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of outstanding interest. This study analyzes the process whereby Golgi membranes 'fragment' during microtubule depolymerization by nocodazole. Using a variety of techniques the authors show that Golgi fragmentation arises from a show but constitutive flux of Golgi resident proteins through the bidirectional membrane pathways connecting the ER and Golgi complex. Since transport of recycling intermediates to the ER is unaffected by microtubule disruption, whereas translocation of pre-Golgi structures into the centrosomal region is blocked, when microtubules are disrupted, Golgi enzymes accumulate at ER exit sites over time.
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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. of outstanding interest Mol Biol Cell. 7:1996;631-650 This study analyzes the process whereby Golgi membranes 'fragment' during microtubule depolymerization by nocodazole. Using a variety of techniques the authors show that Golgi fragmentation arises from a show but constitutive flux of Golgi resident proteins through the bidirectional membrane pathways connecting the ER and Golgi complex. Since transport of recycling intermediates to the ER is unaffected by microtubule disruption, whereas translocation of pre-Golgi structures into the centrosomal region is blocked, when microtubules are disrupted, Golgi enzymes accumulate at ER exit sites over time.
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Cole, N.B.1
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Saraste J, Kuismanen E. Pathways of protein sorting and membrane traffic between the rough endoplasmic reticulum and the Goldi complex. Semin Cell Biol. 3:1992;343-355.
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Saraste, J.1
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of outstanding interest. The viral glycoprotein ts045 VSVG tagged with green fluorescent protein (VSVG-GFP) was used to study ER-to-Golgi traffic in living cells. When visualized at the permissive temperatures, upon export from the ER, VSVG-GFP became concentrated in many differently shaped pre-Golgi structures, which then translocated inwards, along mictoubules, toward the Golgi complex. The motor complex of dynein/dynactin was required for this movement. Because pre-Golgi structures are large tubulovesicular masses rather than individual vesicles, these results focus attention on the role of such structures in Golgi biogensis and trafficking. The study reported the first visualization of ER to Golgi traffic in real time.
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Presley JF, Cole NB, Schroer TA, Lippincott-Schwartz J. ER-to-Golgi transport visualized in living cells. of outstanding interest Nature. 389:1997;81-85 The viral glycoprotein ts045 VSVG tagged with green fluorescent protein (VSVG-GFP) was used to study ER-to-Golgi traffic in living cells. When visualized at the permissive temperatures, upon export from the ER, VSVG-GFP became concentrated in many differently shaped pre-Golgi structures, which then translocated inwards, along mictoubules, toward the Golgi complex. The motor complex of dynein/dynactin was required for this movement. Because pre-Golgi structures are large tubulovesicular masses rather than individual vesicles, these results focus attention on the role of such structures in Golgi biogensis and trafficking. The study reported the first visualization of ER to Golgi traffic in real time.
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Nature
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Presley, J.F.1
Cole, N.B.2
Schroer, T.A.3
Lippincott-Schwartz, J.4
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13
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0030928782
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Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI
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of outstanding interest. This study characterized ER-to-Golgi traffic, again using VSVG-GFP, and addressed the potential roles of COP1 and COPII. Both of these peripheral proteins were associated with pre-Golgi structures at the time of their formation. Only COPI, however, remained associated once the structures started to translocate inward along microtubules toward the Golgi complex.
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Scales SJ, Pepperkok R, Kreis TE. Visualization of ER-to-Golgi transport in living cells reveals a sequential mode of action for COPII and COPI. of outstanding interest Cell. 90:1997;1137-1148 This study characterized ER-to-Golgi traffic, again using VSVG-GFP, and addressed the potential roles of COP1 and COPII. Both of these peripheral proteins were associated with pre-Golgi structures at the time of their formation. Only COPI, however, remained associated once the structures started to translocate inward along microtubules toward the Golgi complex.
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Cell
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Scales, S.J.1
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Bannykh SI, Balch WE. Membrane dynamics at the endoplasmic reticulum-Golgi interface. J Cell Biol. 138:1997;1-4.
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Saraste J, Svensson K. Distribution of the intermediate elements operating in ER to Golgi transport. J Cell Sci. 100:1991;415-430.
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Holzbaur ELF, Vallee RB. Dyneins: molecular structure and cellular function. Annu Rev Cell Biol. 10:1994;339-372.
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Schroer TA. Structure and function of dynactin. Semin Cell Develop Biol. 7:1996;321-328.
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Schafer DA, Gill SR, Cooper JA, Heuser JE, Schroer TA. Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J Cell Biol. 126:1994;403-412.
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Schafer, D.A.1
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21
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Vaughan KT, Vallee RB. Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J Cell Biol. 131:1995;1507-1516.
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22
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The p150glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp1)
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Waterman-Storer CM, Karki S, Holzbauer EL. The p150glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp1). Proc Natl Acad Sci USA. 92:1995;1634-1638.
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Waterman-Storer, C.M.1
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23
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0029913484
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Molecular characterization of the 50-kD subunit of dynacting reveals function for the complex in chromosome alignment and spindle organization during mitosis
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of special interest. This article reports characterization of the 50kDa subunit of dynactin in mitotic cells by overexpression of this protein. The authors found that in these cells mitosis was disrupted, with cells accumulating in prometaphase. Chromosomes were condensed but unlighted, spindles were distorted, and dynactin was dissociated from kinetochores. The data provide evidence for a role of dynactin chromosome alignment and spindle organization.
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Echeverri CJ, Paschal BM, Vaughan KT, Vallee RB. Molecular characterization of the 50-kD subunit of dynacting reveals function for the complex in chromosome alignment and spindle organization during mitosis. of special interest J Cell Biol. 132:1996;617-633 This article reports characterization of the 50kDa subunit of dynactin in mitotic cells by overexpression of this protein. The authors found that in these cells mitosis was disrupted, with cells accumulating in prometaphase. Chromosomes were condensed but unlighted, spindles were distorted, and dynactin was dissociated from kinetochores. The data provide evidence for a role of dynactin chromosome alignment and spindle organization.
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J Cell Biol
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Echeverri, C.J.1
Paschal, B.M.2
Vaughan, K.T.3
Vallee, R.B.4
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24
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Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin
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Paschal BM, Holzbaur EL, Pfister KK, Clark S, Meyer DI, Vallee RB. Characterization of a 50-kDa polypeptide in cytoplasmic dynein preparations reveals a complex with p150GLUED and a novel actin. J Biol Chem. 268:1993;15318-15323.
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Paschal, B.M.1
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Pfister, K.K.3
Clark, S.4
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Vallee, R.B.6
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25
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0030727535
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Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
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of outstanding interest. This paper describes the phenotype observed following overexpression of p50/dynamitin in interphase cells. Early/late endosomes and lysosomes were resitributed to the cell periphery under these conditions and the distribution of Golgi membranes was also affected. Golgi proteins redistributed into scattered structures containing ERGIC53, a marker for the intermediate compartment. The data suggest that dynactin is required for ongoing microtubule minus-end-directed membrane movement within cells.
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Burkhardt JK, Echeverri CJ, Nilsson T, Vallee RB. Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. of outstanding interest J Cell Biol. 139:1997;469-484 This paper describes the phenotype observed following overexpression of p50/dynamitin in interphase cells. Early/late endosomes and lysosomes were resitributed to the cell periphery under these conditions and the distribution of Golgi membranes was also affected. Golgi proteins redistributed into scattered structures containing ERGIC53, a marker for the intermediate compartment. The data suggest that dynactin is required for ongoing microtubule minus-end-directed membrane movement within cells.
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(1997)
J Cell Biol
, vol.139
, pp. 469-484
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Burkhardt, J.K.1
Echeverri, C.J.2
Nilsson, T.3
Vallee, R.B.4
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26
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0029905303
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Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles
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of outstanding interest. This article describes studies of the subcellular localization of two dynein-heavy-chain-like proteins (DHC2 and DHC3). DHC2 was localized predominantly to the Golgi complex, whereas DHC3 was associated with membrane structures of unknown identity. Antibodies to DHC2 (but not DHC3), when microinjected into cells, caused the Golgi complex to fragment. These results suggest that specific cytoplasmic dyneins have different functions in intracellular membrane trafficing.
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Vaisberg EA, Grissom PM, McIntosh JR. Mammalian cells express three distinct dynein heavy chains that are localized to different cytoplasmic organelles. of outstanding interest J Cell Biol. 133:1996;831-842 This article describes studies of the subcellular localization of two dynein-heavy-chain-like proteins (DHC2 and DHC3). DHC2 was localized predominantly to the Golgi complex, whereas DHC3 was associated with membrane structures of unknown identity. Antibodies to DHC2 (but not DHC3), when microinjected into cells, caused the Golgi complex to fragment. These results suggest that specific cytoplasmic dyneins have different functions in intracellular membrane trafficing.
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(1996)
J Cell Biol
, vol.133
, pp. 831-842
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Vaisberg, E.A.1
Grissom, P.M.2
McIntosh, J.R.3
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27
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0030923518
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+-ATPase transport from ER to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in MDCK cells
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of outstanding interest. The authors provide data suggesting Golgi spectrin/ankyrin on pre-Golgi and Golgi membranes forms a docking complex to sequester specific membrane proteins and to crosslink vesicles to microtubule motor protein complexes.
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+-ATPase transport from ER to Golgi requires the Golgi spectrin-ankyrin G119 skeleton in MDCK cells. of outstanding interest Proc Natl Acad Sci USA. 94:1997;10711-10716 The authors provide data suggesting Golgi spectrin/ankyrin on pre-Golgi and Golgi membranes forms a docking complex to sequester specific membrane proteins and to crosslink vesicles to microtubule motor protein complexes.
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(1997)
Proc Natl Acad Sci USA
, vol.94
, pp. 10711-10716
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Devarajan, P.1
Stabach, P.R.2
De Matteis, M.A.3
Morrow, J.S.4
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28
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0029905387
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The spectrin-based membrane skeleton as a membrane protein sorting machine
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of special interest. Speculates on the role of Golgi-spectrin matrix as a protein-sorting machine within the Golgi complex.
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Beck K, Nelson W. The spectrin-based membrane skeleton as a membrane protein sorting machine. of special interest Am J Physiol. 270:1996;C1263-C1270 Speculates on the role of Golgi-spectrin matrix as a protein-sorting machine within the Golgi complex.
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Am J Physiol
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Beck, K.1
Nelson, W.2
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The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane
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Bennett V, Gilligan DM. The spectrin-based membrane skeleton and micron-scale organization of the plasma membrane. Annu Rev Cell Biol. 9:1993;27-66.
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Bennett, V.1
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31
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Polarized assembly of spectrin and ankyrin in epithelial cells
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M.S. Mooseker, Morrow J.S. New York: Academic Press
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Morrow JS, Cianci CD, Kennedy SP, Warren SL. Polarized assembly of spectrin and ankyrin in epithelial cells. Mooseker MS, Morrow JS. Ordering the Membrane Cytoskeleton Trilayer. 1991;227-244 Academic Press, New York.
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Ordering the Membrane Cytoskeleton Trilayer
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Morrow, J.S.1
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Of membrane stability and mosaics: The spectrin cytoskeleton
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J. Hollman, Jamieson J. London: Oxford Press. in press
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Morrow JS, Cianci CD, Kennedy SP, Cianci CD, Sinard JH, Weed SA. Of membrane stability and mosaics: the spectrin cytoskeleton. Hollman J, Jamieson J. Handbook of Physiology. 1996;Oxford Press, London. in press.
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Handbook of Physiology
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Morrow, J.S.1
Cianci, C.D.2
Kennedy, S.P.3
Cianci, C.D.4
Sinard, J.H.5
Weed, S.A.6
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33
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0027993053
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Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex
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Beck KA, Buchanan JA, Malhotra V, Nelson WJ. Golgi spectrin: identification of an erythroid beta-spectrin homolog associated with the Golgi complex. J Cell Biol. 127:1994;707-723.
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Beck, K.A.1
Buchanan, J.A.2
Malhotra, V.3
Nelson, W.J.4
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34
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0029898290
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G119) in the kidney and muscle that binds BIE* spectrin and associates with the Golgi apparatus
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G119 and spectrin form a Golgi-associated membrane skeleton that promotes orgnization of protein microdomains and sorting within the Golgi complex.
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G119 and spectrin form a Golgi-associated membrane skeleton that promotes orgnization of protein microdomains and sorting within the Golgi complex.
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Devarajan, P.1
Stabach, P.2
Mann, A.3
Ardito, T.4
Kashgarian, M.5
Morrow, J.6
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35
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0030918480
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Golgi membrane skeleton: Identification, localization and oligomerization of a 195kDa ankyrin isoform associated with the Golgi complex
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of outstanding interest. The authors report that antibodies to a 195kDa ankyrin isotype localized to the Golgi complex. This protein associated with Golgi β-spectrin in detergent lysates and in cultured cells that were extracted with Triton X100 it was associated with spectrin in a 'Golgi ghost'. This suggested that ankyrin and spectrin form a Golgi-localized cytoskeleton. Golgi ankyrin dissociated from Golgi membranes with BFA and during mitosis with similar kinetics to spectrin and βCOP, indicating its association with the Golgi complex is dynamic and regulated.
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Beck KA, Buchanan JA, Nelson WJ. Golgi membrane skeleton: identification, localization and oligomerization of a 195kDa ankyrin isoform associated with the Golgi complex. of outstanding interest J Cell Sci. 110:1997;1239-1249 The authors report that antibodies to a 195kDa ankyrin isotype localized to the Golgi complex. This protein associated with Golgi β-spectrin in detergent lysates and in cultured cells that were extracted with Triton X100 it was associated with spectrin in a 'Golgi ghost'. This suggested that ankyrin and spectrin form a Golgi-localized cytoskeleton. Golgi ankyrin dissociated from Golgi membranes with BFA and during mitosis with similar kinetics to spectrin and βCOP, indicating its association with the Golgi complex is dynamic and regulated.
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J Cell Sci
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Beck, K.A.1
Buchanan, J.A.2
Nelson, W.J.3
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36
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0030479303
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Centractin (Arp1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles
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of outstanding interest. The authors show that in cells overexpressing ARP1 (a component of the dynactin complex), long actin-like filamants form in the cytoplasm. Golgi membrane proteins and spectrin co-localized on these filaments. Based on these results the authors suggest that dynactin associates with Golgi membranes through an interaction between ARP1 on dynactin and a spectrin-linked cytoskeletal network.
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Holleran E, Tokito M, Karki S, Holzbaur E. Centractin (Arp1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. of outstanding interest J Cell Biol. 135:1996;1815-1829 The authors show that in cells overexpressing ARP1 (a component of the dynactin complex), long actin-like filamants form in the cytoplasm. Golgi membrane proteins and spectrin co-localized on these filaments. Based on these results the authors suggest that dynactin associates with Golgi membranes through an interaction between ARP1 on dynactin and a spectrin-linked cytoskeletal network.
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J Cell Biol
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Holleran, E.1
Tokito, M.2
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The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport
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Waterman-Storer CM, Karki SB, Kuznetsov SA, Tabb JS, Weiss DG, Langford GM, Holzbaur ELF. The interaction between cytoplasmic dynein and dynactin is required for fast axonal transport. Proc Natl Acad Sci USA. 94:1997;12180-12185.
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Waterman-Storer, C.M.1
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Chen Y-G, Siddhanta A, Austin CD, Hammond SM, Sung T-C, Frohman MA, Morris AJ, Shield D. Phospholipase D stimulates release of nascent secretory vesicles from the trans-Golgi network. J Cell Biol. 138:1997;495-504.
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Chen Y-G1
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Pelham HR. Recycling of proteins between the endoplasmic reticulum and Golgi complex. Curr Opin Cell Biol. 3:1991;585-591.
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