a stimulator. Mol. Microbiol. 18, 425-426.
    • (1995) Mol. Microbiol. , vol.18 , pp. 425-426
    • Lasa, I.1    David, V.2    Gouin, E.3    Marchand, J.P.4    Cossart, P.5
  • 20
    • 0021919105 scopus 로고
    • Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin
    • Lassing, I., and Lindberg, U. (1985). Specific interaction between phosphatidylinositol 4,5-bisphosphate and profilactin. Nature 314, 472-474.
    • (1985) Nature , vol.314 , pp. 472-474
    • Lassing, I.1    Lindberg, U.2
  • 21
    • 0032498854 scopus 로고    scopus 로고
    • Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 inducing actin assembly in Xenopusegg extracts
    • Ma, L., Cantley, L.C., Janmey, P.A., and Kirschner, M.W. (1998). Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 inducing actin assembly in Xenopusegg extracts. J. Cell Biol. 140, 1125-1136.
    • (1998) J. Cell Biol. , vol.140 , pp. 1125-1136
    • Ma, L.1    Cantley, L.C.2    Janmey, P.A.3    Kirschner, M.W.4
  • 22
    • 0030670302 scopus 로고    scopus 로고
    • Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionary conserved proteins
    • Machesky, L.M., Reeves, E., Wientjes, F., Mattheyse, F.J., Grogan, A., Totty, N.F., Burlingame, A.L., Hsuan, J.J., and Segal, A.W. (1997). Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionary conserved proteins. Biochem. J. 328, 105-112.
    • (1997) Biochem. J. , vol.328 , pp. 105-112
    • Machesky, L.M.1    Reeves, E.2    Wientjes, F.3    Mattheyse, F.J.4    Grogan, A.5    Totty, N.F.6    Burlingame, A.L.7    Hsuan, J.J.8    Segal, A.W.9
  • 23
    • 0028981496 scopus 로고
    • Actin-based movement of Listeria monocytogenes: Actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface
    • Marchand, J.-P., Moreau, P., Paoletti, A., Cossart, P., Carlier, M.-F., and Pantaloni, D. (1995). Actin-based movement of Listeria monocytogenes: actin assembly results from the local maintenance of uncapped filament barbed ends at the bacterium surface. J. Cell Biol. 130, 331-343.
    • (1995) J. Cell Biol. , vol.130 , pp. 331-343
    • Marchand, J.-P.1    Moreau, P.2    Paoletti, A.3    Cossart, P.4    Carlier, M.-F.5    Pantaloni, D.6
  • 24
    • 0029849062 scopus 로고    scopus 로고
    • The schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin
    • McCollum, D., Feoktistova, A., Morphew, M., Balasubramanian, M., and Gould, K.L. (1996). The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin. EMBO J. 15, 6438-6446.
    • (1996) EMBO J. , vol.15 , pp. 6438-6446
    • McCollum, D.1    Feoktistova, A.2    Morphew, M.3    Balasubramanian, M.4    Gould, K.L.5
  • 25
    • 0029959468 scopus 로고    scopus 로고
    • The saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton
    • Moreau, V., Madania, A., Martin, R.P., and Winson, B. (1996). The Saccharomyces cerevisiae actin-related protein Arp2 is involved in the actin cytoskeleton. J. Cell Biol. 134, 117-132.
    • (1996) J. Cell Biol. , vol.134 , pp. 117-132
    • Moreau, V.1    Madania, A.2    Martin, R.P.3    Winson, B.4
  • 27
    • 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., Heuser, J.A., and Pollard, T.D. (1998a). The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. PNAS 95, 6181-6186.
    • (1998) PNAS , vol.95 , pp. 6181-6186
    • Mullins, R.D.1    Heuser, J.A.2    Pollard, T.D.3
  • 28
    • 0031922638 scopus 로고    scopus 로고
    • Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments
    • Mullins, R.D., Kelleher, J.F., Xu, J., and Pollard, T.O. (1998b). Arp2/3 complex from Acanthamoeba binds profilin and cross-links actin filaments. Mol. Cell Biol. 9, 841-852.
    • (1998) Mol. Cell Biol. , vol.9 , pp. 841-852
    • Mullins, R.D.1    Kelleher, J.F.2    Xu, J.3    Pollard, T.O.4
  • 29
    • 0030864520 scopus 로고    scopus 로고
    • A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
    • Niebuhr, K., Ebel, F., Frank, R., Reinhard, M., Domann, E., Carl, D.D., Walter, U., Gertler, F.B., Wehland, J., and Chakraborty, T. (1997). A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family. EMBO J. 16, 5433-5444.
    • (1997) EMBO J. , vol.16 , pp. 5433-5444
    • Niebuhr, K.1    Ebel, F.2    Frank, R.3    Reinhard, M.4    Domann, E.5    Carl, U.D.6    Walter, U.7    Gertler, F.B.8    Wehland, J.9    Chakraborty, T.10
  • 30
    • 0030466893 scopus 로고    scopus 로고
    • Facio-genital dysplasia protein (FGD1) and vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases
    • Olson, M.F., Pasteris, N.G., Gorski, J.L., and Hall, A. (1996). Facio-genital dysplasia protein (FGD1) and vav, two related proteins required for normal embryonic development, are upstream regulators of Rho GTPases. Curr. Biol. 6, 1628-1633.
    • (1996) Curr. Biol. , vol.6 , pp. 1628-1633
    • Olson, M.F.1    Pasteris, N.G.2    Gorski, J.L.3    Hall, A.4
  • 31
    • 0028117139 scopus 로고
    • The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton
    • Pistor, S., Chakraborty, T., Niebuhr, K., Domann, E., and Wehland, J. (1994). The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton. EMBO J. 13, 758-763.
    • (1994) EMBO J. , vol.13 , pp. 758-763
    • Pistor, S.1    Chakraborty, T.2    Niebuhr, K.3    Domann, E.4    Wehland, J.5
  • 32
    • 0029294733 scopus 로고
    • The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins
    • Pistor, S., Chakraborty, T., Walter, U., and Wehland, J. (1995). The bacterial actin nucleator protein ActA of Listeria monocytogenes contains multiple binding sites for host microfilament proteins. Curr. Biol. 5, 517-525.
    • (1995) Curr. Biol. , vol.5 , pp. 517-525
    • Pistor, S.1    Chakraborty, T.2    Walter, U.3    Wehland, J.4
  • 33
    • 0029025248 scopus 로고
    • The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins
    • Reinhard, M., Giehl, C., Abel, K., Haffner, C., Jarchau, T., Hoppe, V., Jockusch, B.M., and Walter, U. (1995a). The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 74, 1583-1589.
    • (1995) EMBO J. , vol.74 , pp. 1583-1589
    • Reinhard, M.1    Giehl, C.2    Abel, K.3    Haffner, C.4    Jarchau, T.5    Hoppe, V.6    Jockusch, B.M.7    Walter, U.8
  • 34
    • 0029157584 scopus 로고
    • Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard, M., Jouvenal, K., Tripier, D., and Walter, U. (1995b). Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). PNAS 92, 7956-7960.
    • (1995) PNAS , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 35
    • 0027080110 scopus 로고
    • Zyxin and cCRP: Two interactive LIM domain proteins associated with the cytoskeleton
    • Sadler, I., Crawford, A.W., Michelsen, J.W., and Beckerle, M.C. (1992). Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. J. Cell Biol. 119, 1573-1587.
    • (1992) J. Cell Biol. , vol.119 , pp. 1573-1587
    • Sadler, I.1    Crawford, A.W.2    Michelsen, J.W.3    Beckerle, M.C.4
  • 36
    • 0026663057 scopus 로고
    • Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes
    • Sanger, J.M., Sanger, J.W., and Southwick, F.S. (1992). Host cell actin assembly is necessary and likely to provide the propulsive force for intracellular movement of Listeria monocytogenes. Infect. Immun. 60, 3609-3619.
    • (1992) Infect. Immun. , vol.60 , pp. 3609-3619
    • Sanger, J.M.1    Sanger, J.W.2    Southwick, F.S.3
  • 37
    • 0011086565 scopus 로고
    • New York: Academic Press, Inc.
    • Smith, D.S. (1972). Muscle. (New York: Academic Press, Inc.), p. 9.
    • (1972) Muscle , pp. 9
    • Smith, D.S.1
  • 38
    • 0029807736 scopus 로고    scopus 로고
    • The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin
    • Smith, G.A., Theriot, J.A., and Portnoy, D.A. (1996). The tandem repeat domain in the Listeria monocytogenes ActA protein controls the rate of actin-based motility, the percentage of moving bacteria, and the localization of vasodilator-stimulated phosphoprotein and profilin. J. Cell Biol. 135, 647-660.
    • (1996) J. Cell Biol. , vol.135 , pp. 647-660
    • Smith, G.A.1    Theriot, J.A.2    Portnoy, D.A.3
  • 39
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocyctes: Mechanism of cell body translocation
    • Svitkina, T.M., Verkhovsky, A.B., McQuade, K.M., and Borisy, G.G. (1997). Analysis of the actin-myosin II system in fish epidermal keratocyctes: 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
  • 40
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • Theriot, J.A., Mitchison, T.J., Tilney, L.G., and Portnoy, D.A. (1992). The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization. Nature 357, 257-260.
    • (1992) Nature , vol.357 , pp. 257-260
    • Theriot, J.A.1    Mitchison, T.J.2    Tilney, L.G.3    Portnoy, D.A.4
  • 41
    • 0028173688 scopus 로고
    • Involvement of profilin in the actin-based motility of L monocytogenes in cells and cell-free extracts
    • Theriot, J.A., Rosenblatt, J., Portnoy, D.A., Goldschimdt-Clermont, P.J., and Mitchison, T.J. (1994). Involvement of profilin in the actin-based motility of L monocytogenes in cells and 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    Goldschimdt-Clermont, P.J.4    Mitchison, T.J.5
  • 42
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite Listeria monocytogenes
    • Tilney, L.G., and Portnoy, D.A. (1989). Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite Listeria monocytogenes. J. Cell Biol. 109, 1597-1608.
    • (1989) J. Cell Biol. , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 43
    • 0020570679 scopus 로고
    • Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent
    • Tilney, L.G., Egelman, E.H., DeRosier, D.J., and Saunder, J.C. (1983). Actin filaments, stereocilia, and hair cells of the bird cochlea. II. packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent. J. Cell Biol. 96, p. 824.
    • (1983) J. Cell Biol. , vol.96 , pp. 824
    • Tilney, L.G.1    Egelman, E.H.2    DeRosier, D.J.3    Saunder, J.C.4
  • 44
    • 0031021153 scopus 로고    scopus 로고
    • Actin poly-merization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., Iwamatsu, A., and Mitchison, T.J. (1997a). Actin poly-merization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385, 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 45
    • 0030802671 scopus 로고    scopus 로고
    • The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly
    • Welch, M.D., DePace, A.H., Verma, S., Iwamatsu, A., and Mitchison, T.J. (1997b). The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. J. Cell Biol. 138, 375-384.
    • (1997) J. Cell Biol. , vol.138 , pp. 375-384
    • Welch, M.D.1    DePace, A.H.2    Verma, S.3    Iwamatsu, A.4    Mitchison, T.J.5
  • 46
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch, M.D., Rosenblatt, J., Skoble, J., Portnoy, D.A., and Mitchison, T.J. (1998). Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281, 105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 47
  • 48
    • 0032563603 scopus 로고    scopus 로고
    • Mechanism of Cdc42-induced actin polymerization in neutrophil extracts
    • Zigmond, S.H., Joyce, M., Yang, C., Brown, K., Huang, M., and Pring, M. (1998). Mechanism of Cdc42-induced actin polymerization in neutrophil extracts. J. Cell Biol. 142, 1001-1012.
    • (1998) J. Cell Biol. , vol.142 , pp. 1001-1012
    • Zigmond, S.H.1    Joyce, M.2    Yang, C.3    Brown, K.4    Huang, M.5    Pring, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.