메뉴 건너뛰기




Volumn 43, Issue C, 1996, Pages 53-71

Chapter 4 Role of the Cytoskeleton and Molecular Motors in Transport between the Golgi Complex and Plasma Membrane

Author keywords

[No Author keywords available]

Indexed keywords


EID: 77956672574     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)60384-6     Document Type: Article
Times cited : (3)

References (92)
  • 1
    • 0024370276 scopus 로고
    • Role of microtubules in polarized delivery of apical membrane proteins to the brush border of the intestinal epithelium.
    • Achler C., Filmer D., Merte C., and Drenckhahn D. Role of microtubules in polarized delivery of apical membrane proteins to the brush border of the intestinal epithelium. J. Cell Biol. 109 (1989) 179-189
    • (1989) J. Cell Biol. , vol.109 , pp. 179-189
    • Achler, C.1    Filmer, D.2    Merte, C.3    Drenckhahn, D.4
  • 2
    • 0023054684 scopus 로고
    • Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I.
    • Adams R.J., and Pollard T.D. Propulsion of organelles isolated from Acanthamoeba along actin filaments by myosin-I. Nature (London) 322 (1986) 754-756
    • (1986) Nature (London) , vol.322 , pp. 754-756
    • Adams, R.J.1    Pollard, T.D.2
  • 3
    • 0024346185 scopus 로고
    • Binding of myosin I to membrane lipids.
    • Adams R.J., and Pollard T.D. Binding of myosin I to membrane lipids. Nature (London) 340 (1989) 565-568
    • (1989) Nature (London) , vol.340 , pp. 565-568
    • Adams, R.J.1    Pollard, T.D.2
  • 5
    • 0024811663 scopus 로고
    • The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium.
    • Bacallao R., Antony C., Dotti C., Karsenti E., Stelzer E.H.K., and Simons K. The subcellular organization of Madin-Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109 (1989) 2817-2832
    • (1989) J. Cell Biol. , vol.109 , pp. 2817-2832
    • Bacallao, R.1    Antony, C.2    Dotti, C.3    Karsenti, E.4    Stelzer, E.H.K.5    Simons, K.6
  • 6
    • 0026457072 scopus 로고
    • Differential localization of Acanthamoeba myosin I isoforms.
    • Baines I.C., Brzeska H., and Korn E.D. Differential localization of Acanthamoeba myosin I isoforms. J. Cell Biol. 119 (1992) 1193-1203
    • (1992) J. Cell Biol. , vol.119 , pp. 1193-1203
    • Baines, I.C.1    Brzeska, H.2    Korn, E.D.3
  • 7
    • 0029148548 scopus 로고
    • Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii.
    • Baines I.C., Corigliano-Murphy A., and Korn E.D. Quantification and localization of phosphorylated myosin I isoforms in Acanthamoeba castellanii. J. Cell Biol. 130 (1995) 591-603
    • (1995) J. Cell Biol. , vol.130 , pp. 591-603
    • Baines, I.C.1    Corigliano-Murphy, A.2    Korn, E.D.3
  • 8
    • 0024002767 scopus 로고
    • Plasma membrane protein sorting in epithelial cells: Do secretory pathways hold the key?
    • Bartles J.R., and Hubbard A.L. Plasma membrane protein sorting in epithelial cells: Do secretory pathways hold the key?. Trends Biochem. Sci. 13 (1988) 181-184
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 181-184
    • Bartles, J.R.1    Hubbard, A.L.2
  • 11
    • 0025605057 scopus 로고
    • Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells.
    • Breitfeld P.P., McKinnon W.C., and Mostov K.E. Effect of nocodazole on vesicular traffic to the apical and basolateral surfaces of polarized MDCK cells. J. Cell Biol. 111 (1990) 2365-2373
    • (1990) J. Cell Biol. , vol.111 , pp. 2365-2373
    • Breitfeld, P.P.1    McKinnon, W.C.2    Mostov, K.E.3
  • 12
    • 33646298348 scopus 로고
    • The brush border: A model for structure, biochemistry, motility, and assembly of the cytoskeleton.
    • Burgess D.R. The brush border: A model for structure, biochemistry, motility, and assembly of the cytoskeleton. Adv. Cell Biol. 1 (1987) 31-58
    • (1987) Adv. Cell Biol. , vol.1 , pp. 31-58
    • Burgess, D.R.1
  • 15
    • 0025264994 scopus 로고
    • Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.
    • Collins K., Sellers J.R., and Matsudaira P. Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro. J. Cell Biol. 110 (1990) 1137-1147
    • (1990) J. Cell Biol. , vol.110 , pp. 1137-1147
    • Collins, K.1    Sellers, J.R.2    Matsudaira, P.3
  • 17
    • 0027523460 scopus 로고
    • Relative distribution of actin, myosin I, and myosin II during wound healing response of fibroblasts.
    • Conrad P.A., Giuliano K.A., Fisher G., Collins K., Matsudaira P.T., and Taylor D.L. Relative distribution of actin, myosin I, and myosin II during wound healing response of fibroblasts. J. Cell Biol. 120 (1993) 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
  • 18
    • 0023368572 scopus 로고
    • The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.
    • Conzelman K.A., and Mooseker M.S. The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase. J. Cell Biol. 105 (1987) 313-324
    • (1987) J. Cell Biol. , vol.105 , pp. 313-324
    • Conzelman, K.A.1    Mooseker, M.S.2
  • 19
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex.
    • Corthésy-Theulaz I., Pauloin A., and Pfeffer S. Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol. 118 (1992) 1333-1345
    • (1992) J. Cell Biol. , vol.118 , pp. 1333-1345
    • Corthésy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.3
  • 20
    • 0028091983 scopus 로고
    • Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles.
    • Dillman J.F., and Pfister K.K. Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles. J. Cell Biol. 127 (1994) 1671-1681
    • (1994) J. Cell Biol. , vol.127 , pp. 1671-1681
    • Dillman, J.F.1    Pfister, K.K.2
  • 21
    • 0027452047 scopus 로고
    • Inhibition of contractile vacuole function in vivo by antibodies against myosin-I.
    • Doberstein S.K., Baines I.C., Wiegand G., Korn E.D., and Pollard T.P. Inhibition of contractile vacuole function in vivo by antibodies against myosin-I. Nature (London) 365 (1993) 841-843
    • (1993) Nature (London) , vol.365 , pp. 841-843
    • Doberstein, S.K.1    Baines, I.C.2    Wiegand, G.3    Korn, E.D.4    Pollard, T.P.5
  • 22
    • 0026017320 scopus 로고
    • Polarized sorting of glypiated proteins in hippocampal neurons.
    • Dotti C.G., Parton R.G., and Simons K. Polarized sorting of glypiated proteins in hippocampal neurons. Nature (London) 349 (1991) 158-161
    • (1991) Nature (London) , vol.349 , pp. 158-161
    • Dotti, C.G.1    Parton, R.G.2    Simons, K.3
  • 23
    • 0024078086 scopus 로고
    • Organization of the actin filament cytoskeleton in the intestinal brush border: A quantitative and qualitative immunoelectron microscope study.
    • Drenckhahn D., and Dermietzel R. Organization of the actin filament cytoskeleton in the intestinal brush border: A quantitative and qualitative immunoelectron microscope study. J. Cell Biol. 107 (1988) 1037-1048
    • (1988) J. Cell Biol. , vol.107 , pp. 1037-1048
    • Drenckhahn, D.1    Dermietzel, R.2
  • 24
    • 77956681111 scopus 로고
    • Brush border myosin I is required for the apical translocation of GPI anchor membrane proteins.
    • Durrbach A., Louvard D., and Coudrier E. Brush border myosin I is required for the apical translocation of GPI anchor membrane proteins. Mol. Biol. Cell 6 (1995) 268a
    • (1995) Mol. Biol. Cell , vol.6
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 25
    • 0024509437 scopus 로고
    • Nocodazole, a microtubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2).
    • Eilers U., Klumperman J., and Hauri H.-P. Nocodazole, a microtubule-active drug, interferes with apical protein delivery in cultured intestinal epithelial cells (Caco-2). J. Cell Biol. 108 (1989) 13-22
    • (1989) J. Cell Biol. , vol.108 , pp. 13-22
    • Eilers, U.1    Klumperman, J.2    Hauri, H.-P.3
  • 26
    • 0027068050 scopus 로고
    • Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains.
    • Espreafico E.M., Cheney R.E., Matteoli M., Nascimento A.A.C., DeCamilli P.V., Larson R.E., and Mooseker M.S. Primary structure and cellular localization of chicken brain myosin-V (p190), an unconventional myosin with calmodulin light chains. J. Cell Biol. 119 (1992) 1541-1558
    • (1992) J. Cell Biol. , vol.119 , pp. 1541-1558
    • Espreafico, E.M.1    Cheney, R.E.2    Matteoli, M.3    Nascimento, A.A.C.4    DeCamilli, P.V.5    Larson, R.E.6    Mooseker, M.S.7
  • 27
    • 0024283152 scopus 로고
    • An ATPase with properties expected for the organelle motor of the giant amoeba, Reticulomyxa.
    • Euteneur U., Koonce M.P., Pfister K.K., and Schliwa M. An ATPase with properties expected for the organelle motor of the giant amoeba, Reticulomyxa. Nature (London) 332 (1988) 176-178
    • (1988) Nature (London) , vol.332 , pp. 176-178
    • Euteneur, U.1    Koonce, M.P.2    Pfister, K.K.3    Schliwa, M.4
  • 28
    • 8944252897 scopus 로고
    • Subcellular localization of myosin V in nerve growth cones.
    • Evans L.L., Hammer J., and Bridgman P.C. Subcellular localization of myosin V in nerve growth cones. Mol. Biol. Cell 6 (1995) 145a
    • (1995) Mol. Biol. Cell , vol.6
    • Evans, L.L.1    Hammer, J.2    Bridgman, P.C.3
  • 29
    • 0027393092 scopus 로고
    • Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein.
    • Fath K.R., and Burgess D.R. 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 (1993) 117-127
    • (1993) J. Cell Biol. , vol.120 , pp. 117-127
    • Fath, K.R.1    Burgess, D.R.2
  • 30
    • 0028049387 scopus 로고
    • Membrane motility mediated by unconventional myosin.
    • Fath K.R., and Burgess D.R. Membrane motility mediated by unconventional myosin. Curr. Opin. Cell Biol. 6 (1994) 131-135
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 131-135
    • Fath, K.R.1    Burgess, D.R.2
  • 32
    • 0023746711 scopus 로고
    • Two classes of actin microfilaments are associated with the inner cytoskeleton of axons.
    • Fath K., and Lasek R. Two classes of actin microfilaments are associated with the inner cytoskeleton of axons. J. Cell Biol. 107 (1988) 613-621
    • (1988) J. Cell Biol. , vol.107 , pp. 613-621
    • Fath, K.1    Lasek, R.2
  • 33
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells.
    • Fath K.R., Trimbur G.M., and Burgess D.R. Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells. J. Cell Biol. 126 (1994) 661-675
    • (1994) J. Cell Biol. , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 34
    • 0024956931 scopus 로고
    • Myosin I is located at the leading edges of locomoting Dictyostelium amoebae.
    • Fukui Y., Lynch T.J., Brzeska H., and Korn E.D. Myosin I is located at the leading edges of locomoting Dictyostelium amoebae. Nature (London) 341 (1989) 328-331
    • (1989) Nature (London) , vol.341 , pp. 328-331
    • Fukui, Y.1    Lynch, T.J.2    Brzeska, H.3    Korn, E.D.4
  • 35
    • 0025905152 scopus 로고
    • Microtubular organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells.
    • Gilbert T., Le Bivic A., Quaroni A., and Rodriguez-Boulan E. Microtubular organization and its involvement in the biogenetic pathways of plasma membrane proteins in Caco-2 intestinal epithelial cells. J. Cell Biol. 113 (1991) 275-288
    • (1991) J. Cell Biol. , vol.113 , pp. 275-288
    • Gilbert, T.1    Le Bivic, A.2    Quaroni, A.3    Rodriguez-Boulan, E.4
  • 36
    • 0028902506 scopus 로고
    • The role of Myo2, a yeast class V myosin, in vesicular transport.
    • Govindan B., Bowser R., and Novick P. The role of Myo2, a yeast class V myosin, in vesicular transport. J. Cell Biol. 128 (1995) 1055-1068
    • (1995) J. Cell Biol. , vol.128 , pp. 1055-1068
    • Govindan, B.1    Bowser, R.2    Novick, P.3
  • 37
    • 0019074235 scopus 로고
    • Intracellular transport in neurons.
    • Grafstein B., and Forman D.S. Intracellular transport in neurons. Physiol. Rev. 60 (1980) 1167-1283
    • (1980) Physiol. Rev. , vol.60 , pp. 1167-1283
    • Grafstein, B.1    Forman, D.S.2
  • 38
    • 0024997819 scopus 로고
    • Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo.
    • Hirokawa N., Sato-Yoshitake R., Yoshida T., and Kawashima T. Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo. J. Cell Biol. 111 (1990) 1027-1037
    • (1990) J. Cell Biol. , vol.111 , pp. 1027-1037
    • Hirokawa, N.1    Sato-Yoshitake, R.2    Yoshida, T.3    Kawashima, T.4
  • 41
    • 0028170819 scopus 로고
    • Dyneins: Molecular structure and cellular function.
    • Holzbaur E.L.F., and Vallee R.B. Dyneins: Molecular structure and cellular function. Annu. Rev. Cell Biol 10 (1994) 339-372
    • (1994) Annu. Rev. Cell Biol , vol.10 , pp. 339-372
    • Holzbaur, E.L.F.1    Vallee, R.B.2
  • 42
    • 23444436196 scopus 로고
    • Cellular roles of kinesin and related proteins.
    • Hoyt M.A. Cellular roles of kinesin and related proteins. Curr. Biol. 6 (1994) 63-68
    • (1994) Curr. Biol. , vol.6 , pp. 63-68
    • Hoyt, M.A.1
  • 43
    • 0023268698 scopus 로고
    • Loss of microtubules and alteration of glycoprotein migration in organ cultures of mouse intestine exposed to nocadazole or colchicine.
    • Hugon J.S., Bennett G., Pothier P., and Ngoma Z. Loss of microtubules and alteration of glycoprotein migration in organ cultures of mouse intestine exposed to nocadazole or colchicine. Cell Tissue Res. 248 (1987) 653-662
    • (1987) Cell Tissue Res. , vol.248 , pp. 653-662
    • Hugon, J.S.1    Bennett, G.2    Pothier, P.3    Ngoma, Z.4
  • 44
    • 0025168710 scopus 로고
    • Differential microtubule requirements for transcytosis in MDCK cells.
    • Hunziker W., Male P., and Mellman I. Differential microtubule requirements for transcytosis in MDCK cells. EMBO J. 9 (1990) 3515-3525
    • (1990) EMBO J. , vol.9 , pp. 3515-3525
    • Hunziker, W.1    Male, P.2    Mellman, I.3
  • 45
    • 0025801365 scopus 로고
    • The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles.
    • Johnston G.C., Prendergast J.A., and Singer R.A. The Saccharomyces cerevisiae MYO2 gene encodes an essential myosin for vectorial transport of vesicles. J. Cell Biol. 113 (1991) 539-551
    • (1991) J. Cell Biol. , vol.113 , pp. 539-551
    • Johnston, G.C.1    Prendergast, J.A.2    Singer, R.A.3
  • 46
    • 0028806377 scopus 로고
    • Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex.
    • Karki S., and Holzbaur E.L.F. Affinity chromatography demonstrates a direct binding between cytoplasmic dynein and the dynactin complex. J. Biol. Chem. 270 (1995) 28806-28811
    • (1995) J. Biol. Chem. , vol.270 , pp. 28806-28811
    • Karki, S.1    Holzbaur, E.L.F.2
  • 47
    • 0026475396 scopus 로고
    • An unconventional myosin heavy chain gene from Drosophila melanoguster.
    • Kellerman K.A., and Miller K.G. An unconventional myosin heavy chain gene from Drosophila melanoguster. J. Cell Biol. 119 (1992) 823-834
    • (1992) J. Cell Biol. , vol.119 , pp. 823-834
    • Kellerman, K.A.1    Miller, K.G.2
  • 48
    • 0020316410 scopus 로고
    • Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound.
    • Kupfer A.G., Louvard D., and Singer S.J. Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound. Proc. Natl. Acad. Sci. U.S.A. 79 (1983) 2603-2607
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 2603-2607
    • Kupfer, A.G.1    Louvard, D.2    Singer, S.J.3
  • 49
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm.
    • Kuznetsov S.A., Langford G.M., and Weiss D.G. Actin-dependent organelle movement in squid axoplasm. Nature (London) 356 (1992) 722-725
    • (1992) Nature (London) , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 50
    • 0026630055 scopus 로고
    • Cytoplasmic dynein is a vesicle protein.
    • Lacey M.L., and Haimo L.T. Cytoplasmic dynein is a vesicle protein. J. Biol. Chem. 267 (1992) 4793-4798
    • (1992) J. Biol. Chem. , vol.267 , pp. 4793-4798
    • Lacey, M.L.1    Haimo, L.T.2
  • 51
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells.
    • Lafont F., Burkhardt J.K., and Simons K. Involvement of microtubule motors in basolateral and apical transport in kidney cells. Nature (London) 372 (1994) 801-803
    • (1994) Nature (London) , vol.372 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 52
    • 0028093376 scopus 로고
    • Movement of axoplasmic organelles on actin filaments assembled on acrosomal processes: Evidence for a barbed-end-directed organelle motor.
    • Langford G.M., Kuznetsov S.A., Johnson D., Cohen D.L., and Weiss D.G. Movement of axoplasmic organelles on actin filaments assembled on acrosomal processes: Evidence for a barbed-end-directed organelle motor. J. Cell Sci. 107 (1994) 2291-2298
    • (1994) J. Cell Sci. , vol.107 , pp. 2291-2298
    • Langford, G.M.1    Kuznetsov, S.A.2    Johnson, D.3    Cohen, D.L.4    Weiss, D.G.5
  • 53
    • 0026539415 scopus 로고
    • Suppression of a myosin defect by a kinesin-related gene.
    • Lillie S.H., and Brown S.S. Suppression of a myosin defect by a kinesin-related gene. Nature (London) 356 (1992) 358-361
    • (1992) Nature (London) , vol.356 , pp. 358-361
    • Lillie, S.H.1    Brown, S.S.2
  • 54
    • 0026601916 scopus 로고
    • Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells.
    • Lin S.X.H., and Collins C.A. Immunolocalization of cytoplasmic dynein to lysosomes in cultured cells. J. Cell Sci. 101 (1992) 125-137
    • (1992) J. Cell Sci. , vol.101 , pp. 125-137
    • Lin, S.X.H.1    Collins, C.A.2
  • 55
    • 0029103105 scopus 로고
    • Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex.
    • Lippincott-Schwartz J., and Cole N.B. Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex. Biochem. Soc. Trans. 23 (1995) 544-548
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 544-548
    • Lippincott-Schwartz, J.1    Cole, N.B.2
  • 56
    • 0024362690 scopus 로고
    • The function of the major cytoskeletal components of the brush border.
    • Louvard D. The function of the major cytoskeletal components of the brush border. Curr. Opin. Cell Biol. 1 (1989) 51-57
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 51-57
    • Louvard, D.1
  • 57
    • 0028078889 scopus 로고
    • Physical properties of cytoplasm.
    • Luby-Phelps K. Physical properties of cytoplasm. Curr. Biol. 6 (1994) 3-9
    • (1994) Curr. Biol. , vol.6 , pp. 3-9
    • Luby-Phelps, K.1
  • 58
    • 0025184423 scopus 로고
    • Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2).
    • Matter K., Bucher K., and Hauri H.-P. Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2). EMBO J. 9 (1990) 3163-3170
    • (1990) EMBO J. , vol.9 , pp. 3163-3170
    • Matter, K.1    Bucher, K.2    Hauri, H.-P.3
  • 59
    • 0028126085 scopus 로고
    • Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery.
    • Mays R.W., Beck K.A., and Nelson J.W. Organization and function of the cytoskeleton in polarized epithelial cells: A component of the protein sorting machinery. Curr. Opin. Cell Biol. 6 (1994) 16-24
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 16-24
    • Mays, R.W.1    Beck, K.A.2    Nelson, J.W.3
  • 60
    • 0011856830 scopus 로고
    • Mechanisms of molecular sorting in polarized cells: relevance to Alzheimer's disease.
    • Kosik K.S., Christen Y., and Selkoe D.J. (Eds), Springer-Verlag, Berlin
    • Mellman I., Matter K., Yamamoto E., Pollack N., Roome J., Felsenstein K., and Roberts S. Mechanisms of molecular sorting in polarized cells: relevance to Alzheimer's disease. In: Kosik K.S., Christen Y., and Selkoe D.J. (Eds). "Alzheimer's Disease: Lessons from Cell Biology" (1995), Springer-Verlag, Berlin 14-26
    • (1995) "Alzheimer's Disease: Lessons from Cell Biology" , pp. 14-26
    • Mellman, I.1    Matter, K.2    Yamamoto, E.3    Pollack, N.4    Roome, J.5    Felsenstein, K.6    Roberts, S.7
  • 61
    • 0028359778 scopus 로고
    • Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos.
    • Mermall V., McNally J.G., and Miller K.G. Transport of cytoplasmic particles catalysed by an unconventional myosin in living Drosophila embryos. Nature (London) 369 (1994) 560-562
    • (1994) Nature (London) , vol.369 , pp. 560-562
    • Mermall, V.1    McNally, J.G.2    Miller, K.G.3
  • 62
    • 0022172245 scopus 로고
    • Organization, chemistry and assembly of the cytoskeletal apparatus of the intestinal brush border.
    • Mooseker M.S. Organization, chemistry and assembly of the cytoskeletal apparatus of the intestinal brush border. Annu. Rev. Cell Biol. 1 (1985) 209-241
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 209-241
    • Mooseker, M.S.1
  • 63
    • 0344914021 scopus 로고
    • A multitude of myosins.
    • Mooseker M. A multitude of myosins. Curr. Biol. 3 (1993) 245-248
    • (1993) Curr. Biol. , vol.3 , pp. 245-248
    • Mooseker, M.1
  • 65
    • 0021244966 scopus 로고
    • Monomer-polymer equilibria in the axon: direct measurement of tubulin and actin as polymer and monomer in axoplasm.
    • Morris J., and Lasek R. Monomer-polymer equilibria in the axon: direct measurement of tubulin and actin as polymer and monomer in axoplasm. J. Cell Biol. 98 (1984) 2064-2076
    • (1984) J. Cell Biol. , vol.98 , pp. 2064-2076
    • Morris, J.1    Lasek, R.2
  • 66
    • 0024454714 scopus 로고
    • Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial cell, Madin-Darby kidney.
    • Parczyk K., Haase W., and Kondor-Koch C. Microtubules are involved in the secretion of proteins at the apical cell surface of the polarized epithelial cell, Madin-Darby kidney. J. Biol. Chem. 264 (1989) 16837-16846
    • (1989) J. Biol. Chem. , vol.264 , pp. 16837-16846
    • Parczyk, K.1    Haase, W.2    Kondor-Koch, C.3
  • 67
    • 0023608935 scopus 로고
    • Map 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties.
    • Paschal B.M., Shpetner H.S., and Vallee R.B. Map 1C is a microtubule-activated ATPase which translocates microtubules in vitro and has dynein-like properties. Nature (London) 105 (1987) 1273-1282
    • (1987) Nature (London) , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 68
    • 4243947092 scopus 로고
    • Association of dilute with melanosomes in melanocytes.
    • Provance Jr. D.W., and Mercer J.A. Association of dilute with melanosomes in melanocytes. Mol. Biol. Cell. 6 (1995) 146a
    • (1995) Mol. Biol. Cell. , vol.6
    • Provance Jr., D.W.1    Mercer, J.A.2
  • 71
    • 0023293841 scopus 로고
    • Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells.
    • Rindler M.J., Ivanov I.E., and Sabatini D.D. Microtubule-acting drugs lead to the nonpolarized delivery of the influenza hemagglutinin to the cell surface of polarized Madin-Darby canine kidney cells. J. Cell Biol. 104 (1987) 231-241
    • (1987) J. Cell Biol. , vol.104 , pp. 231-241
    • Rindler, M.J.1    Ivanov, I.E.2    Sabatini, D.D.3
  • 72
    • 0021189557 scopus 로고
    • Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane.
    • Rogalski A.A., Bergmann J.E., and Singer S.J. Effect of microtubule assembly status on the intracellular processing and surface expression of an integral protein of the plasma membrane. J. Cell Biol. 99 (1984) 1101-1109
    • (1984) J. Cell Biol. , vol.99 , pp. 1101-1109
    • Rogalski, A.A.1    Bergmann, J.E.2    Singer, S.J.3
  • 73
    • 0022479585 scopus 로고
    • Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity.
    • Salas P.J.I., Misek D.E., Vega-Salas D.E., Gundersen D., Cereijido M., and Rodriguez-Boulan R. Microtubules and actin filaments are not critically involved in the biogenesis of epithelial cell surface polarity. J. Cell Biol. 102 (1986) 1853-1867
    • (1986) J. Cell Biol. , vol.102 , pp. 1853-1867
    • Salas, P.J.I.1    Misek, D.E.2    Vega-Salas, D.E.3    Gundersen, D.4    Cereijido, M.5    Rodriguez-Boulan, R.6
  • 74
    • 0022609508 scopus 로고
    • Distribution of microtubules within the intestinal terminal web as revealed by quick-freezing and cryosubstitution.
    • Sandoz D., Lainé M.-C., and Nicolas G. Distribution of microtubules within the intestinal terminal web as revealed by quick-freezing and cryosubstitution. Eur. J. Cell Biol. 39 (1985) 481-484
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 481-484
    • Sandoz, D.1    Lainé, M.-C.2    Nicolas, G.3
  • 75
    • 0006163872 scopus 로고
    • Dynein is the motor for retrograde axonal transport of organelles.
    • Schnapp B.J., and Reese T.S. Dynein is the motor for retrograde axonal transport of organelles. Proc. Natl. Acad. Sci. U.S.A. 86 (1989) 1548-1552
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 1548-1552
    • Schnapp, B.J.1    Reese, T.S.2
  • 76
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus end-directed motor for membranous organelles.
    • Schroer T.A., Steuer E.R., and Sheetz M.P. Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell 56 (1989) 937-946
    • (1989) Cell , vol.56 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 77
    • 0029069185 scopus 로고
    • Transport of dendritic microtubules establishes their nonuniform polarity orientation.
    • Sharp D.J., Yu W., and Baas P.W. Transport of dendritic microtubules establishes their nonuniform polarity orientation. J. Cell Biol. 130 (1995) 95-103
    • (1995) J. Cell Biol. , vol.130 , pp. 95-103
    • Sharp, D.J.1    Yu, W.2    Baas, P.W.3
  • 78
    • 0026236553 scopus 로고
    • Axonal transport: Beyond kinesin and cytoplasmic dynein.
    • Sheetz M.P., and Martenson C.H. Axonal transport: Beyond kinesin and cytoplasmic dynein. Curr. Opin. Neurobiol. 1 (1991) 393-398
    • (1991) Curr. Opin. Neurobiol. , vol.1 , pp. 393-398
    • Sheetz, M.P.1    Martenson, C.H.2
  • 79
    • 0023376195 scopus 로고
    • Assembly of the intestinal brush border: Appearance and redistribution of microvillar core proteins in developing chick enterocytes.
    • Shibayama T., Carboni J.M., and Mooseker M.S. Assembly of the intestinal brush border: Appearance and redistribution of microvillar core proteins in developing chick enterocytes. J. Cell Biol. 105 (1987) 335-344
    • (1987) J. Cell Biol. , vol.105 , pp. 335-344
    • Shibayama, T.1    Carboni, J.M.2    Mooseker, M.S.3
  • 80
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia.
    • Simons K., and Wandinger-Ness A. Polarized sorting in epithelia. Cell 62 (1990) 207-210
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 81
    • 0022412716 scopus 로고
    • Microtubules and the organization of the Golgi complex.
    • Thyberg J., and Moskalewski S. Microtubules and the organization of the Golgi complex. Exp. Cell Res. 159 (1985) 146
    • (1985) Exp. Cell Res. , vol.159 , pp. 146
    • Thyberg, J.1    Moskalewski, S.2
  • 82
    • 0027367571 scopus 로고
    • From fat yeast and nervous mice to brain myosin-V.
    • Titus M.A. From fat yeast and nervous mice to brain myosin-V. Cell 75 (1993) 9-11
    • (1993) Cell , vol.75 , pp. 9-11
    • Titus, M.A.1
  • 84
    • 0024841330 scopus 로고
    • Use of transgenic mice to study the routing of secretory proteins in intestinal epithelial cells: Analysis of human growth hormone compartmentalization as a function of cell type and differentiation.
    • Trahair J.F., Neutra M.R., and Gordon J.I. Use of transgenic mice to study the routing of secretory proteins in intestinal epithelial cells: Analysis of human growth hormone compartmentalization as a function of cell type and differentiation. J. Cell Biol. 109 (1989) 3231-3242
    • (1989) J. Cell Biol. , vol.109 , pp. 3231-3242
    • Trahair, J.F.1    Neutra, M.R.2    Gordon, J.I.3
  • 85
    • 0022385727 scopus 로고
    • Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility.
    • Vale R.D., Reese T.S., and Sheetz M.P. Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility. Cell 42 (1985) 39-50
    • (1985) Cell , vol.42 , pp. 39-50
    • Vale, R.D.1    Reese, T.S.2    Sheetz, M.P.3
  • 88
    • 0026779476 scopus 로고
    • Tissue distribution and subcellular localization of mammalian myosin 1.
    • Wagner M.C., Barylko B., and Albanesi J.P. Tissue distribution and subcellular localization of mammalian myosin 1. J. Cell Biol. 119 (1992) 163-170
    • (1992) J. Cell Biol. , vol.119 , pp. 163-170
    • Wagner, M.C.1    Barylko, B.2    Albanesi, J.P.3
  • 89
    • 0027267694 scopus 로고
    • Cytoplasmic microtubule-associated motors.
    • Walker R.A., and Sheetz M.P. Cytoplasmic microtubule-associated motors. Annu. Rev. Biochem. 62 (1993) 429-451
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 429-451
    • Walker, R.A.1    Sheetz, M.P.2
  • 90
    • 0028790030 scopus 로고
    • Identification of Acan325 as a myosin-I-binding protein present with myosin-I on cellular organelles of Acanthamoeba.
    • Xu P., Zott A.S., and Zott H.G. Identification of Acan325 as a myosin-I-binding protein present with myosin-I on cellular organelles of Acanthamoeba. J. Biol. Chem. 270 (1995) 25316-25319
    • (1995) J. Biol. Chem. , vol.270 , pp. 25316-25319
    • Xu, P.1    Zott, A.S.2    Zott, H.G.3
  • 91
    • 0026754022 scopus 로고
    • The localization of myosin I and myosin II in Acanthamoeba by fluorescence microscopy.
    • Yonemura S., and Pollard T.D. The localization of myosin I and myosin II in Acanthamoeba by fluorescence microscopy. J. Cell Sci. 102 (1992) 629-642
    • (1992) J. Cell Sci. , vol.102 , pp. 629-642
    • Yonemura, S.1    Pollard, T.D.2
  • 92
    • 0026776714 scopus 로고
    • Association of calmodulin and an unconventional myosin with the contractile vacuole complex of Dictyostelium discoideum.
    • Zhu Q., and Clarke M. Association of calmodulin and an unconventional myosin with the contractile vacuole complex of Dictyostelium discoideum. J. Cell Biol. 118 (1992) 347-358
    • (1992) J. Cell Biol. , vol.118 , pp. 347-358
    • Zhu, Q.1    Clarke, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.