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Volumn 47, Issue 2, 1999, Pages 93-106

Vesicle transport: The role of actin filaments and myosin motors

Author keywords

Actin filaments; Myosin; Organelle vesicle movement; Vesicle transport

Indexed keywords

CELL MEMBRANES; CYTOLOGY; MITOCHONDRIA; PROTEINS;

EID: 0033569627     PISSN: 1059910X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0029(19991015)47:2<93::AID-JEMT2>3.0.CO;2-P     Document Type: Article
Times cited : (135)

References (132)
  • 1
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento F, Emans N, Griffiths G, Gruenberg J. 1993. Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J Cell Biol 123:1373-1387.
    • (1993) J Cell Biol , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 2
    • 0025341466 scopus 로고
    • Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors
    • Arikawa K, Hicks JL, Williams DS. 1990. Identification of actin filaments in the rhabdomeral microvilli of Drosophila photoreceptors. J Cell Biol 110:1993-1998.
    • (1990) J Cell Biol , vol.110 , pp. 1993-1998
    • Arikawa, K.1    Hicks, J.L.2    Williams, D.S.3
  • 3
    • 0342419162 scopus 로고
    • Polarity orientation of microtubules in hippocampal neurons: Uniformity in the axon and nonuniformity in the dendrite
    • Baas PW, Deitch JS, Black MM, Banker GA. 1988. Polarity orientation of microtubules in hippocampal neurons: uniformity in the axon and nonuniformity in the dendrite. Proc Natl Acad Sci USA 85:8335-8339.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 8335-8339
    • Baas, P.W.1    Deitch, J.S.2    Black, M.M.3    Banker, G.A.4
  • 4
    • 0026457072 scopus 로고
    • Differential localization of acanthamoeba myosin I isoforms
    • Baines IC, Brzeska H, Korn ED. 1992. Differential localization of Acanthamoeba myosin I isoforms. J Cell Biol 119:1193-1203.
    • (1992) J Cell Biol , vol.119 , pp. 1193-1203
    • Baines, I.C.1    Brzeska, H.2    Korn, E.D.3
  • 5
    • 0026550465 scopus 로고
    • Structural interactions of actin filaments and endoplasmic reticulum in honeybee photoreceptor cells
    • Baumann O. 1992. Structural interactions of actin filaments and endoplasmic reticulum in honeybee photoreceptor cells. Cell Tissue Res 268:71-79.
    • (1992) Cell Tissue Res , vol.268 , pp. 71-79
    • Baumann, O.1
  • 6
    • 0031940485 scopus 로고    scopus 로고
    • The Golgi apparatus in honeybee photoreceptor cells: Structural organization and spatial relationship to microtubules and actin filaments
    • Baumann O. 1998. The Golgi apparatus in honeybee photoreceptor cells: structural organization and spatial relationship to microtubules and actin filaments. Cell Tissue Res 291:351-361.
    • (1998) Cell Tissue Res , vol.291 , pp. 351-361
    • Baumann, O.1
  • 7
    • 0027984649 scopus 로고
    • The role of actin filaments in the organization of the endoplasmic reticulum in honeybee photoreceptor cells
    • Baumann O, Lautenschlager B. 1994. The role of actin filaments in the organization of the endoplasmic reticulum in honeybee photoreceptor cells. Cell Tissue Res 278:419-432.
    • (1994) Cell Tissue Res , vol.278 , pp. 419-432
    • Baumann, O.1    Lautenschlager, B.2
  • 8
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex
    • Beck KA, Buchanan JA, Malhotra V, Nelson WJ. 1994. Golgi spectrin: identification of an erythroid beta-spectrin homolog associated with the Golgi complex. J Cell Biol 127:707-723.
    • (1994) J Cell Biol , vol.127 , pp. 707-723
    • Beck, K.A.1    Buchanan, J.A.2    Malhotra, V.3    Nelson, W.J.4
  • 9
    • 0025084457 scopus 로고
    • Radiolabel-transfer cross-linking demonstrates that protein 4.1 binds to the N-terminal region of beta spectrin and to actin in binary interactions
    • Becker PS, Schwartz MA, Morrow JS, Lux SE. 1990. Radiolabel-transfer cross-linking demonstrates that protein 4.1 binds to the N-terminal region of beta spectrin and to actin in binary interactions. Eur JBiochem 193:827-836.
    • (1990) Eur Jbiochem , vol.193 , pp. 827-836
    • Becker, P.S.1    Schwartz, M.A.2    Morrow, J.S.3    Lux, S.E.4
  • 10
    • 0018252047 scopus 로고
    • The visualization of actin filament polarity in thin sections. Evidence for the uniform polarity of membrane-associated filaments
    • Begg DA, Rodewald R, Rebhun LI. 1978. The visualization of actin filament polarity in thin sections. Evidence for the uniform polarity of membrane-associated filaments. J Cell Biol 79:846-852.
    • (1978) J Cell Biol , vol.79 , pp. 846-852
    • Begg, D.A.1    Rodewald, R.2    Rebhun, L.I.3
  • 11
    • 0031059722 scopus 로고    scopus 로고
    • Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast
    • Berger KH, Sogo LF, Yaffe MP. 1997. Mdm12p, a component required for mitochondrial inheritance that is conserved between budding and fission yeast. J Cell Biol 136:545-553.
    • (1997) J Cell Biol , vol.136 , pp. 545-553
    • Berger, K.H.1    Sogo, L.F.2    Yaffe, M.P.3
  • 14
    • 0030695228 scopus 로고    scopus 로고
    • Drosophila unconventional myosin VI is involved in intra-and intercellular transport during oogenesis
    • Bohrmann J. 1997. Drosophila unconventional myosin VI is involved in intra-and intercellular transport during oogenesis. Cell Mol Life Sci 53:652-662.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 652-662
    • Bohrmann, J.1
  • 15
    • 0023890858 scopus 로고
    • The melanocyte. Its structure, function, and subpopulations in skin, eyes, and hair
    • Boissy RE. 1988. The melanocyte. Its structure, function, and subpopulations in skin, eyes, and hair. Dermatol Clin 6:161-173.
    • (1988) Dermatol Clin , vol.6 , pp. 161-173
    • Boissy, R.E.1
  • 16
    • 0032526412 scopus 로고    scopus 로고
    • Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p
    • Boldogh I, Vojtov N, Karmon S, Pon LA. 1998. Interaction between mitochondria and the actin cytoskeleton in budding yeast requires two integral mitochondrial outer membrane proteins, Mmm1p and Mdm10p. J Cell Biol 141:1371-1381.
    • (1998) J Cell Biol , vol.141 , pp. 1371-1381
    • Boldogh, I.1    Vojtov, N.2    Karmon, S.3    Pon, L.A.4
  • 18
    • 0025029828 scopus 로고
    • Microtubule-and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells
    • Bomsel M, Parton R, Kuznetsov SA, Schroer TA, Gruenberg J. 1990. Microtubule-and motor-dependent fusion in vitro between apical and basolateral endocytic vesicles from MDCK cells. Cell 62:719-731.
    • (1990) Cell , vol.62 , pp. 719-731
    • Bomsel, M.1    Parton, R.2    Kuznetsov, S.A.3    Schroer, T.A.4    Gruenberg, J.5
  • 19
    • 0019381919 scopus 로고
    • Serial analysis of microtubules in cultured rat sensory axons
    • Bray D, Bunge MB. 1981. Serial analysis of microtubules in cultured rat sensory axons. J Neurocytol 10:589-605.
    • (1981) J Neurocytol , vol.10 , pp. 589-605
    • Bray, D.1    Bunge, M.B.2
  • 20
    • 0028129071 scopus 로고
    • MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria
    • Burgess SM, Delannoy M, Jensen RE. 1994. MMM1 encodes a mitochondrial outer membrane protein essential for establishing and maintaining the structure of yeast mitochondria. J Cell Biol 126:1375-1391.
    • (1994) J Cell Biol , vol.126 , pp. 1375-1391
    • Burgess, S.M.1    Delannoy, M.2    Jensen, R.E.3
  • 21
    • 0032517817 scopus 로고    scopus 로고
    • The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation
    • Buss F, Kendrick-Jones J, Lionne C, Knight AE, Cote GP, Luzio JP. 1998. The localization of myosin VI at the Golgi complex and leading edge of fibroblasts and its phosphorylation and recruitment into membrane ruffles of A431 cells after growth factor stimulation. J Cell Biol 143:1535-1545.
    • (1998) J Cell Biol , vol.143 , pp. 1535-1545
    • Buss, F.1    Kendrick-Jones, J.2    Lionne, C.3    Knight, A.E.4    Cote, G.P.5    Luzio, J.P.6
  • 22
    • 0018385401 scopus 로고
    • Organization of neuronal microtubules in the nematode Caenorhabditis elegans
    • Chalfie M, Thomson JN. 1979. Organization of neuronal microtubules in the nematode Caenorhabditis elegans. J Cell Biol 82:278-289.
    • (1979) J Cell Biol , vol.82 , pp. 278-289
    • Chalfie, M.1    Thomson, J.N.2
  • 24
    • 0021151351 scopus 로고
    • Functional characterization of human erythrocyte spectrin alpha and beta chains: Association with actin and erythrocyte protein 4.1
    • Cohen CM, Langley RC Jr. 1984. Functional characterization of human erythrocyte spectrin alpha and beta chains: association with actin and erythrocyte protein 4.1. Biochemistry 23:4488-4495.
    • (1984) Biochemistry , vol.23 , pp. 4488-4495
    • Cohen, C.M.1    Langley R.C., Jr.2
  • 25
    • 0029126573 scopus 로고
    • Recombinant expression of the brush border myosin I heavy chain
    • Collins K, Matsudaira PT. 1995. Recombinant expression of the brush border myosin I heavy chain. Cell Motil Cytoskeleton 32:151-161.
    • (1995) Cell Motil Cytoskeleton , vol.32 , pp. 151-161
    • Collins, K.1    Matsudaira, P.T.2
  • 26
    • 0027523460 scopus 로고
    • Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts
    • Conrad PA, Giuliano KA, Fisher G, Collins K, Matsudaira PT, Taylor DL. 1993. Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts. J Cell Biol 120:1381-1391.
    • (1993) J Cell Biol , vol.120 , pp. 1381-1391
    • Conrad, P.A.1    Giuliano, K.A.2    Fisher, G.3    Collins, K.4    Matsudaira, P.T.5    Taylor, D.L.6
  • 27
    • 0028106091 scopus 로고
    • Identification of coelomocyte unconventional myosin and its association with in vivo particle/vesicle motility
    • D'Andrea L, Danon MA, Sgourdas GP, Bonder EM. 1994. Identification of coelomocyte unconventional myosin and its association with in vivo particle/vesicle motility. J Cell Sci 107:2081-2094.
    • (1994) J Cell Sci , vol.107 , pp. 2081-2094
    • D'Andrea, L.1    Danon, M.A.2    Sgourdas, G.P.3    Bonder, E.M.4
  • 29
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin DG, Jones HD, Wertman KF. 1993. Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol Biol Cell 4:1277-1294.
    • (1993) Mol Biol Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 30
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach A, Louvard D, Coudrier E. 1996a. Actin filaments facilitate two steps of endocytosis. J Cell Sci 109:457-465.
    • (1996) J Cell Sci , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 31
    • 0029957036 scopus 로고    scopus 로고
    • Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in a hepatoma cell line
    • Durrbach A, Collins K, Matsudaira P, Louvard D, Coudrier E. 1996b. Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in a hepatoma cell line. Proc Natl Acad Sci USA 93:7053-7058.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7053-7058
    • Durrbach, A.1    Collins, K.2    Matsudaira, P.3    Louvard, D.4    Coudrier, E.5
  • 32
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains
    • Espreafico EM, Cheney RE, Matteoli M, Nascimento AA, De Camilli PV, Larson RE, Mooseker MS. 1992. Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J Cell Biol 119:1541-1557.
    • (1992) J Cell Biol , vol.119 , pp. 1541-1557
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.4    De Camilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 33
    • 0031049775 scopus 로고    scopus 로고
    • Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons
    • Evans LL, Hammer J, Bridgman PC. 1997. Subcellular localization of myosin V in nerve growth cones and outgrowth from dilute-lethal neurons. J Cell Sci 110:439-449.
    • (1997) J Cell Sci , vol.110 , pp. 439-449
    • Evans, L.L.1    Hammer, J.2    Bridgman, P.C.3
  • 34
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein
    • Path KR, Burgess DR. 1993. Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein. J Cell Biol 120:117-127.
    • (1993) J Cell Biol , vol.120 , pp. 117-127
    • Path, K.R.1    Burgess, D.R.2
  • 35
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells
    • Path KR, Trimbur GM, Burgess DR. 1994. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J Cell Biol 126:661-675.
    • (1994) J Cell Biol , vol.126 , pp. 661-675
    • Path, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 36
    • 0030780090 scopus 로고    scopus 로고
    • Molecular motors and a spectrin matrix associate with Golgi membranes in vitro
    • Fath KR, Trimbur GM, Burgess DR. 1997. Molecular motors and a spectrin matrix associate with Golgi membranes in vitro. J Cell Biol 139:1169-1181.
    • (1997) J Cell Biol , vol.139 , pp. 1169-1181
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 37
    • 0028239967 scopus 로고
    • Brush border myosin-I microinjected into cultured cells is targeted to actin-containing surface structures
    • Footer M, Bretscher A. 1994. Brush border myosin-I microinjected into cultured cells is targeted to actin-containing surface structures. J Cell Sci 107:1623-1631.
    • (1994) J Cell Sci , vol.107 , pp. 1623-1631
    • Footer, M.1    Bretscher, A.2
  • 38
    • 0029923034 scopus 로고    scopus 로고
    • Role of type I myosins in receptor-mediated endocytosis in yeast
    • Geli MI, Riezman H. 1996. Role of type I myosins in receptor-mediated endocytosis in yeast. Science 272:533-535.
    • (1996) Science , vol.272 , pp. 533-535
    • Geli, M.I.1    Riezman, H.2
  • 39
    • 0029984773 scopus 로고    scopus 로고
    • Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): Myosin I proteins are required for polarization of the actin cytoskeleton
    • Goodson HV, Anderson BL, Warrick HM, Pon LA, Spudich JA. 1996. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. J Cell Biol 133:1277-1291.
    • (1996) J Cell Biol , vol.133 , pp. 1277-1291
    • Goodson, H.V.1    Anderson, B.L.2    Warrick, H.M.3    Pon, L.A.4    Spudich, J.A.5
  • 40
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport
    • Govindan B, Bowser R, Novick P. 1995. The role of Myo2, a yeast class V myosin, in vesicular transport. J Cell Biol 128:1055-1068.
    • (1995) J Cell Biol , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 41
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg J, Griffiths G, Howell KE. 1989. Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J Cell Biol 108:1301-1316.
    • (1989) J Cell Biol , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 42
    • 0025738251 scopus 로고
    • Changes in the microvillus cytoskeleton during rhabdom formation in the retina of the crayfish Procambarus clarkii
    • Hafner GS, Tokarski TR, Kipp J. 1991. Changes in the microvillus cytoskeleton during rhabdom formation in the retina of the crayfish Procambarus clarkii. J Neurocytol 20:585-596.
    • (1991) J Neurocytol , vol.20 , pp. 585-596
    • Hafner, G.S.1    Tokarski, T.R.2    Kipp, J.3
  • 43
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-614.
    • (1998) Science , vol.279 , pp. 509-614
    • Hall, A.1
  • 44
    • 0027993176 scopus 로고
    • Porcine myosin-VI: Characterization of a new mammalian unconventional myosin
    • Hasson T, Mooseker MS. 1994. Porcine myosin-VI: characterization of a new mammalian unconventional myosin. J Cell Biol 127:425-440.
    • (1994) J Cell Biol , vol.127 , pp. 425-440
    • Hasson, T.1    Mooseker, M.S.2
  • 45
    • 17344380140 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation
    • He H, Watanabe T, Zhan X, Huang C, Schuuring E, Fukami K, Takenawa T, Kumar CC, Simpson RJ, Maruta H. 1998. Role of phosphatidylinositol 4,5-bisphosphate in Ras/Rac-induced disruption of the cortactin-actomyosin II complex and malignant transformation. Mol Cell Biol 18:3829-3837.
    • (1998) Mol Cell Biol , vol.18 , pp. 3829-3837
    • He, H.1    Watanabe, T.2    Zhan, X.3    Huang, C.4    Schuuring, E.5    Fukami, K.6    Takenawa, T.7    Kumar, C.C.8    Simpson, R.J.9    Maruta, H.10
  • 46
    • 0002254410 scopus 로고
    • Determinants of skin color: Melanocytes and melanization
    • Levine N, editor. London: CRC Press
    • Hearing VJ, King RA. 1993. Determinants of skin color: melanocytes and melanization. In: Levine N, editor. Pigmentation and pigmentary disorders. London: CRC Press, p 4-18.
    • (1993) Pigmentation and Pigmentary Disorders , pp. 4-18
    • Hearing, V.J.1    King, R.A.2
  • 47
    • 0024523485 scopus 로고
    • Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
    • Heuser J. 1989. Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH. J Cell Biol 108:855-864.
    • (1989) J Cell Biol , vol.108 , pp. 855-864
    • Heuser, J.1
  • 48
    • 0019308174 scopus 로고
    • Filament organization revealed in platinum replicas of freeze-dried cytoskeletons
    • Heuser JE, Kirschner MW. 1980. Filament organization revealed in platinum replicas of freeze-dried cytoskeletons. J Cell Biol 86:212-234.
    • (1980) J Cell Biol , vol.86 , pp. 212-234
    • Heuser, J.E.1    Kirschner, M.W.2
  • 49
    • 0030470182 scopus 로고    scopus 로고
    • Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae
    • Hill KL, Catlett NL, Weisman LS. 1996. Actin and myosin function in directed vacuole movement during cell division in Saccharomyces cerevisiae. J Cell Biol 135:1535-1549.
    • (1996) J Cell Biol , vol.135 , pp. 1535-1549
    • Hill, K.L.1    Catlett, N.L.2    Weisman, L.S.3
  • 50
    • 0025045429 scopus 로고
    • Radial extension of macrophage tubular lysosomes supported by kinesin
    • Hollenbeck PJ, Swanson JA. 1990. Radial extension of macrophage tubular lysosomes supported by kinesin. Nature 346:864-866.
    • (1990) Nature , vol.346 , pp. 864-866
    • Hollenbeck, P.J.1    Swanson, J.A.2
  • 51
    • 0030479303 scopus 로고    scopus 로고
    • Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
    • Holleran EA, Tokito MK, Karki S, Holzbaur EL. 1996. Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. J Cell Biol 135:1815-1829.
    • (1996) J Cell Biol , vol.135 , pp. 1815-1829
    • Holleran, E.A.1    Tokito, M.K.2    Karki, S.3    Holzbaur, E.L.4
  • 52
    • 0028339264 scopus 로고
    • In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella
    • Hopkins CR, Gibson A, Shipman M, Strickland DK, Trowbridge IS. 1994. In migrating fibroblasts, recycling receptors are concentrated in narrow tubules in the pericentriolar area, and then routed to the plasma membrane of the leading lamella. J Cell Biol 125:1265-1274.
    • (1994) J Cell Biol , vol.125 , pp. 1265-1274
    • Hopkins, C.R.1    Gibson, A.2    Shipman, M.3    Strickland, D.K.4    Trowbridge, I.S.5
  • 54
    • 0029894049 scopus 로고    scopus 로고
    • Analysis of the role of p200-containing vesicles in post-Golgi traffic
    • Ikonen E, Parton RG, Lafont F, Simons K. 1996. Analysis of the role of p200-containing vesicles in post-Golgi traffic. Mol Biol Cell 7:961-974.
    • (1996) Mol Biol Cell , vol.7 , pp. 961-974
    • Ikonen, E.1    Parton, R.G.2    Lafont, F.3    Simons, K.4
  • 55
    • 0030820352 scopus 로고    scopus 로고
    • Myosin II is associated with Golgi membranes: Identification of p200 as nonmuscle myosin II on Golgi-derived vesicles
    • Ikonen E, de Almeid JB, Fath KF, Burgess DR, Ashman K, Simons K, Stow JL. 1997. Myosin II is associated with Golgi membranes: identification of p200 as nonmuscle myosin II on Golgi-derived vesicles. J Cell Sci 110:2155-2164.
    • (1997) J Cell Sci , vol.110 , pp. 2155-2164
    • Ikonen, E.1    De Almeid, J.B.2    Fath, K.F.3    Burgess, D.R.4    Ashman, K.5    Simons, K.6    Stow, J.L.7
  • 56
    • 0017885642 scopus 로고
    • Filamentous actin, 100 a filaments and microtubules in neuroblastoma cells. Their distribution in relation to sites of movement and neuronal transport
    • Isenberg G, Small JV. 1978. Filamentous actin, 100 A filaments and microtubules in neuroblastoma cells. Their distribution in relation to sites of movement and neuronal transport, Cytobiologie 16:326-344.
    • (1978) Cytobiologie , vol.16 , pp. 326-344
    • Isenberg, G.1    Small, J.V.2
  • 57
    • 0028085551 scopus 로고
    • Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D
    • Jackman MR, Shurety W, Ellis JA, Luzio JP. 1994. Inhibition of apical but not basolateral endocytosis of ricin and folate in Caco-2 cells by cytochalasin D. J Cell Sci 107:2547-2556.
    • (1994) J Cell Sci , vol.107 , pp. 2547-2556
    • Jackman, M.R.1    Shurety, W.2    Ellis, J.A.3    Luzio, J.P.4
  • 59
    • 0025801365 scopus 로고
    • The saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles
    • Johnston GC, Prendergast JA, Singer RA. 1991. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J Cell Biol 113:539-551.
    • (1991) J Cell Biol , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 60
    • 0029925627 scopus 로고    scopus 로고
    • Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions
    • Jung G, Wu X, Hammer JA III. 1996. Dictyostelium mutants lacking multiple classic myosin I isoforms reveal combinations of shared and distinct functions. J Cell Biol 133:305-323.
    • (1996) J Cell Biol , vol.133 , pp. 305-323
    • Jung, G.1    Wu, X.2    Hammer J.A. III3
  • 61
    • 0029374716 scopus 로고
    • Origin of PDZ (DHR, GLGF) domains
    • Kennedy MB. 1995. Origin of PDZ (DHR, GLGF) domains. Trends Biochem Sci 20:350.
    • (1995) Trends Biochem Sci , vol.20 , pp. 350
    • Kennedy, M.B.1
  • 62
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov SA, Langford G, Weiss DG. 1992. Actin-dependent organelle movement in squid axoplasm. Nature 356:722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.2    Weiss, D.G.3
  • 64
    • 0032212657 scopus 로고    scopus 로고
    • Myosin V in the brain: Mutations lead to neurological defects
    • Langford GM, Molyneaux BJ. 1998. Myosin V in the brain: mutations lead to neurological defects. Brain Res Rev 28:1-8.
    • (1998) Brain Res Rev , vol.28 , pp. 1-8
    • Langford, G.M.1    Molyneaux, B.J.2
  • 65
    • 0028048692 scopus 로고
    • Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity
    • Lazzarino DA, Boldogh I, Smith MG, Rosand J, Pon LA. 1994. Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Mol Biol Cell 5:807-818.
    • (1994) Mol Biol Cell , vol.5 , pp. 807-818
    • Lazzarino, D.A.1    Boldogh, I.2    Smith, M.G.3    Rosand, J.4    Pon, L.A.5
  • 66
    • 0026437563 scopus 로고
    • Nerve growth cone lamellipodia contain two populations of actin filaments that differ in organization and polarity
    • Lewis AK, Bridgman PC. 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
  • 67
    • 0029550559 scopus 로고
    • Actomyosin-based motility of endoplasmic reticulum and chloroplasts in Vallisneria mesophyll cells
    • Liebe S, Menzel D. 1995, Actomyosin-based motility of endoplasmic reticulum and chloroplasts in Vallisneria mesophyll cells. Biol Cell 85:207-222.
    • (1995) Biol Cell , vol.85 , pp. 207-222
    • Liebe, S.1    Menzel, D.2
  • 68
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization
    • Machesky LM, Hall A. 1997. Role of actin polymerization and adhesion to extracellular matrix in Rac-and Rho-induced cytoskeletal reorganization. J Cell Biol 138:913-926.
    • (1997) J Cell Biol , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 69
    • 0028917977 scopus 로고
    • Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein
    • Marfatia SM, Leu RA, Branton D, Chishti AH. 1995. Identification of the protein 4.1 binding interface on glycophorin C and p55, a homologue of the Drosophila discs-large tumor suppressor protein. J Biol Chem 270:715-719.
    • (1995) J Biol Chem , vol.270 , pp. 715-719
    • Marfatia, S.M.1    Leu, R.A.2    Branton, D.3    Chishti, A.H.4
  • 70
    • 0023576902 scopus 로고
    • Translocation and clustering of endosomes and lysosomes depends on microtubules
    • Matteoni R, Kreis TE. 1987. Translocation and clustering of endosomes and lysosomes depends on microtubules. J Cell Biol 105:1253-1265.
    • (1987) J Cell Biol , vol.105 , pp. 1253-1265
    • Matteoni, R.1    Kreis, T.E.2
  • 72
    • 0028359778 scopus 로고
    • Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos
    • Mermall V, McNally JG, Miller KG. 1994. Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos. Nature 369:560-562.
    • (1994) Nature , vol.369 , pp. 560-562
    • Mermall, V.1    McNally, J.G.2    Miller, K.G.3
  • 73
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V, Post PL, Mooseker MS. 1998. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science 279:527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 74
    • 0028987993 scopus 로고
    • Canoe encodes a novel protein containing a GLGF/DHR motif and functions with Notch and scabrous in common developmental pathways in Drosophila
    • Miyamoto H, Nihonmatsu I, Kondo S, Ueda R, Togashi S, Hirata K, Ikegami Y, Yamamoto D. 1995. Canoe encodes a novel protein containing a GLGF/DHR motif and functions with Notch and scabrous in common developmental pathways in Drosophila. Genes Dev 9:612-625.
    • (1995) Genes Dev , vol.9 , pp. 612-625
    • Miyamoto, H.1    Nihonmatsu, I.2    Kondo, S.3    Ueda, R.4    Togashi, S.5    Hirata, K.6    Ikegami, Y.7    Yamamoto, D.8
  • 75
    • 0031056345 scopus 로고    scopus 로고
    • Centrosomal deployment of gamma-tubulin and pericentrin: Evidence for a microtubule-nucleating domain and a minus-end docking domain in certain mouse epithelial cells
    • Mogensen MM, Mackie JB, Doxsey SJ, Stearns T, Tucker JB. 1997. Centrosomal deployment of gamma-tubulin and pericentrin: evidence for a microtubule-nucleating domain and a minus-end docking domain in certain mouse epithelial cells, Cell Motil Cytoskeleton 36:276-290.
    • (1997) Cell Motil Cytoskeleton , vol.36 , pp. 276-290
    • Mogensen, M.M.1    Mackie, J.B.2    Doxsey, S.J.3    Stearns, T.4    Tucker, J.B.5
  • 76
    • 0030823761 scopus 로고    scopus 로고
    • Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers
    • Montes de Oca G, Lezama RA, Mondragon R, Castillo AM, Meza I. 1997. Myosin I interactions with actin filaments and trans-Golgi-derived vesicles in MDCK cell monolayers. Arch Med Res 28:321-328.
    • (1997) Arch Med Res , vol.28 , pp. 321-328
    • Montes De Oca, G.1    Lezama, R.A.2    Mondragon, R.3    Castillo, A.M.4    Meza, I.5
  • 77
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris RL, Hollenbeck PJ. 1995. Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J Cell Biol 131:1315-1326.
    • (1995) J Cell Biol , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 78
    • 0028889137 scopus 로고
    • Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells
    • Muallem S, Kwiatkowska K, Xu X, Yin HL. 1995. Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. J Cell Biol 128:589-598.
    • (1995) J Cell Biol , vol.128 , pp. 589-598
    • Muallem, S.1    Kwiatkowska, K.2    Xu, X.3    Yin, H.L.4
  • 80
    • 0040971539 scopus 로고    scopus 로고
    • Myosin II is involved in the production of constitutive transport vesicles from the TGN
    • Müsch A, Cohen D, Rodriguez-Boulan E. 1997. Myosin II is involved in the production of constitutive transport vesicles from the TGN. J Cell Biol 138:291-306.
    • (1997) J Cell Biol , vol.138 , pp. 291-306
    • Müsch, A.1    Cohen, D.2    Rodriguez-Boulan, E.3
  • 81
    • 0032412643 scopus 로고    scopus 로고
    • Actin-filaments localize on the sorting endosomes of 3Y1 fibroblastic cells
    • Nakagawa H, Miyamoto S. 1998. Actin-filaments localize on the sorting endosomes of 3Y1 fibroblastic cells. Cell Struct Funct 23:283-290.
    • (1998) Cell Struct Funct , vol.23 , pp. 283-290
    • Nakagawa, H.1    Miyamoto, S.2
  • 82
    • 0030822624 scopus 로고    scopus 로고
    • Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene
    • Nascimento AA, Amaral RG, Bizario JC, Larson RE, Espreafico EM. 1997. Subcellular localization of myosin-V in the B16 melanoma cells, a wild-type cell line for the dilute gene. Mol Biol Cell 8:1971-1988.
    • (1997) Mol Biol Cell , vol.8 , pp. 1971-1988
    • Nascimento, A.A.1    Amaral, R.G.2    Bizario, J.C.3    Larson, R.E.4    Espreafico, E.M.5
  • 83
    • 0028838302 scopus 로고
    • Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis
    • Novak KD, Peterson MD, Reedy MC, Titus MA. 1995. Dictyostelium myosin I double mutants exhibit conditional defects in pinocytosis. J Cell Biol 131:1205-1221.
    • (1995) J Cell Biol , vol.131 , pp. 1205-1221
    • Novak, K.D.1    Peterson, M.D.2    Reedy, M.C.3    Titus, M.A.4
  • 84
    • 0021906692 scopus 로고
    • Phenotypic analysis of temperature-sensitive yeast actin mutants
    • Novick P, Botstein D. 1985. Phenotypic analysis of temperature-sensitive yeast actin mutants. Cell 40:405-416.
    • (1985) Cell , vol.40 , pp. 405-416
    • Novick, P.1    Botstein, D.2
  • 85
    • 0025829695 scopus 로고
    • pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells
    • Parton RG, Dotti CG, Bacallao R, Kurtz I, Simons K, Prydz K. 1991. pH-induced microtubule-dependent redistribution of late endosomes in neuronal and epithelial cells. J Cell Biol 113:261-274.
    • (1991) J Cell Biol , vol.113 , pp. 261-274
    • Parton, R.G.1    Dotti, C.G.2    Bacallao, R.3    Kurtz, I.4    Simons, K.5    Prydz, K.6
  • 86
    • 0024847344 scopus 로고
    • Erythrocyte protein 4.1 binds and regulates myosin
    • Pasternack GR, Racusen RH. 1989. Erythrocyte protein 4.1 binds and regulates myosin. Proc Natl Acad Sci USA 86:9712-9716.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9712-9716
    • Pasternack, G.R.1    Racusen, R.H.2
  • 88
    • 0030700638 scopus 로고    scopus 로고
    • Identification of cytoskeleton-associated proteins in isolated rat liver endosomes
    • Pol A, Ortega D, Enrich C. 1997. Identification of cytoskeleton-associated proteins in isolated rat liver endosomes. Biochem J 327:741-746.
    • (1997) Biochem J , vol.327 , pp. 741-746
    • Pol, A.1    Ortega, D.2    Enrich, C.3
  • 89
    • 0029035839 scopus 로고
    • AF-6/cno: Neither a kinesin nor a myosin, but a bit of both
    • Ponting CP. 1995. AF-6/cno: neither a kinesin nor a myosin, but a bit of both. Trends Biochem Sci 20:265-266.
    • (1995) Trends Biochem Sci , vol.20 , pp. 265-266
    • Ponting, C.P.1
  • 90
    • 0028902098 scopus 로고
    • DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins
    • Ponting CP, Phillips C. 1995. DHR domains in syntrophins, neuronal NO synthases and other intracellular proteins. Trends Biochem Sci 20:102-103.
    • (1995) Trends Biochem Sci , vol.20 , pp. 102-103
    • Ponting, C.P.1    Phillips, C.2
  • 91
    • 0031977198 scopus 로고    scopus 로고
    • Human myosin-IXb is a mechanochemically active motor and a GAP for rho
    • Post PL, Bokoch GM, Mooseker MS. 1998. Human myosin-IXb is a mechanochemically active motor and a GAP for rho. J Cell Sci 111:941-950.
    • (1998) J Cell Sci , vol.111 , pp. 941-950
    • Post, P.L.1    Bokoch, G.M.2    Mooseker, M.S.3
  • 93
    • 0030921711 scopus 로고    scopus 로고
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex
    • 2+-dependent interaction with the synaptobrevin-synaptophysin complex. J Cell Biol 137:1589-1601.
    • (1997) J Cell Biol , vol.137 , pp. 1589-1601
    • Prekeris, R.1    Terrian, D.M.2
  • 94
    • 0029955902 scopus 로고    scopus 로고
    • Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution
    • Provance DW Jr, Wei M, Ipe V, Mercer JA. 1996. Cultured melanocytes from dilute mutant mice exhibit dendritic morphology and altered melanosome distribution. Proc Natl Acad Sci USA 93:14554-14558.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14554-14558
    • Provance D.W., Jr.1    Wei, M.2    Ipe, V.3    Mercer, J.A.4
  • 97
    • 0032576766 scopus 로고    scopus 로고
    • Functional coordination of microtubule-based and actin-based motility in melanophores
    • Rodionov VI, Hope AJ, Svitkina TM, Borisy GG. 1998. Functional coordination of microtubule-based and actin-based motility in melanophores. Curr Biol 8:165-168.
    • (1998) Curr Biol , vol.8 , pp. 165-168
    • Rodionov, V.I.1    Hope, A.J.2    Svitkina, T.M.3    Borisy, G.G.4
  • 98
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • Rogers SL, Gelfand VI. 1998. Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr Biol 8:161-164.
    • (1998) Curr Biol , vol.8 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 99
    • 0031009586 scopus 로고    scopus 로고
    • Myosin functions in Xenopus retinal ganglion cell growth cone motility in vivo
    • Ruchhoeft ML, Harris WA. 1997. Myosin functions in Xenopus retinal ganglion cell growth cone motility in vivo. J Neurobiol 32:567-578.
    • (1997) J Neurobiol , vol.32 , pp. 567-578
    • Ruchhoeft, M.L.1    Harris, W.A.2
  • 100
    • 0024454465 scopus 로고
    • Fusion accessibility of endocytic compartments along the recycling and lysosomal endocytic pathways in intact cells
    • Salzman NH, Maxfield FR. 1989. Fusion accessibility of endocytic compartments along the recycling and lysosomal endocytic pathways in intact cells. J Cell Biol 109:2097-2104.
    • (1989) J Cell Biol , vol.109 , pp. 2097-2104
    • Salzman, N.H.1    Maxfield, F.R.2
  • 101
    • 0001812897 scopus 로고    scopus 로고
    • Golgi-membrane dynamics are cytoskeleton dependent
    • Satiat-Jeunemaitre B, Steel C, Hawes C. 1996. Golgi-membrane dynamics are cytoskeleton dependent. Protoplasma 191:21-23.
    • (1996) Protoplasma , vol.191 , pp. 21-23
    • Satiat-Jeunemaitre, B.1    Steel, C.2    Hawes, C.3
  • 102
    • 84966140454 scopus 로고
    • A lethal allele of dilute in the house mouse
    • Searle AG. 1952. A lethal allele of dilute in the house mouse. Heredity 6:395-401.
    • (1952) Heredity , vol.6 , pp. 395-401
    • Searle, A.G.1
  • 103
    • 0025343106 scopus 로고
    • Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein
    • Shariff A, Luna EJ. 1990. Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein. J Cell Biol 110:681-692.
    • (1990) J Cell Biol , vol.110 , pp. 681-692
    • Shariff, A.1    Luna, E.J.2
  • 104
    • 0030462308 scopus 로고    scopus 로고
    • Actin-based organelle movement
    • Simon VR, Pon LA. 1996. Actin-based organelle movement. Experientia 52:1117-1122.
    • (1996) Experientia , vol.52 , pp. 1117-1122
    • Simon, V.R.1    Pon, L.A.2
  • 105
    • 0029078227 scopus 로고
    • Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: Identification of a motor activity on the mitochondrial surface
    • Simon VR, Swavne TC, Pon LA. 1995. Actin-dependent mitochondrial motility in mitotic yeast and cell-free systems: identification of a motor activity on the mitochondrial surface. J Cell Biol 130:345-354.
    • (1995) J Cell Biol , vol.130 , pp. 345-354
    • Simon, V.R.1    Swavne, T.C.2    Pon, L.A.3
  • 106
    • 0032477853 scopus 로고    scopus 로고
    • Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus
    • Simon JP, Shen TH, Ivanov IE, Gravotta D, Morimoto T, Adesnik M, Sabatini DD. 1998. Coatomer, but not P200/myosin II, is required for the in vitro formation of trans-Golgi network-derived vesicles containing the envelope glycoprotein of vesicular stomatitis virus. Proc Natl Acad Sci USA 95:1073-1078.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1073-1078
    • Simon, J.P.1    Shen, T.H.2    Ivanov, I.E.3    Gravotta, D.4    Morimoto, T.5    Adesnik, M.6    Sabatini, D.D.7
  • 107
    • 0017871029 scopus 로고
    • Filament arrangements in negatively stained cultured cells: The organization of actin
    • Small JV, Celis JE. 1978. Filament arrangements in negatively stained cultured cells: the organization of actin. Cytobiologie 16:308-325.
    • (1978) Cytobiologie , vol.16 , pp. 308-325
    • Small, J.V.1    Celis, J.E.2
  • 108
    • 0017802361 scopus 로고
    • Polarity of actin at the leading edge of cultured cells
    • Small JV, Isenberg G, Celis JE. 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
  • 109
    • 0028024592 scopus 로고
    • Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane
    • Sogo LF, Yaffe MP. 1994. Regulation of mitochondrial morphology and inheritance by Mdm10p, a protein of the mitochondrial outer membrane. J Cell Biol 126:1361-1373.
    • (1994) J Cell Biol , vol.126 , pp. 1361-1373
    • Sogo, L.F.1    Yaffe, M.P.2
  • 110
    • 0032516854 scopus 로고    scopus 로고
    • Vesicle budding on Golgi membranes: Regulation by G proteins and myosin motors
    • Stow JL, Heimann K. 1998. Vesicle budding on Golgi membranes: regulation by G proteins and myosin motors. Biochim Biophys Acta 1404:161-171.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 161-171
    • Stow, J.L.1    Heimann, K.2
  • 112
    • 0029048597 scopus 로고
    • Actin-dependent light-induced translocation of mitochondria and ER cisternae in the photoreceptor cells of the locust Schistocerca gregaria
    • Stürmer K, Baumann O, Walz B. 1995. Actin-dependent light-induced translocation of mitochondria and ER cisternae in the photoreceptor cells of the locust Schistocerca gregaria. J Cell Sci 108:2273-2283.
    • (1995) J Cell Sci , vol.108 , pp. 2273-2283
    • Stürmer, K.1    Baumann, O.2    Walz, B.3
  • 113
    • 0022733229 scopus 로고
    • Actin cytoskeleton of spread fibroblasts appears to assemble at the cell edges
    • Svitkina TM, Neyfakh AA Jr, Bershadsky AD. 1986. Actin cytoskeleton of spread fibroblasts appears to assemble at the cell edges. J Cell Sci 82:235-248.
    • (1986) J Cell Sci , vol.82 , pp. 235-248
    • Svitkina, T.M.1    Neyfakh A.A., Jr.2    Bershadsky, A.D.3
  • 114
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization
    • Symons M, Derry JM, Karlak B, Jiang S, Lemahieu V, McCormick F, Francke U, Abo A. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 117
    • 0029974997 scopus 로고    scopus 로고
    • Examination of the endosomal and lysosomal pathways in Dictyostelium discoideum myosin I mutants
    • Temesvari LA, Bush JM, Peterson MD, Novak KD, Titus MA, Cardelli, JA. 1996. Examination of the endosomal and lysosomal pathways in Dictyostelium discoideum myosin I mutants. J Cell Sci 109:663-673.
    • (1996) J Cell Sci , vol.109 , pp. 663-673
    • Temesvari, L.A.1    Bush, J.M.2    Peterson, M.D.3    Novak, K.D.4    Titus, M.A.5    Cardelli, J.A.6
  • 118
    • 0019503649 scopus 로고
    • Actin filaments elongate from their membrane-associated ends
    • Tilney LG, Bonder EM, DeRosier DJ. 1981. Actin filaments elongate from their membrane-associated ends. J Cell Biol 90:485-494.
    • (1981) J Cell Biol , vol.90 , pp. 485-494
    • Tilney, L.G.1    Bonder, E.M.2    DeRosier, D.J.3
  • 119
    • 0031779777 scopus 로고    scopus 로고
    • Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex
    • Valderrama F, Babia T, Ayala I, Kok JW, Renau-Piqueras J, Egea G. 1998. Actin microfilaments are essential for the cytological positioning and morphology of the Golgi complex. Eur J Cell Biol 76:9-17.
    • (1998) Eur J Cell Biol , vol.76 , pp. 9-17
    • Valderrama, F.1    Babia, T.2    Ayala, I.3    Kok, J.W.4    Renau-Piqueras, J.5    Egea, G.6
  • 120
    • 0032896483 scopus 로고    scopus 로고
    • The subapical actin cytoskeleton regulates secretion and membrane retrieval in pancreatic acinar cells
    • Valentijn KM, Gumkowski FD, Jamieson JD. 1998. The subapical actin cytoskeleton regulates secretion and membrane retrieval in pancreatic acinar cells. J Cell Sci 112:81-96.
    • (1998) J Cell Sci , vol.112 , pp. 81-96
    • Valentijn, K.M.1    Gumkowski, F.D.2    Jamieson, J.D.3
  • 121
    • 0028940724 scopus 로고
    • Delivery to lysosomes in the human carcinoma cell line HEp-2 involves an actin filament-facilitated fusion between mature endosomes and preexisting lysosomes
    • Van Deurs B, Holm PK, Kayser L, Sandvig K. 1995. Delivery to lysosomes in the human carcinoma cell line HEp-2 involves an actin filament-facilitated fusion between mature endosomes and preexisting lysosomes. Eur J Cell Biol 66:309-323.
    • (1995) Eur J Cell Biol , vol.66 , pp. 309-323
    • Van Deurs, B.1    Holm, P.K.2    Kayser, L.3    Sandvig, K.4
  • 122
    • 0030665266 scopus 로고    scopus 로고
    • Cytoplasmic assembly of microtubules in cultured cells
    • Vorobjev IA, Svitkina TM, Borisy GG. 1997. Cytoplasmic assembly of microtubules in cultured cells. J Cell Sci 110:2635-2645.
    • (1997) J Cell Sci , vol.110 , pp. 2635-2645
    • Vorobjev, I.A.1    Svitkina, T.M.2    Borisy, G.G.3
  • 123
    • 0026779476 scopus 로고
    • Tissue distribution and subcellular localization of mammalian myosin I
    • Wagner MC, Barylko B, Albanesi JP. 1992. Tissue distribution and subcellular localization of mammalian myosin I. J Cell Biol 119:163-170.
    • (1992) J Cell Biol , vol.119 , pp. 163-170
    • Wagner, M.C.1    Barylko, B.2    Albanesi, J.P.3
  • 124
    • 0030056271 scopus 로고    scopus 로고
    • Unmasking mRNA in clam oocytes: Role of phosphorylation of a 3' UTR masking element-binding protein at fertilization
    • Walker J, Dale M, Standart N. 1996. Unmasking mRNA in clam oocytes: role of phosphorylation of a 3' UTR masking element-binding protein at fertilization. Dev Biol 173:292-305.
    • (1996) Dev Biol , vol.173 , pp. 292-305
    • Walker, J.1    Dale, M.2    Standart, N.3
  • 125
    • 0022390903 scopus 로고
    • Exchange of actin subunits at the leading edge of living fibroblasts: Possible role of treadmilling
    • Wang YL. 1985. Exchange of actin subunits at the leading edge of living fibroblasts: possible role of treadmilling. J Cell Biol 101:597-602.
    • (1985) J Cell Biol , vol.101 , pp. 597-602
    • Wang, Y.L.1
  • 126
    • 0030803342 scopus 로고    scopus 로고
    • The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport
    • Wei Q, Wu X, Hammer JA III. 1997. The predominant defect in dilute melanocytes is in melanosome distribution and not cell shape, supporting a role for myosin V in melanosome transport. J Muscle Res Cell Motil 18:517-527.
    • (1997) J Muscle Res Cell Motil , vol.18 , pp. 517-527
    • Wei, Q.1    Wu, X.2    Hammer J.A. III3
  • 128
  • 129
    • 0030964893 scopus 로고    scopus 로고
    • Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor
    • Wu X, Bowers B, Wei Q, Kocher B, Hammer JA III. 1997. Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J Cell Sci 110:847-859.
    • (1997) J Cell Sci , vol.110 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer J.A. III5
  • 130
    • 0032576622 scopus 로고    scopus 로고
    • Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo
    • Wu X, Bowers B, Rao K, Wei Q, Hammer JA III. 1998. Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J Cell Biol 143:1899-1918.
    • (1998) J Cell Biol , vol.143 , pp. 1899-1918
    • Wu, X.1    Bowers, B.2    Rao, K.3    Wei, Q.4    Hammer J.A. III5
  • 131
    • 0033525615 scopus 로고    scopus 로고
    • The machinery of mitochondrial inheritance and behavior
    • Yaffe MP. 1999. The machinery of mitochondrial inheritance and behavior. Science 283:1493-1497.
    • (1999) Science , vol.283 , pp. 1493-1497
    • Yaffe, M.P.1
  • 132
    • 0026754022 scopus 로고
    • The localization of myosin I and myosin II in Acanthamoeba by fluorescence microscopy
    • Yonemura S, Pollard TD. 1992. The localization of myosin I and myosin II in Acanthamoeba by fluorescence microscopy. J Cell Sci 102:629-642.
    • (1992) J Cell Sci , vol.102 , pp. 629-642
    • Yonemura, S.1    Pollard, T.D.2


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