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Volumn 11, Issue 4, 1999, Pages 476-482

Membrane motors

Author keywords

[No Author keywords available]

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MYOSIN; PROTEIN;

EID: 0033179891     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80068-4     Document Type: Article
Times cited : (95)

References (85)
  • 1
    • 0032578031 scopus 로고    scopus 로고
    • Microtubule-based membrane movement
    • Lane J, Allan V: Microtubule-based membrane movement. Biochim Biophys Acta 1998, 1376:27-55.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 27-55
    • Lane, J.1    Allan, V.2
  • 3
    • 0029868995 scopus 로고    scopus 로고
    • Kinesin-II, a membrane traffic motor in axons, axonemes, and spindles
    • Scholey JM: Kinesin-ll, a membrane traffic motor in axons, axonemes, and spindles. J Cell Biol 1996, 133:1-4.
    • (1996) J Cell Biol , vol.133 , pp. 1-4
    • Scholey, J.M.1
  • 5
    • 0029155982 scopus 로고
    • KIF3A/B: A heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport
    • Yamazaki H, Nakata T, Okada Y, Hirokawa N: KIF3A/B: A heterodimeric kinesin superfamily protein that works as a microtubule plus end-directed motor for membrane organelle transport. J Cell Biol 1995, 130:1387-1399.
    • (1995) J Cell Biol , vol.130 , pp. 1387-1399
    • Yamazaki, H.1    Nakata, T.2    Okada, Y.3    Hirokawa, N.4
  • 6
    • 0031951034 scopus 로고    scopus 로고
    • Characterization of the KIF3C neural kinesin-like motor from mouse
    • Yang Z, Goldstein LSB: Characterization of the KIF3C neural kinesin-like motor from mouse. Mol Biol Cell 1998, 9:249-261.
    • (1998) Mol Biol Cell , vol.9 , pp. 249-261
    • Yang, Z.1    Goldstein, L.S.B.2
  • 7
    • 0032472369 scopus 로고    scopus 로고
    • The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin super-family motor KIF3
    • Nagata K-I, Puls A, Futter C, Aspenstrom P, Schaefer E, Nakata T, Hirokawa N, Hall A: The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin super-family motor KIF3. EMBO J 1998, 17:149-158.
    • (1998) EMBO J , vol.17 , pp. 149-158
    • Nagata, K.-I.1    Puls, A.2    Futter, C.3    Aspenstrom, P.4    Schaefer, E.5    Nakata, T.6    Hirokawa, N.7    Hall, A.8
  • 9
    • 0030933293 scopus 로고    scopus 로고
    • Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro
    • Rogers S, Tint I, Fanapour P, Gelfand V: Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro. Proc Natl Acad Sci USA 1997, 94:3720-3725.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3720-3725
    • Rogers, S.1    Tint, I.2    Fanapour, P.3    Gelfand, V.4
  • 10
    • 0032517764 scopus 로고    scopus 로고
    • Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores
    • Tuma MC, Zill A, Le Bot N, Vernos l, Gelfand V: Heterotrimeric kinesin II is the microtubule motor protein responsible for pigment dispersion in Xenopus melanophores. J Cell Biol 1998, 143:1547-1558. A variety of approaches are used to show that kinesin II, and not conventional kinesin, drives the rapid dispersal of pigment granules in Xenopus melanophores. We now know more about the motility of this organelle type than any other.
    • (1998) J Cell Biol , vol.143 , pp. 1547-1558
    • Tuma, M.C.1    Zill, A.2    Le Bot, N.3    Vernos, L.4    Gelfand, V.5
  • 11
    • 0032517780 scopus 로고    scopus 로고
    • Role of XKIp3, a subunit of the xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus
    • Le Bot N, Antony C, White J, Karsenti E, Vernos I: Role of XKIps, a subunit of the xenopus kinesin II heterotrimeric complex, in membrane transport between the endoplasmic reticulum and the Golgi apparatus. J Cell Biol 1998, 143:1559-1573. This study identifies XKlp3 as a motor protein, the activity of which seems to be required for traffic in both directions between the Golgi apparatus and the ER. One of a growing number of KRPs involved in Golgi apparatus function.
    • (1998) J Cell Biol , vol.143 , pp. 1559-1573
    • Le Bot, N.1    Antony, C.2    White, J.3    Karsenti, E.4    Vernos, I.5
  • 12
    • 0028641560 scopus 로고
    • KIF1B, a novel microtubule plus-end-directed monomeric motor protein for transport of mitochondria
    • Nangaku M, Sato Yoshitake R, Okada Y, Noda Y, Takemura R, Yamazaki H, Hirokawa N: KIF1B, a novel microtubule plus-end- Directed monomeric motor protein for transport of mitochondria. Cell 1994, 79:1209-1220.
    • (1994) Cell , vol.79 , pp. 1209-1220
    • Nangaku, M.1    Sato Yoshitake, R.2    Okada, Y.3    Noda, Y.4    Takemura, R.5    Yamazaki, H.6    Hirokawa, N.7
  • 13
    • 0032493768 scopus 로고    scopus 로고
    • Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum
    • Dorner C, Ciossek T, Muller S, Moller NPH, Ullrich A, Lammers R: Characterization of KIF1C, a new kinesin-like protein involved in vesicle transport from the Golgi apparatus to the endoplasmic reticulum. J Biol Chem 1998, 273:20267-20275.
    • (1998) J Biol Chem , vol.273 , pp. 20267-20275
    • Dorner, C.1    Ciossek, T.2    Muller, S.3    Moller, N.P.H.4    Ullrich, A.5    Lammers, R.6
  • 14
    • 0032559265 scopus 로고    scopus 로고
    • Interaction of a Golgi-associated kinesin-like protein with Rab6
    • Echard A, Jollivet F, Martinez O, Lacapère J-J, Rousselet A, Janoueix Lerosey I, Goud B: Interaction of a Golgi-associated kinesin-like protein with Rab6. Science 1998, 279:580-585. The authors identify Rabkinesin6 - a Golgi-localized KRP that interacts with Rab6 in its GTP- but not GDP-bound forms. This establishes a new, direct link between a regulator of membrane traffic and a motor protein.
    • (1998) Science , vol.279 , pp. 580-585
    • Echard, A.1    Jollivet, F.2    Martinez, O.3    Lacapère, J.-J.4    Rousselet, A.5    Lerosey, I.6    Goud, B.7
  • 15
    • 0032531562 scopus 로고    scopus 로고
    • KIF2β, a new kinesin superfamily protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation
    • Santama N, Krijnse-Locker J, Griffiths G, Noda Y, Hirokawa N, Dotti CG: KIF2β, a new kinesin superfamily protein in non-neuronal cells, is associated with lysosomes and may be implicated in their centrifugal translocation. EMBO J 1998, 17:5855-5867.
    • (1998) EMBO J , vol.17 , pp. 5855-5867
    • Santama, N.1    Krijnse-Locker, J.2    Griffiths, G.3    Noda, Y.4    Hirokawa, N.5    Dotti, C.G.6
  • 16
    • 0031965953 scopus 로고    scopus 로고
    • Dynein and dynein-related genes
    • Milisav I: Dynein and dynein-related genes. Cell Motil Cytoskeleton 1998, 39:261-272. A comprehensive review of dynein composition with an emphasis on molecular and classical genetic approaches.
    • (1998) Cell Motil Cytoskeleton , vol.39 , pp. 261-272
    • Milisav, I.1
  • 17
    • 0029905303 scopus 로고    scopus 로고
    • Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles
    • Vaisberg EA, Grissom PM, McIntosh JR: Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles. J Cell Biol 1996, 133:831-842.
    • (1996) J Cell Biol , vol.133 , pp. 831-842
    • Vaisberg, E.A.1    Grissom, P.M.2    McIntosh, J.R.3
  • 18
    • 0026345013 scopus 로고
    • Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein
    • Gill SR, Schroer TA, Szilak I, Steuer ER, Sheetz MP: Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J Cell Biol 1991, 115:1639-1650.
    • (1991) J Cell Biol , vol.115 , pp. 1639-1650
    • Gill, S.R.1    Schroer, T.A.2    Szilak, I.3    Steuer, E.R.4    Sheetz, M.P.5
  • 19
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterisation of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organisation during mitosis
    • Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB: Molecular characterisation of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organisation during mitosis. J Cell Biol 1996, 132:617-633.
    • (1996) J Cell Biol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 20
    • 0032622374 scopus 로고    scopus 로고
    • Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellular processes
    • Edited by CL Rieder. San Diego: Academic Press
    • Wittmann T, Hyman T: Recombinant p50/dynamitin as a tool to examine the role of dynactin in intracellular processes. In Mitosis and Meiosis. Edited by CL Rieder. San Diego: Academic Press; 1999:137-143.
    • (1999) Mitosis and Meiosis , pp. 137-143
    • Wittmann, T.1    Hyman, T.2
  • 21
    • 0032563618 scopus 로고    scopus 로고
    • Characterizaton of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells
    • Karki S, LaMonte B, Holzbaur ELF: Characterizaton of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells. J Cell Biol 1998, 142:1023-1034.
    • (1998) J Cell Biol , vol.142 , pp. 1023-1034
    • Karki, S.1    LaMonte, B.2    Holzbaur, E.L.F.3
  • 22
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt J, Echeverri C, Nilsson T, Vallee R: Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein- dependent maintenance of membrane organelle distribution. J Cell Biol 1997, 139:469-484.
    • (1997) J Cell Biol , vol.139 , pp. 469-484
    • Burkhardt, J.1    Echeverri, C.2    Nilsson, T.3    Vallee, R.4
  • 24
    • 0032489870 scopus 로고    scopus 로고
    • Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein
    • Harada A, Takei Y, Kanai Y, Tanaka Y, Nonaka S, Hirokawa N: Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J Cell Biol 1998, 141:51-59.
    • (1998) J Cell Biol , vol.141 , pp. 51-59
    • Harada, A.1    Takei, Y.2    Kanai, Y.3    Tanaka, Y.4    Nonaka, S.5    Hirokawa, N.6
  • 25
    • 0026534466 scopus 로고
    • Actin-dependent organelle movement in squid axoplasm
    • Kuznetsov SA, Langford GM, Weiss DG: Actin-dependent organelle movement in squid axoplasm. Nature 1992, 356:722-725.
    • (1992) Nature , vol.356 , pp. 722-725
    • Kuznetsov, S.A.1    Langford, G.M.2    Weiss, D.G.3
  • 27
    • 0025086823 scopus 로고
    • Regulation of organelle transport in melanophores by calcineurin
    • Thaler CD, Haimo LT: Regulation of organelle transport in melanophores by calcineurin. J Cell Biol 1990, 111:1939-1948.
    • (1990) J Cell Biol , vol.111 , pp. 1939-1948
    • Thaler, C.D.1    Haimo, L.T.2
  • 28
    • 0031875170 scopus 로고    scopus 로고
    • Regulation of organelle movement in melanophores by protein kinase A (PKA), protein kinase C (PKC) and protein phosphatase 2A (PP2A)
    • Reilen AR, Tint IS, Peunova NI, Enikolopov GN, Gelfand VI: Regulation of organelle movement in melanophores by protein kinase A (PKA), protein kinase C (PKC) and protein phosphatase 2A (PP2A). J Cell Biol 1998, 142:803-813. Protein kinases A and C, along with protein phosphatase 2A are shown to regulate melanophore movement using a novel transfection approach.
    • (1998) J Cell Biol , vol.142 , pp. 803-813
    • Reilen, A.R.1    Tint, I.S.2    Peunova, N.I.3    Enikolopov, G.N.4    Gelfand, V.I.5
  • 29
    • 0032576766 scopus 로고    scopus 로고
    • Functional coordination of microtubule-based and actin-based motility in melanophores
    • Rodionov VI, Hope AJ, SvitkinaTM, Borisy GM: Functional coordination of microtubule-based and actin-based motility in melanophores. Curr Biol 1998, 8:165-168. Elegant report demonstrating that actin-based movement is absolutely required to obtain an even dispersal of pigment granules in fish melanophores: without actin, the granules translocate right to the cell periphery when stimulated to disperse.
    • (1998) Curr Biol , vol.8 , pp. 165-168
    • Rodionov, V.I.1    Hope, A.J.2    Svitkina, T.M.3    Borisy, G.M.4
  • 30
    • 0032576778 scopus 로고    scopus 로고
    • Myosin cooperates with microtubule motors during organelle transport in melanophores
    • Rogers SL, Gelfand VI: Myosin cooperates with microtubule motors during organelle transport in melanophores. Curr Biol 1998, 8:161-164. A classic study revealing that both actin- and microtubule-based motors are needed for proper melanosome movement, and that melanosomes possess myosin V by immunoblotting.
    • (1998) Curr Biol , vol.8 , pp. 161-164
    • Rogers, S.L.1    Gelfand, V.I.2
  • 31
    • 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: Visualization of melanosome dynamics within wild-type and dilute melanocytes suggests a paradigm for myosin V function in vivo. J Cell Biol 1998, 143:1899-1918. This paper shows that, although their function is rather different from fish and frog melanophores, mammalian melanocytes use the same combination of myosin V with microtubule motors in order to localize melanosomes to the periphery of the cell .
    • (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
  • 32
    • 0029955902 scopus 로고    scopus 로고
    • Cultured melanocytes from dilute mice exhibit dendritic morphology and altered melanosome distribution
    • Provance D, Wei M, Ipe V, Mercer J: Cultured melanocytes from dilute mice exhibit dendritic morphology and altered melanosome distribution. Proc Natl Acad Sci USA 1996, 93:14554-14558.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14554-14558
    • Provance, D.1    Wei, M.2    Ipe, V.3    Mercer, J.4
  • 33
    • 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 J III: Myosin V associates with melanosomes in mouse melanocytes: Evidence that myosin V is an organelle motor. J Cell Sci 1997, 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. III5
  • 35
    • 0030861056 scopus 로고    scopus 로고
    • Dimerization of the highly conserved light chain shared by dynein and myosin V
    • Benashski SE, Harrison A, Patel-King R, King SM: Dimerization of the highly conserved light chain shared by dynein and myosin V. J Biol Chem 1997, 272:20929-20935.
    • (1997) J Biol Chem , vol.272 , pp. 20929-20935
    • Benashski, S.E.1    Harrison, A.2    Patel-King, R.3    King, S.M.4
  • 36
    • 0031149266 scopus 로고    scopus 로고
    • Myosin V - The multi-purpose transport motor
    • Titus M: Myosin V - The multi-purpose transport motor. Curr Biol 1997, 7:R301-R304.
    • (1997) Curr Biol , vol.7
    • Titus, M.1
  • 37
    • 0029081168 scopus 로고
    • Melanosomes are specialized members of the lysosomal lineage of organelles
    • Orlow SJ: Melanosomes are specialized members of the lysosomal lineage of organelles. J Invest Dermatol 1995, 105:3-7.
    • (1995) J Invest Dermatol , vol.105 , pp. 3-7
    • Orlow, S.J.1
  • 38
    • 0027457958 scopus 로고
    • Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro
    • Burkhardt JK, McIlvain JM, Sheetz MP, Argon Y: Lytic granules from cytotoxic T cells exhibit kinesin-dependent motility on microtubules in vitro. J Cell Sci 1993, 104:151-162.
    • (1993) J Cell Sci , vol.104 , pp. 151-162
    • Burkhardt, J.K.1    McIlvain, J.M.2    Sheetz, M.P.3    Argon, Y.4
  • 42
    • 0033052099 scopus 로고    scopus 로고
    • Microtubule-based endoplasmic reticulum motility in Xenopus laevis: Activation of membrane-associated kinesin during development
    • Lane JD, Allan VJ: Microtubule-based endoplasmic reticulum motility in Xenopus laevis: Activation of membrane-associated kinesin during development. Mol Biol Cell 1999, 10:1909-1922.
    • (1999) Mol Biol Cell , vol.10 , pp. 1909-1922
    • Lane, J.D.1    Allan, V.J.2
  • 43
    • 0028019867 scopus 로고
    • Kinesin-mediated organelle translocation revealed by specific cellular manipulations
    • Feiguin F, Ferreira A, Kosik KS, Caceres A: Kinesin-mediated organelle translocation revealed by specific cellular manipulations. J Cell Biol 1994, 127:1021-1039.
    • (1994) J Cell Biol , vol.127 , pp. 1021-1039
    • Feiguin, F.1    Ferreira, A.2    Kosik, K.S.3    Caceres, A.4
  • 44
    • 0028943648 scopus 로고
    • Protein phosphatase 1 regulates the cytoplasmic dynein-driven formation of endoplasmic reticulum networks in vitro
    • Allan V: Protein phosphatase 1 regulates the cytoplasmic dynein- Driven formation of endoplasmic reticulum networks in vitro. J Cell Biol 1995, 128:879-891.
    • (1995) J Cell Biol , vol.128 , pp. 879-891
    • Allan, V.1
  • 45
    • 0031926806 scopus 로고    scopus 로고
    • Disassembly of actin filaments leads to increased rate and frequency of mitochondrial movement along microtubules
    • Krendel M, Sgourdas G, Bonder EM: Disassembly of actin filaments leads to increased rate and frequency of mitochondrial movement along microtubules. Cell Motil Cytoskeleton 1998, 40:368-378.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 368-378
    • Krendel, M.1    Sgourdas, G.2    Bonder, E.M.3
  • 46
    • 0028861992 scopus 로고
    • Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons
    • Morris RL, Hollenbeck PJ: Axonal transport of mitochondria along microtubules and F-actin in living vertebrate neurons. J Cell Biol 1995, 131:1315-1326.
    • (1995) J Cell Biol , vol.131 , pp. 1315-1326
    • Morris, R.L.1    Hollenbeck, P.J.2
  • 47
    • 0032476645 scopus 로고    scopus 로고
    • Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease
    • Ebneth A, Godemann R, Stamer K, Illenberger S, Trnczek B, Mandelkow E-M, Mandelkow E: Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer's disease. J Cell Biol 1998, 143:777-794. Overexpression of the microtubule-associated protein, tau, is seen to impair outward translocation of membranes preferentially. These results prompt speculation on how the kinesin and dynein motors might differ with respect to their interactions with microtubules.
    • (1998) J Cell Biol , vol.143 , pp. 777-794
    • Ebneth, A.1    Godemann, R.2    Stamer, K.3    Illenberger, S.4    Trnczek, B.5    Mandelkow, E.-M.6    Mandelkow, E.7
  • 48
    • 0032568790 scopus 로고    scopus 로고
    • Targeted disruption of mouse conventional kinesin heavy chain, Kif5B, results in abnormal perinuclear clustering of mitochondria
    • Tanaka Y, Kanai Y, Okada Y, Nonaka S, Takeda S, Harada A, Hirokawa N: Targeted disruption of mouse conventional kinesin heavy chain, Kif5B, results in abnormal perinuclear clustering of mitochondria. Cell 1998, 93:1147-1158.
    • (1998) Cell , vol.93 , pp. 1147-1158
    • Tanaka, Y.1    Kanai, Y.2    Okada, Y.3    Nonaka, S.4    Takeda, S.5    Harada, A.6    Hirokawa, N.7
  • 49
    • 0029074236 scopus 로고
    • Fast axonal transport of kinesin in the rat visual system: Functionality of kinesin heavy chain isoforms
    • Elluru RG, Bloom GS, Brady ST: Fast axonal transport of kinesin in the rat visual system: Functionality of kinesin heavy chain isoforms. Mol Biol Cell 1995, 6:21-40.
    • (1995) Mol Biol Cell , vol.6 , pp. 21-40
    • Elluru, R.G.1    Bloom, G.S.2    Brady, S.T.3
  • 50
    • 0000348259 scopus 로고    scopus 로고
    • Role of motor proteins in organizing the endoplasmic reticulum and Golgi apparatus
    • Allan V: Role of motor proteins in organizing the endoplasmic reticulum and Golgi apparatus. Semin Cell Dev Biol 1996, 7:335-342.
    • (1996) Semin Cell Dev Biol , vol.7 , pp. 335-342
    • Allan, V.1
  • 51
    • 0029550559 scopus 로고
    • Actomyosin-based motility of endoplasmic reticulum and chloroplasts in vallisneria mesophyll cells
    • Liebe S, Menzel D: Actomyosin-based motility of endoplasmic reticulum and chloroplasts in vallisneria mesophyll cells. Biol Cell 1995, 85:207-222.
    • (1995) Biol Cell , vol.85 , pp. 207-222
    • Liebe, S.1    Menzel, D.2
  • 52
    • 0030727892 scopus 로고    scopus 로고
    • Actinomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling
    • Waterman-Storer C, Salmon E: Actinomyosin-based retrograde flow of microtubules in the lamella of migrating epithelial cells influences microtubule dynamic instability and turnover and is associated with microtubule breakage and treadmilling. J Cell Biol 1997, 139:417-434.
    • (1997) J Cell Biol , vol.139 , pp. 417-434
    • Waterman-Storer, C.1    Salmon, E.2
  • 53
    • 0032474825 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms
    • Waterman-Storer CM, Salmon ED: Endoplasmic reticulum membrane tubules are distributed by microtubules in living cells using three distinct mechanisms. Curr Biol 1998, 8:798-806. Microtubule dynamics and ER tubule extension is visualized in living cells, showing that ER tubules extend either by translocation along microtubules or by attachment to growing microtubule ends.
    • (1998) Curr Biol , vol.8 , pp. 798-806
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 55
    • 0030928782 scopus 로고    scopus 로고
    • Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
    • Scales S, Pepperkok R, Kreis T: Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. Cell 1997, 90:1137-1148.
    • (1997) Cell , vol.90 , pp. 1137-1148
    • Scales, S.1    Pepperkok, R.2    Kreis, T.3
  • 56
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole NB, Sciaky N, Marotta A, Song J, Lippincott-Schwartz J: Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol Biol Cell 1996, 7:631-650.
    • (1996) Mol Biol Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 57
    • 0032517823 scopus 로고    scopus 로고
    • Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole-induced Golgi scattering
    • Storrie B, White J, Röttger S, Stelzer EHK, Suganuma T, Nilsson T: Recycling of Golgi-resident glycosyltransferases through the ER reveals a novel pathway and provides an explanation for nocodazole- Induced Golgi scattering. J Cell Biol 1998, 143:1505-1521.
    • (1998) J Cell Biol , vol.143 , pp. 1505-1521
    • Storrie, B.1    White, J.2    Röttger, S.3    Stelzer, E.H.K.4    Suganuma, T.5    Nilsson, T.6
  • 58
    • 0032584612 scopus 로고    scopus 로고
    • Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity
    • Tai AW, Chuang J-Z, Sung C-H: Localization of Tctex-1, a cytoplasmic dynein light chain, to the Golgi apparatus and evidence for dynein complex heterogeneity. J Biol Chem 1998, 273:19639-19649.
    • (1998) J Biol Chem , vol.273 , pp. 19639-19649
    • Tai, A.W.1    Chuang, J.-Z.2    Sung, C.-H.3
  • 59
    • 0033000412 scopus 로고    scopus 로고
    • Coalescence of Golgi fragments in microtubule-deprived living cells
    • Polishchuk RS, Polishchuk EV, Mironov AA: Coalescence of Golgi fragments in microtubule-deprived living cells. Eur J Cell Biol 1999, 78:170-185.
    • (1999) Eur J Cell Biol , vol.78 , pp. 170-185
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Mironov, A.A.3
  • 60
    • 0010524385 scopus 로고    scopus 로고
    • Dispersal of Golgi apparatus in nocodazole-treated fibroblasts is a kinesin-driven process
    • Minin A: Dispersal of Golgi apparatus in nocodazole-treated fibroblasts is a kinesin-driven process. J Cell Sci 1997, 110:2495-2505.
    • (1997) J Cell Sci , vol.110 , pp. 2495-2505
    • Minin, A.1
  • 61
    • 0028026746 scopus 로고
    • Molecular motors are differentially distributed on Golgi membranes from polarised epithelial cells
    • Fath KR, Trimbur GM, Burgess DR: Molecular motors are differentially distributed on Golgi membranes from polarised epithelial cells. J Cell Biol 1994, 126:661-675.
    • (1994) J Cell Biol , vol.126 , pp. 661-675
    • Fath, K.R.1    Trimbur, G.M.2    Burgess, D.R.3
  • 62
    • 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: 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 1998, 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
  • 64
    • 0031781229 scopus 로고    scopus 로고
    • An ordered inheritance strategy for the Golgi apparatus: Visualization of mitotic disassembly reveals a role for the mitotic spindle
    • Shima DT, Cabrera-Poch N, Pepperkok R, Warren G: An ordered inheritance strategy for the Golgi apparatus: Visualization of mitotic disassembly reveals a role for the mitotic spindle. J Cell Biol 1998, 141:955-966.
    • (1998) J Cell Biol , vol.141 , pp. 955-966
    • Shima, D.T.1    Cabrera-Poch, N.2    Pepperkok, R.3    Warren, G.4
  • 67
    • 0031664962 scopus 로고    scopus 로고
    • Vitro reconstitution of microtubule plus end-directed, GTPγS-sensitive motility of Golgi membranes
    • Fullerton AT, Bau M-Y, Conrad PA, Bloom GS: In Vitro reconstitution of microtubule plus end-directed, GTPγS-sensitive motility of Golgi membranes. Mol Biol Cell 1998, 9:2699-2714.
    • (1998) Mol Biol Cell , vol.9 , pp. 2699-2714
    • Fullerton, A.T.1    Bau, M.-Y.2    Conrad, P.A.3    Bloom, G.S.4
  • 70
    • 0029911077 scopus 로고    scopus 로고
    • SWAP, an Smg GDS-associated protein having arm repeats and phosphorylated by src tyrosine kinase
    • Shimizu K, Kawabe H, Minami S, Honda T, Takaishi K, Shirataki H, Takai Y: SWAP, an Smg GDS-associated protein having arm repeats and phosphorylated by src tyrosine kinase. J Biol Chem 1996, 271:27013-27017.
    • (1996) J Biol Chem , vol.271 , pp. 27013-27017
    • Shimizu, K.1    Kawabe, H.2    Minami, S.3    Honda, T.4    Takaishi, K.5    Shirataki, H.6    Takai, Y.7
  • 71
    • 0028579468 scopus 로고
    • Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli
    • Huang TG, Suhan J, Hackney DD: Drosophila kinesin motor domain extending to amino acid position 392 is dimeric when expressed in Escherichia coli. J Biol Chem 1994, 269:32708.
    • (1994) J Biol Chem , vol.269 , pp. 32708
    • Huang, T.G.1    Suhan, J.2    Hackney, D.D.3
  • 72
    • 0029954709 scopus 로고    scopus 로고
    • Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport
    • Niclas J, Allan VJ, Vale RD: Cell cycle regulation of dynein association with membranes modulates microtubule-based organelle transport. J Cell Biol 1996, 133:585-593.
    • (1996) J Cell Biol , vol.133 , pp. 585-593
    • Niclas, J.1    Allan, V.J.2    Vale, R.D.3
  • 73
    • 0033582659 scopus 로고    scopus 로고
    • CLIP-170 highlights growing microtubule ends in vivo
    • Perez F, Diamantopoulos GS, Stadier R, Kreis TE: CLIP-170 highlights growing microtubule ends in vivo. Cell 1999, 96:517-527. A spectacular study that illustrates the dynamic behavior of CLIP-170 in living cells.
    • (1999) Cell , vol.96 , pp. 517-527
    • Perez, F.1    Diamantopoulos, G.S.2    Stadier, R.3    Kreis, T.E.4
  • 74
    • 0032559641 scopus 로고    scopus 로고
    • A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos
    • Lantz VA, Miller KG: A class VI unconventional myosin is associated with a homologue of a microtubule-binding protein, cytoplasmic linker protein-170, in neurons and at the posterior pole of Drosophila embryos. J Cell Biol 1998, 140:897-910. Drosophila myosin VI (95F myosin) is shown to interact in vitro with a CLIP-170 homologue. The work provides food for thought regarding interactions between actin- and microtubule-based motility systems.
    • (1998) J Cell Biol , vol.140 , pp. 897-910
    • Lantz, V.A.1    Miller, K.G.2
  • 75
    • 0033051741 scopus 로고    scopus 로고
    • Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends
    • Vaughan KT, Tynan SH, Faulkner NE, Echeverri CJ, Vallee RB: Colocalization of cytoplasmic dynein with dynactin and CLIP-170 at microtubule distal ends. J Cell Sci 1999, 112:1437-1447. The authors of this paper describe the unexpected finding that the dynein activator, dynactin, and CLIP-170 bind together to microtubule plus ends. The apparent interaction between these proteins might provide a means of bringing dynein to membranous cargoes located in the cell periphery.
    • (1999) J Cell Sci , vol.112 , pp. 1437-1447
    • Vaughan, K.T.1    Tynan, S.H.2    Faulkner, N.E.3    Echeverri, C.J.4    Vallee, R.B.5
  • 77
    • 0030884680 scopus 로고    scopus 로고
    • Phosphotransferases associated with the regulation of kinesin motor activity
    • Lindesmith L, McIlvain JM, Argon Y, Sheetz MP: Phosphotransferases associated with the regulation of kinesin motor activity. J Biol Chem 1997, 272:22929-22933.
    • (1997) J Biol Chem , vol.272 , pp. 22929-22933
    • Lindesmith, L.1    McIlvain, J.M.2    Argon, Y.3    Sheetz, M.P.4
  • 79
    • 0031469160 scopus 로고    scopus 로고
    • Overexpression of MAP4 inhibits organelle motility and trafficking in vivo
    • Bulinski JC, McGraw TE, Gruber D, Nguyen HL, Sheetz MP: Overexpression of MAP4 inhibits organelle motility and trafficking in vivo. J Cell Sci 1997, 110:3055-3064.
    • (1997) J Cell Sci , vol.110 , pp. 3055-3064
    • Bulinski, J.C.1    McGraw, T.E.2    Gruber, D.3    Nguyen, H.L.4    Sheetz, M.P.5
  • 80
    • 0030813618 scopus 로고    scopus 로고
    • Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins
    • Ulitzur N, Rancano C, Pfeffer SR: Biochemical characterization of mapmodulin, a protein that binds microtubule-associated proteins. J Biol Chem 1997, 272:30577-30582.
    • (1997) J Biol Chem , vol.272 , pp. 30577-30582
    • Ulitzur, N.1    Rancano, C.2    Pfeffer, S.R.3
  • 81
    • 0028999047 scopus 로고
    • A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain
    • Lopez LA, Sheetz MP: A microtubule-associated protein (MAP2) kinase restores microtubule motility in embryonic brain. J Biol Chem 1995, 270:12511-12517.
    • (1995) J Biol Chem , vol.270 , pp. 12511-12517
    • Lopez, L.A.1    Sheetz, M.P.2
  • 82
    • 0033526005 scopus 로고    scopus 로고
    • GMAP 210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein
    • Infante C, Ramos Morales F, Fedriani C, Bornens M, Rios RM: GMAP 210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J Cell Biol 1999, 145:83-98. The Golgi-associated protein described in this study might stabilize interactions between this organelle and the microtubule cytoskeleton. GMAP-210 might be one of a growing number of proteins in the 'static linker' class of microtubule binding proteins.
    • (1999) J Cell Biol , vol.145 , pp. 83-98
    • Infante, C.1    Ramos Morales, F.2    Fedriani, C.3    Bornens, M.4    Rios, R.M.5
  • 83
    • 0032584725 scopus 로고    scopus 로고
    • 58k, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase
    • Bashour AM, Bloom GS: 58k, a microtubule-binding Golgi protein, is a formiminotransferase cyclodeaminase. J Biol Chem 1998, 273:19612-19617.
    • (1998) J Biol Chem , vol.273 , pp. 19612-19617
    • Bashour, A.M.1    Bloom, G.S.2
  • 84
    • 0032476663 scopus 로고    scopus 로고
    • A novel direct interaction of endoplasmic reticulum with microtubules
    • Klopfenstein DRC, Kappeler F, Hauri H-P: A novel direct interaction of endoplasmic reticulum with microtubules. EMBO J 1998, 17:6168-6177.
    • (1998) EMBO J , vol.17 , pp. 6168-6177
    • Klopfenstein, D.R.C.1    Kappeler, F.2    Hauri, H.-P.3
  • 85
    • 0032584740 scopus 로고    scopus 로고
    • A formiminotrasferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules
    • Hennig D, Scales SJ, Moreau A, Murley LL, De Mey J, Kreis TE: A formiminotrasferase cyclodeaminase isoform is localized to the Golgi complex and can mediate interaction of trans-Golgi network-derived vesicles with microtubules. J Biol Chem 1998, 273:19602-19611.
    • (1998) J Biol Chem , vol.273 , pp. 19602-19611
    • Hennig, D.1    Scales, S.J.2    Moreau, A.3    Murley, L.L.4    De Mey, J.5    Kreis, T.E.6


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