메뉴 건너뛰기




Volumn 79, Issue 9, 2014, Pages 917-927

Intracellular transport based on actin polymerization

Author keywords

"comet like tails"; actin; Arp2 3; cytoskeleton; dynamin; intracellular vesicles

Indexed keywords

ACTIN; DYNAMIN;

EID: 84920930176     PISSN: 00062979     EISSN: 16083040     Source Type: Journal    
DOI: 10.1134/S0006297914090089     Document Type: Review
Times cited : (26)

References (79)
  • 1
    • 0028942256 scopus 로고
    • Actin- and microtubule-dependent organelle motors: Interrelationships between the two motility systems
    • 7755993 10.1016/0955-0674(95)80048-4 1:CAS:528:DyaK2MXjsVyktrY%3D
    • Langford, G. M. (1995) Actin- and microtubule-dependent organelle motors: interrelationships between the two motility systems, Curr. Opin. Cell Biol., 7, 82-88.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 82-88
    • Langford, G.M.1
  • 2
    • 84855337379 scopus 로고    scopus 로고
    • The myosin family: Unconventional roles of actin-dependent molecular motors in immune cells
    • Maravillas-Montero, J., and Santos-Argumedo, L. (2013) The myosin family: unconventional roles of actin-dependent molecular motors in immune cells, J. Leukocyte Biol., 91, 35-45.
    • (2013) J. Leukocyte Biol. , vol.91 , pp. 35-45
    • Maravillas-Montero, J.1    Santos-Argumedo, L.2
  • 3
    • 84355161386 scopus 로고    scopus 로고
    • Walking to work: Roles for class v myosins as cargo transporters
    • 1:CAS:528:DC%2BC3MXhsFOitL7L
    • Hammer, J. A., 3rd, and Sellers, J. R. (2012) Walking to work: roles for class V myosins as cargo transporters, Nat. Rev. Mol. Cell. Biol., 13, 13-26.
    • (2012) Nat. Rev. Mol. Cell. Biol. , vol.13 , pp. 13-26
    • Hammer, J.A.1    Sellers, J.R.2
  • 4
    • 0033527043 scopus 로고    scopus 로고
    • Myosin-V is a processive actin-based motor
    • 10448864 10.1038/23072 1:CAS:528:DyaK1MXltFKrsLY%3D
    • Mehta, A. D., Rock, R. S., Rief, M., Spudich, J. A., Mooseker, M. S., and Cheney, R. E. (1999) Myosin-V is a processive actin-based motor, Nature, 400, 590-593.
    • (1999) Nature , vol.400 , pp. 590-593
    • Mehta, A.D.1    Rock, R.S.2    Rief, M.3    Spudich, J.A.4    Mooseker, M.S.5    Cheney, R.E.6
  • 5
    • 0037175377 scopus 로고    scopus 로고
    • Activation of myosin V-based motility and F-actin-dependent network formation of endoplasmic reticulum during mitosis
    • Wollert, T. D., Weiss, G., Gerdes, H.-H., and Kuznetsov, S. A. (2002) Activation of myosin V-based motility and F-actin-dependent network formation of endoplasmic reticulum during mitosis, J. Cell Biol., 150, 571-577.
    • (2002) J. Cell Biol. , vol.150 , pp. 571-577
    • Wollert, T.D.1    Weiss, G.2    Gerdes, H.-H.3    Kuznetsov, S.A.4
  • 6
    • 84877582279 scopus 로고    scopus 로고
    • Myosin-V opposes microtubule-based cargo transport and drives directional motility on cortical actin
    • 23602478 10.1016/j.cub.2013.03.068 1:CAS:528:DC%2BC3sXmt1Cmt78%3D
    • Kapitein, L. C., van Bergeijk, P., Lipka, J., Keijzer, N., Wulf, P. S., Katrukha, E. A., Akhmanova, A., and Hoogenraad, C. C. (2013) Myosin-V opposes microtubule-based cargo transport and drives directional motility on cortical actin, Curr. Biol., 23, 828-834.
    • (2013) Curr. Biol. , vol.23 , pp. 828-834
    • Kapitein, L.C.1    Van Bergeijk, P.2    Lipka, J.3    Keijzer, N.4    Wulf, P.S.5    Katrukha, E.A.6    Akhmanova, A.7    Hoogenraad, C.C.8
  • 8
    • 84858123747 scopus 로고    scopus 로고
    • Molecular motors in cargo trafficking and synapse assembly
    • 22351056 10.1007/978-3-7091-0932-8-8
    • Van den Berg, R., and Hoogenraad, C. C. (2012) Molecular motors in cargo trafficking and synapse assembly, Adv. Exp. Med. Biol., 970, 173-196.
    • (2012) Adv. Exp. Med. Biol. , vol.970 , pp. 173-196
    • Van Den Berg, R.1    Hoogenraad, C.C.2
  • 9
    • 42449129759 scopus 로고    scopus 로고
    • Myosin v and kinesin act as tethers to enhance each others' processivity
    • 18347333 10.1073/pnas.0711531105 1:CAS:528:DC%2BD1cXkt12qs7c%3D 2290781
    • Ali, M. Y., Lu, H., Bookwalter, C. S., Warshaw, D. M., and Trybus, K. M. (2008) Myosin V and kinesin act as tethers to enhance each others' processivity, Proc. Natl. Acad. Sci. USA, 105, 4691-4696.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 4691-4696
    • Ali, M.Y.1    Lu, H.2    Bookwalter, C.S.3    Warshaw, D.M.4    Trybus, K.M.5
  • 10
    • 39149138988 scopus 로고    scopus 로고
    • Cargo transport: Molecular motors navigate a complex cytoskeleton
    • 18226515 10.1016/j.ceb.2007.11.006 1:CAS:528:DC%2BD1cXhvVWgsL0%3D 2688467
    • Ross, J. L., Ali, M. Y., and Warshaw, D. M. (2008) Cargo transport: molecular motors navigate a complex cytoskeleton, Curr. Opin. Cell Biol., 20, 41-47.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 41-47
    • Ross, J.L.1    Ali, M.Y.2    Warshaw, D.M.3
  • 11
    • 77951207269 scopus 로고    scopus 로고
    • Motor number controls cargo switching at actin-microtubule intersections in vitro
    • 20399098 10.1016/j.cub.2010.03.024 1:CAS:528:DC%2BC3cXlsFCrs7w%3D
    • Schroeder, H. W., III, Mitchell, C., Shuman, H., Holzbaur, E. L., and Goldman, Y. E. (2010) Motor number controls cargo switching at actin-microtubule intersections in vitro, Curr. Biol., 20, 687-696.
    • (2010) Curr. Biol. , vol.20 , pp. 687-696
    • Schroeder, H.W.1    Mitchell, C.2    Shuman, H.3    Holzbaur, E.L.4    Goldman, Y.E.5
  • 12
    • 42049092972 scopus 로고    scopus 로고
    • Regulation of actin assembly associated with protrusion and adhesion in cell migration
    • 18391171 10.1152/physrev.00021.2007
    • Le Clainche, C., and Carlier, M.-F. (2008) Regulation of actin assembly associated with protrusion and adhesion in cell migration, Physiol. Rev., 88, 489-513.
    • (2008) Physiol. Rev. , vol.88 , pp. 489-513
    • Le Clainche, C.1    Carlier, M.-F.2
  • 13
    • 0037195267 scopus 로고    scopus 로고
    • Dynamin 2 and cortactin regulate actin assembly and filament organization
    • 12419186 10.1016/S0960-9822(02)01228-9 1:CAS:528:DC%2BD38XosFOiu7s%3D
    • Schafer, D. A., Weed, S. A., Binns, D., Karginov, A. V., Parsons, J. T., and Cooper, J. A. (2002) Dynamin 2 and cortactin regulate actin assembly and filament organization, Curr. Biol., 12, 1852-1857.
    • (2002) Curr. Biol. , vol.12 , pp. 1852-1857
    • Schafer, D.A.1    Weed, S.A.2    Binns, D.3    Karginov, A.V.4    Parsons, J.T.5    Cooper, J.A.6
  • 15
    • 0037039414 scopus 로고    scopus 로고
    • The large GTPase dynamin regulates actin comet formation and movement in living cells
    • 11782546 10.1073/pnas.012607899 1:CAS:528:DC%2BD38Xlt1Cgtg%3D%3D 117533
    • Orth, J. D., Krueger, E. W., Cao, H., and McNiven, M. A. (2002) The large GTPase dynamin regulates actin comet formation and movement in living cells, Proc. Natl. Acad. Sci. USA, 99, 167-172.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 167-172
    • Orth, J.D.1    Krueger, E.W.2    Cao, H.3    McNiven, M.A.4
  • 16
    • 0036714223 scopus 로고    scopus 로고
    • Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits
    • 12198492 10.1038/ncb837 1:CAS:528:DC%2BD38Xms1aht7s%3D
    • Merrifield, C. J., Feldman, M. E., Wan, L., and Almers, W. (2002) Imaging actin and dynamin recruitment during invagination of single clathrin-coated pits, Nature Cell Biol., 4, 691-698.
    • (2002) Nature Cell Biol. , vol.4 , pp. 691-698
    • Merrifield, C.J.1    Feldman, M.E.2    Wan, L.3    Almers, W.4
  • 17
    • 0034614930 scopus 로고    scopus 로고
    • Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP
    • 10662777 10.1083/jcb.148.3.519 1:CAS:528:DC%2BD3cXhtFSqt78%3D 2174808
    • Taunton, J., Rowning, B. A., Coughlin, M. L., Wu, M., Moon, R. T., Mitchison, T. J., and Larabell, C. A. (2000) Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP, J. Cell. Biol., 148, 519-530.
    • (2000) J. Cell. Biol. , vol.148 , pp. 519-530
    • Taunton, J.1    Rowning, B.A.2    Coughlin, M.L.3    Wu, M.4    Moon, R.T.5    Mitchison, T.J.6    Larabell, C.A.7
  • 18
    • 17144439652 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft enriched vesicles through WASP-Arp2/3
    • 10744973 10.1016/S0960-9822(00)00384-5 1:CAS:528:DC%2BD3cXitFegtrk%3D
    • Rozelle, A. L., Machesky, L. M., Yamamoto, M., Driessens, M. H., Insall, R. H., Roth, M. G., Luby-Phelps, K., Marriott, G., Hall, A., and Yin, H. L. (2000) Phosphatidylinositol 4,5-bisphosphate induces actin-based movement of raft enriched vesicles through WASP-Arp2/3, Curr. Biol., 10, 311-320.
    • (2000) Curr. Biol. , vol.10 , pp. 311-320
    • Rozelle, A.L.1    Machesky, L.M.2    Yamamoto, M.3    Driessens, M.H.4    Insall, R.H.5    Roth, M.G.6    Luby-Phelps, K.7    Marriott, G.8    Hall, A.9    Yin, H.L.10
  • 19
    • 60349086029 scopus 로고    scopus 로고
    • Spindle positioning: Actin mediates pushing and pulling
    • Bezanilla, M., and Wadsworth, P. (2008) Spindle positioning: actin mediates pushing and pulling, Curr. Biol., 19, R168-R169.
    • (2008) Curr. Biol. , vol.19 , pp. 168-R169
    • Bezanilla, M.1    Wadsworth, P.2
  • 20
    • 79951552071 scopus 로고    scopus 로고
    • Nuclear and spindle positioning during oocyte meiosis
    • 20708397 10.1016/j.ceb.2010.07.008 1:CAS:528:DC%2BC3MXit12ju70%3D 2994957
    • Fabritius, A. S., Ellefson, M. L., and McNally, J. (2011) Nuclear and spindle positioning during oocyte meiosis, Curr. Opin. Cell Biol., 23, 78-84.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 78-84
    • Fabritius, A.S.1    Ellefson, M.L.2    McNally, J.3
  • 21
    • 84875422207 scopus 로고    scopus 로고
    • The road to maturation: Somatic cell interaction and self-organization of the mammalian oocyte
    • 23429793 10.1038/nrm3531 1:CAS:528:DC%2BC3sXivVKmsrY%3D
    • Li, R., and Albertini, D. F. (2013) The road to maturation: somatic cell interaction and self-organization of the mammalian oocyte, Nat. Rev. Mol. Cell. Biol., 14, 141-152.
    • (2013) Nat. Rev. Mol. Cell. Biol. , vol.14 , pp. 141-152
    • Li, R.1    Albertini, D.F.2
  • 22
    • 0024988340 scopus 로고
    • Atomic structure of the actin-DNase i complex
    • 2395459 10.1038/347037a0 1:CAS:528:DyaK3cXls1yjsLk%3D
    • Kabsch, W., Mannherz, H. G., Suck, D., Pai, E. F., and Holmes, K. C. (1990) Atomic structure of the actin-DNase I complex, Nature, 347, 37-44.
    • (1990) Nature , vol.347 , pp. 37-44
    • Kabsch, W.1    Mannherz, H.G.2    Suck, D.3    Pai, E.F.4    Holmes, K.C.5
  • 23
    • 85010916780 scopus 로고
    • The structure of F-actin and of actin filaments isolated from muscle
    • 1:CAS:528:DyaF3sXnsVGhtg%3D%3D
    • Hanson, J., and Lowy, J. (1963) The structure of F-actin and of actin filaments isolated from muscle, J. Mol. Biol., 6, 46-60.
    • (1963) J. Mol. Biol. , vol.6 , pp. 46-60
    • Hanson, J.1    Lowy, J.2
  • 24
    • 79955859521 scopus 로고    scopus 로고
    • Actin structure and function
    • 21314430 10.1146/annurev-biophys-042910-155359 1:CAS:528:DC%2BC3MXnvFaitbk%3D 3130349
    • Dominguez, R., and Holmes, K. C. (2011) Actin structure and function, Annu. Rev. Biophys., 40, 169-186.
    • (2011) Annu. Rev. Biophys. , vol.40 , pp. 169-186
    • Dominguez, R.1    Holmes, K.C.2
  • 25
    • 0016826292 scopus 로고
    • Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method
    • 240859 10.1083/jcb.67.1.231 1:CAS:528:DyaE2MXlsVegsL0%3D
    • Woodrum, D. T., Rich, S. A., and Pollard, T. D. (1975) Evidence for biased bidirectional polymerization of actin filaments using heavy meromyosin prepared by an improved method, J. Cell Biol., 67, 231-237.
    • (1975) J. Cell Biol. , vol.67 , pp. 231-237
    • Woodrum, D.T.1    Rich, S.A.2    Pollard, T.D.3
  • 26
    • 0035909233 scopus 로고    scopus 로고
    • ATPase activity and conformational changes in the regulation of actin
    • 11690650 10.1016/S0167-4838(01)00255-2 1:CAS:528:DC%2BD3MXnvFCrsrY%3D
    • Schuler, H. (2001) ATPase activity and conformational changes in the regulation of actin, Biochim. Biophys. Acta, 1549, 137-147.
    • (2001) Biochim. Biophys. Acta , vol.1549 , pp. 137-147
    • Schuler, H.1
  • 27
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • 12600310 10.1016/S0092-8674(03)00120-X 1:CAS:528:DC%2BD3sXhs1SnsL0%3D
    • Pollard, T. D., and Borisy, G. G. (2003) Cellular motility driven by assembly and disassembly of actin filaments, Cell, 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 28
    • 0035947404 scopus 로고    scopus 로고
    • Mechanism of actin-based motility
    • 11379633 10.1126/science.1059975 1:CAS:528:DC%2BD3MXktVyrurs%3D
    • Pantaloni, D., Le Clainche, C., and Carlier, M.-F. (2001) Mechanism of actin-based motility, Science, 292, 1502-1506.
    • (2001) Science , vol.292 , pp. 1502-1506
    • Pantaloni, D.1    Le Clainche, C.2    Carlier, M.-F.3
  • 29
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: Matching assembly factors with cellular structures
    • 17909522 10.1038/ncb1007-1110 1:CAS:528:DC%2BD2sXhtFSntbzO
    • Chhabra, E. S., and Higgs, H. N. (2007) The many faces of actin: matching assembly factors with cellular structures, Nat. Cell Biol., 9, 1110-1121.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 30
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors - Structure-function relationships
    • Domingues, R. (2009) Actin filament nucleation and elongation factors - structure-function relationships, Crit. Rev. Biochem. Mol. Biol., 44, 351-366.
    • (2009) Crit. Rev. Biochem. Mol. Biol. , vol.44 , pp. 351-366
    • Domingues, R.1
  • 31
    • 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
    • 9600938 10.1073/pnas.95.11.6181 1:CAS:528:DyaK1cXjtlKntrY%3D 27619
    • Mullins, R. D., Heuser, J. A., and Pollard, T. D. (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
  • 32
    • 0029621142 scopus 로고
    • Improved procedures for electron microscopic visualization of the cytoskeleton of cultured cells
    • 8573471 10.1006/jsbi.1995.1054 1:STN:280:DyaK287it12luw%3D%3D
    • Svitkina, T. M., Verkhovsky, A. B., and Borisy, G. G. (1995) Improved procedures for electron microscopic visualization of the cytoskeleton of cultured cells, J. Struct. Biol., 115, 290-303.
    • (1995) J. Struct. Biol. , vol.115 , pp. 290-303
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 33
    • 1842430006 scopus 로고    scopus 로고
    • Bacterial invasion: The paradigms of enteroinvasive pathogens
    • 15073367 10.1126/science.1090124 1:CAS:528:DC%2BD2cXivV2isbk%3D
    • Cossart, P., and Sansonetti, P. J. (2004) Bacterial invasion: the paradigms of enteroinvasive pathogens, Science, 304, 242-248.
    • (2004) Science , vol.304 , pp. 242-248
    • Cossart, P.1    Sansonetti, P.J.2
  • 34
    • 0026547790 scopus 로고
    • The rate of actin-based motility of intracellular Listeria monocytogenes equals the rate of actin polymerization
    • 1589024 10.1038/357257a0 1:CAS:528:DyaK38Xkt1aqu7s%3D
    • 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
  • 35
    • 0025606399 scopus 로고
    • Actin filament nucleation by the bacterial pathogen, Listeria monocytogenes
    • 2125302 10.1083/jcb.111.6.2979 1:CAS:528:DyaK3MXjtlGr
    • Tilney, L. G., Connelly, P. S., and Portnoy, D. A. (1990) Actin filament nucleation by the bacterial pathogen, Listeria monocytogenes, J. Cell Biol., 111, 2979-2988.
    • (1990) J. Cell Biol. , vol.111 , pp. 2979-2988
    • Tilney, L.G.1    Connelly, P.S.2    Portnoy, D.A.3
  • 36
    • 0025239739 scopus 로고
    • Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocyte-like cell line Caco-2
    • Mounier, J., Ryter, A., Coquis-Rondon, M., and Sansonetti, P. J. (1989) Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocyte-like cell line Caco-2, Infect. Immun., 58, 1048-1058.
    • (1989) Infect. Immun. , vol.58 , pp. 1048-1058
    • Mounier, J.1    Ryter, A.2    Coquis-Rondon, M.3    Sansonetti, P.J.4
  • 37
    • 0033055077 scopus 로고    scopus 로고
    • A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii
    • 10318762 1:CAS:528:DyaK1MXktVCisL4%3D
    • Gouin, E., Gantelet, H., Egile, C., Lasa, I., Ohayon, H., Villiers, V., Gounon, P., Sansonetti, P. J., and Cossart, P. (1999) A comparative study of the actin-based motilities of the pathogenic bacteria Listeria monocytogenes, Shigella flexneri and Rickettsia conorii, J. Cell Sci., 112, 1697-1708.
    • (1999) J. Cell Sci. , vol.112 , pp. 1697-1708
    • Gouin, E.1    Gantelet, H.2    Egile, C.3    Lasa, I.4    Ohayon, H.5    Villiers, V.6    Gounon, P.7    Sansonetti, P.J.8    Cossart, P.9
  • 38
    • 13444301168 scopus 로고    scopus 로고
    • Actin-based motility of intracellular pathogens
    • 15694855 10.1016/j.mib.2004.12.013 1:CAS:528:DC%2BD2MXhtV2ks7Y%3D
    • Gouin, E., Welch, M. D., and Cossart, P. (2005) Actin-based motility of intracellular pathogens, Curr. Opin. Microbiol., 8, 35-45.
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 35-45
    • Gouin, E.1    Welch, M.D.2    Cossart, P.3
  • 39
    • 0028117139 scopus 로고
    • The ActA protein of Listeria monocytogenes acts as a nucleator inducing reorganization of the actin cytoskeleton
    • 8112291 1:CAS:528:DyaK2cXivFagsL4%3D 394872
    • 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
  • 40
    • 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 innocua and Escherichia coli, respectively
    • 8748026 10.1111/j.1365-2958.1995.mmi-18030413.x 1:CAS:528:DyaK2MXpvVeku7o%3D
    • Kocks, C., Marchand, J. B., Gouin, E., 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 innocua 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, E.3    D'Hauteville, H.4    Sansonetti, P.J.5    Carlier, M.F.6    Cossart, P.7
  • 41
    • 0024362336 scopus 로고
    • Identification of IcsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin
    • 2542950 10.1073/pnas.86.10.3867 1:CAS:528:DyaL1MXktFynt7Y%3D 287242
    • Bernardini, M. L., Mounier, J., Hauteville, H. L., Coquis-Ronton, M., and Sansonetti, P. J. (1989) Identification of IcsA, a plasmid locus of Shigella flexneri that governs bacterial intra- and intercellular spread through interaction with F-actin, Proc. Nat. Acad. Sci. USA, 86, 3867-3871.
    • (1989) Proc. Nat. Acad. Sci. USA , vol.86 , pp. 3867-3871
    • Bernardini, M.L.1    Mounier, J.2    Hauteville, H.L.3    Coquis-Ronton, M.4    Sansonetti, P.J.5
  • 42
    • 0028837734 scopus 로고
    • Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility
    • 8596443 10.1111/j.1365-2958.1995.mmi-17050945.x 1:CAS:528:DyaK2MXovVGrtrw%3D
    • Smith, G. A., Portnoy, D. A., and Theriot, J. A. (1995) Asymmetric distribution of the Listeria monocytogenes ActA protein is required and sufficient to direct actin-based motility, Mol. Microbiol., 17, 945-951.
    • (1995) Mol. Microbiol. , vol.17 , pp. 945-951
    • Smith, G.A.1    Portnoy, D.A.2    Theriot, J.A.3
  • 43
    • 0027191844 scopus 로고
    • Unipolar localization and ATPase activity of Ics A, a Shigella flexneri protein involved in intracellular movement
    • 8468279 1:CAS:528:DyaK3sXisFWitbY%3D 204503
    • Goldberg, M. B., Barzu, O., Parsot, C., and Sansonetti, P. J. (1993) Unipolar localization and ATPase activity of Ics A, a Shigella flexneri protein involved in intracellular movement, J. Bacteriol., 175, 2189-2196.
    • (1993) J. Bacteriol. , vol.175 , pp. 2189-2196
    • Goldberg, M.B.1    Barzu, O.2    Parsot, C.3    Sansonetti, P.J.4
  • 44
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • 20237478 10.1038/nrm2867 1:CAS:528:DC%2BC3cXjsFSqu7g%3D 2929822
    • Campellone, K. G., and Welch, M. D. (2010) A nucleator arms race: cellular control of actin assembly, Nat. Rev. Mol. Cell Biol., 11, 237-251.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 45
    • 0032525132 scopus 로고    scopus 로고
    • Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri
    • 9582270 10.1093/emboj/17.10.2767 1:CAS:528:DyaK1cXjslyks74%3D 1170617
    • Suzuki, T., Miki, H., Takenawa, T., and Sasakawa, C. (1998) Neural Wiskott-Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri, EMBO J., 17, 2767-2776.
    • (1998) EMBO J. , vol.17 , pp. 2767-2776
    • Suzuki, T.1    Miki, H.2    Takenawa, T.3    Sasakawa, C.4
  • 46
    • 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
    • 10491394 10.1083/jcb.146.6.1319 1:CAS:528:DyaK1MXmt1Gns7w%3D 2156126
    • Egile, C., Loisel, T. P., Laurent, V., Pantaloni, D., Sansonetti, P. J., and Carlier, M.-F. (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, 1319-1322.
    • (1999) J. Cell Biol. , vol.146 , pp. 1319-1322
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Pantaloni, D.4    Sansonetti, P.J.5    Carlier, M.-F.6
  • 47
    • 0029775654 scopus 로고    scopus 로고
    • Cell motility driven by actin polymerization
    • 8968574 10.1016/S0006-3495(96)79496-1 1:CAS:528:DyaK28XnsFKltLs%3D 1233792
    • Mogilner, A., and Oster, G. (1996) Cell motility driven by actin polymerization, Biophys. J., 71, 3030-3045.
    • (1996) Biophys. J. , vol.71 , pp. 3030-3045
    • Mogilner, A.1    Oster, G.2
  • 48
    • 0033533789 scopus 로고    scopus 로고
    • Reconstitution of actin-based motility of Listeria and Shigella using pure proteins
    • 10524632 10.1038/44183 1:STN:280:DyaK1Mvlt1alsQ%3D%3D
    • Loisel, T. P., Boujemaa, R., Pantaloni, D., and Carlier, M. F. (1999) Reconstitution of actin-based motility of Listeria and Shigella using pure proteins, Nature, 401, 613-616.
    • (1999) Nature , vol.401 , pp. 613-616
    • Loisel, T.P.1    Boujemaa, R.2    Pantaloni, D.3    Carlier, M.F.4
  • 49
    • 0033533677 scopus 로고    scopus 로고
    • Bare bones of the cytoskeleton
    • 10524617 10.1038/44044 1:CAS:528:DyaK1MXmvFCnt7Y%3D
    • Machesky, L. M., and Cooper, J. A. (1999) Bare bones of the cytoskeleton, Nature, 401, 542-543.
    • (1999) Nature , vol.401 , pp. 542-543
    • Machesky, L.M.1    Cooper, J.A.2
  • 51
    • 82155202494 scopus 로고    scopus 로고
    • Structure and functions of profilins
    • 1:CAS:528:DC%2BD1MXhtV2jtbzE
    • Krishnan, K., and Moens, P. D. J. (2009) Structure and functions of profilins, Biophys. Rev., 1, 71-81.
    • (2009) Biophys. Rev. , vol.1 , pp. 71-81
    • Krishnan, K.1    Moens, P.D.J.2
  • 52
    • 0033951186 scopus 로고    scopus 로고
    • Actin machinery: Pushing the envelope
    • Borisi, G. G., and Svitkina, T. M. (2000) Actin machinery: pushing the envelope, Curr. Opin. Cell Biol., 12, 104-112.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 104-112
    • Borisi, G.G.1    Svitkina, T.M.2
  • 53
    • 84882823562 scopus 로고    scopus 로고
    • Ultrastructure of protrusive actin filament arrays
    • 23639311 10.1016/j.ceb.2013.04.003 1:CAS:528:DC%2BC3sXmvVWisrs%3D
    • Svitkina, T. (2013) Ultrastructure of protrusive actin filament arrays, Curr. Opin. Cell Biol., 25, 574-581.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 574-581
    • Svitkina, T.1
  • 54
    • 0035145716 scopus 로고    scopus 로고
    • Actin filament nucleation by endosomes, lysosomes and secretory vesicles
    • 11163138 10.1016/S0955-0674(00)00178-2 1:CAS:528:DC%2BD3MXht1Kgsbo%3D
    • Taunton, J. (2001) Actin filament nucleation by endosomes, lysosomes and secretory vesicles, Curr. Opin. Cell Biol., 13, 85-91.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 85-91
    • Taunton, J.1
  • 55
    • 0034496280 scopus 로고    scopus 로고
    • Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles
    • 11082035 1:CAS:528:DC%2BD3MXmsVKmsA%3D%3D
    • Kaksonen, M., Peng, H. B., and Rauvala, H. (2000) Association of cortactin with dynamic actin in lamellipodia and on endosomal vesicles, J. Cell Sci., 113, 4421-4426.
    • (2000) J. Cell Sci. , vol.113 , pp. 4421-4426
    • Kaksonen, M.1    Peng, H.B.2    Rauvala, H.3
  • 57
    • 0037215997 scopus 로고    scopus 로고
    • Actin-based endosome and phagosome rocketing in macrophages: Activation by the secretagogue antagonists lanthanum and zinc
    • 12451594 10.1002/cm.10083 1:CAS:528:DC%2BD3sXhtVSgtbc%3D
    • Southwick, F. S., Li, W., Zhang, F., Zeile, W. L., and Purich, D. L. (2003) Actin-based endosome and phagosome rocketing in macrophages: activation by the secretagogue antagonists lanthanum and zinc, Cell Motil. Cytoskeleton, 54, 41-55.
    • (2003) Cell Motil. Cytoskeleton , vol.54 , pp. 41-55
    • Southwick, F.S.1    Li, W.2    Zhang, F.3    Zeile, W.L.4    Purich, D.L.5
  • 58
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • 11964480 10.1126/science.1069784 1:CAS:528:DC%2BD38XjtFCjs7k%3D
    • Pelkmans, L., Puntener, D., and Helenius, A. (2002) Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae, Science, 296, 535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Puntener, D.2    Helenius, A.3
  • 59
    • 0034329741 scopus 로고    scopus 로고
    • Actin assembly at membranes controlled by ARF6
    • 11273133 10.1034/j.1600-0854.2000.011108.x 1:CAS:528:DC%2BD3cXoslWrt78%3D
    • Schafer, D. A., D'Souza-Schorey, C., and Cooper, J. A. (2000) Actin assembly at membranes controlled by ARF6, Traffic, 1, 892-903.
    • (2000) Traffic , vol.1 , pp. 892-903
    • Schafer, D.A.1    D'Souza-Schorey, C.2    Cooper, J.A.3
  • 61
    • 0041813064 scopus 로고    scopus 로고
    • Rickettsia-like mitochondrial motility in Drosophila spermiogenesis
    • 12823454 10.1046/j.1525-142X.2003.03045.x
    • Bazinet, C., and Rollins, J. E. (2003) Rickettsia-like mitochondrial motility in Drosophila spermiogenesis, Evol. Dev., 5, 379-385.
    • (2003) Evol. Dev. , vol.5 , pp. 379-385
    • Bazinet, C.1    Rollins, J.E.2
  • 62
    • 3042794632 scopus 로고    scopus 로고
    • Seeing is believing: Imaging actin dynamics at single sites of endocytosis
    • 15246428 10.1016/j.tcb.2004.05.008 1:CAS:528:DC%2BD2cXls1Wkurk%3D
    • Merrifield, C. J. (2004) Seeing is believing: imaging actin dynamics at single sites of endocytosis, Trends Cell Biol., 14, 352-358.
    • (2004) Trends Cell Biol. , vol.14 , pp. 352-358
    • Merrifield, C.J.1
  • 63
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells
    • 15907472 10.1016/j.cell.2005.03.015 1:CAS:528:DC%2BD2MXkslelsLo%3D
    • Merrifield, C. J., Perrais, D., and Zenisek, D. (2005) Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells, Cell, 121, 593-606.
    • (2005) Cell , vol.121 , pp. 593-606
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 64
    • 79960743030 scopus 로고    scopus 로고
    • Structural organization of the actin cytoskeleton at sites of clathrin-mediated endocytosis
    • 21723126 10.1016/j.cub.2011.05.048 1:CAS:528:DC%2BC3MXptlektL8%3D 3143238
    • Collins, A., Warrington, A., Taylor, K. A., and Svitkina, T. (2011) Structural organization of the actin cytoskeleton at sites of clathrin-mediated endocytosis, Curr. Biol., 21, 1167-1175.
    • (2011) Curr. Biol. , vol.21 , pp. 1167-1175
    • Collins, A.1    Warrington, A.2    Taylor, K.A.3    Svitkina, T.4
  • 65
    • 80052248915 scopus 로고    scopus 로고
    • Dynamin: Functional design of a membrane fission catalyst
    • 21599493 10.1146/annurev-cellbio-100109-104016 1:CAS:528:DC%2BC3MXhsFyqtbnE
    • Schmid, S. L., and Frolov, V. A. (2011) Dynamin: functional design of a membrane fission catalyst, Annu. Rev. Cell. Dev. Biol., 27, 79-105.
    • (2011) Annu. Rev. Cell. Dev. Biol. , vol.27 , pp. 79-105
    • Schmid, S.L.1    Frolov, V.A.2
  • 66
    • 84856111189 scopus 로고    scopus 로고
    • Dynamin, a membrane-remodeling GTPase
    • 22233676 1:CAS:528:DC%2BC38XlsF2gsw%3D%3D 3519936
    • Ferguson, S. M., and De Camilli, P. (2012) Dynamin, a membrane-remodeling GTPase, Nat. Rev. Mol. Cell Biol., 13, 75-88.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 75-88
    • Ferguson, S.M.1    De Camilli, P.2
  • 67
    • 84872651484 scopus 로고    scopus 로고
    • Dynamin: Expanding its scope to the cytoskeleton
    • 23351711 10.1016/B978-0-12-407699-0.00003-0 1:CAS:528:DC%2BC3sXhtValtLbK
    • Menon, M., and Schafer, D. A. (2013) Dynamin: expanding its scope to the cytoskeleton, Int. Rev. Cell. Mol. Biol., 302, 187-219.
    • (2013) Int. Rev. Cell. Mol. Biol. , vol.302 , pp. 187-219
    • Menon, M.1    Schafer, D.A.2
  • 68
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • 12621426 10.1038/nature01451 1:CAS:528:DC%2BD3sXhs1yit7Y%3D
    • Conner, S. D., and Schmid, S. L. (2003) Regulated portals of entry into the cell, Nature, 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 69
    • 12844265252 scopus 로고    scopus 로고
    • Dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis
    • 15601897 10.1091/mbc.E04-09-0774 1:CAS:528:DC%2BD2MXhtVGiu78%3D 545926
    • Yarar, D., Waterman-Storer, C. M., and Schmid, S. L. A. (2005) Dynamic actin cytoskeleton functions at multiple stages of clathrin-mediated endocytosis, Mol. Biol. Cell, 16, 964-975.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 964-975
    • Yarar, D.1    Waterman-Storer, C.M.2    Schmid, S.L.A.3
  • 70
    • 0037039431 scopus 로고    scopus 로고
    • Dynamin at actin tails
    • 11782545 10.1073/pnas.012607799 1:CAS:528:DC%2BD38Xlt1CgsQ%3D%3D 117532
    • Lee, E., and De Camilli, P. (2002) Dynamin at actin tails, Proc. Natl. Acad. Sci. USA, 99, 161-166.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 161-166
    • Lee, E.1    De Camilli, P.2
  • 71
    • 4344674527 scopus 로고    scopus 로고
    • Cortactin signaling and dynamic actin networks
    • 15186216 10.1042/BJ20040737 1:CAS:528:DC%2BD2cXmsVChsLs%3D 1133910
    • Daly, R. J. (2004) Cortactin signaling and dynamic actin networks, Biochem. J., 382, 13-25.
    • (2004) Biochem. J. , vol.382 , pp. 13-25
    • Daly, R.J.1
  • 73
    • 78149266925 scopus 로고    scopus 로고
    • Direct dynamin-actin interactions regulate the actin cytoskeleton
    • 20935625 10.1038/emboj.2010.249 1:CAS:528:DC%2BC3cXht1GqurvI 2982766
    • Gu, C., Yaddanapudi, S., Weins, A., Osborn, T., Reiser, J., Pollak, M., Hartwig, J., and Sever, S. (2010) Direct dynamin-actin interactions regulate the actin cytoskeleton, EMBO J., 29, 3593-3606.
    • (2010) EMBO J. , vol.29 , pp. 3593-3606
    • Gu, C.1    Yaddanapudi, S.2    Weins, A.3    Osborn, T.4    Reiser, J.5    Pollak, M.6    Hartwig, J.7    Sever, S.8
  • 74
    • 84859986511 scopus 로고    scopus 로고
    • A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis
    • 22505844 10.1371/journal.pbio.1001302 1:CAS:528:DC%2BC38XlvF2gsLY%3D 3323523
    • Taylor, M. J., Lampe, M., and Merrifield, C. J. (2012) A feedback loop between dynamin and actin recruitment during clathrin-mediated endocytosis, PLoS Biol., 10, e1001302.
    • (2012) PLoS Biol. , vol.10 , pp. 1001302
    • Taylor, M.J.1    Lampe, M.2    Merrifield, C.J.3
  • 75
    • 0023875598 scopus 로고
    • Polymerization of G-actin by myosin subfragment 1
    • 2962999 1:CAS:528:DyaL1cXht1OjtrY%3D
    • Miller, L., Phillips, M., and Reisler, E. (1988) Polymerization of G-actin by myosin subfragment 1, J. Biol. Chem., 263, 1996-2002.
    • (1988) J. Biol. Chem. , vol.263 , pp. 1996-2002
    • Miller, L.1    Phillips, M.2    Reisler, E.3
  • 76
    • 22144478226 scopus 로고    scopus 로고
    • Role of DNase-I-binding loop in myosin subfragment 1-induced actin polymerization. Implications to the polymerization mechanism
    • 15665122 10.1529/biophysj.104.049155 1:CAS:528:DC%2BD2MXjtFCjtL4%3D 1305383
    • Wawro, B., Khaitlina, S. Yu., Galinska-Rakoczy, A., and Strzelecka-Golaszewska, H. (2005) Role of DNase-I-binding loop in myosin subfragment 1-induced actin polymerization. Implications to the polymerization mechanism, Biophys. J., 88, 2883-2896.
    • (2005) Biophys. J. , vol.88 , pp. 2883-2896
    • Wawro, B.1    Khaitlina, S.Y.2    Galinska-Rakoczy, A.3    Strzelecka-Golaszewska, H.4
  • 77
    • 84864743481 scopus 로고    scopus 로고
    • Myosin 1E coordinated actin assembly and cargo trafficking during clathrin-mediated endocytosis
    • 22675027 10.1091/mbc.E11-04-0383 1:CAS:528:DC%2BC38XhtF2hsrjP 3408416
    • Cheng, J., Grassart, A., and Drubin, D. G. (2012) Myosin 1E coordinated actin assembly and cargo trafficking during clathrin-mediated endocytosis, Mol. Biol. Cell, 23, 2891-2904.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2891-2904
    • Cheng, J.1    Grassart, A.2    Drubin, D.G.3
  • 78
    • 33644873004 scopus 로고    scopus 로고
    • Actin dynamics at the Golgi complex in mammalian cells
    • 16488588 10.1016/j.ceb.2006.02.007 1:CAS:528:DC%2BD28Xit1Chsbs%3D
    • Egea, G., Lazaro-Dieguez, F., and Vilella, M. (2006) Actin dynamics at the Golgi complex in mammalian cells, Curr. Opin. Cell Biol., 18, 168-178.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 168-178
    • Egea, G.1    Lazaro-Dieguez, F.2    Vilella, M.3
  • 79
    • 84861868826 scopus 로고    scopus 로고
    • Roles for actin assembly in endocytosis
    • 22663081 10.1146/annurev-biochem-060910-094416 1:CAS:528:DC%2BC38XhtVGlsL7O
    • Mooren, O. L., Galletta, B. J., and Cooper, J. A. (2012) Roles for actin assembly in endocytosis, Annu. Rev. Biochem., 81, 661-686.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 661-686
    • Mooren, O.L.1    Galletta, B.J.2    Cooper, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.