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0030763228
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of special interest. Inner nuclear membrane dynamics were studied through the cell cycle. An integral membrane protein, lamin B receptor (LBR) was fused to green fluorescent protein (GFP) to make a fluorescent marker of the inner membrane which was followed by confocal time-lapse imaging. The LBR - GFP was localized to the endoplasmic reticulum, where it was found by photobleaching to be mobile, and to the nuclear envelope, where it was immobilized. At prometaphase, the nuclear envelope LBR - GFP was redistributed to the endoplasmic reticulum network, where it was now highly mobile. No vesiculation of LBR - GFP-containing membranes was seen at mitosis. The relocalization of LBR - GFP to the inner membrane after mitosis was shown to be via diffusion followed by immobilization.
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Ellenberg J, Siggia ED, Moreira JE, Smith CL, Presley JF, Worman HJ, Lippincott-Schwartz J. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. of special interest J Cell Biol. 138:1997;1193-1206 Inner nuclear membrane dynamics were studied through the cell cycle. An integral membrane protein, lamin B receptor (LBR) was fused to green fluorescent protein (GFP) to make a fluorescent marker of the inner membrane which was followed by confocal time-lapse imaging. The LBR - GFP was localized to the endoplasmic reticulum, where it was found by photobleaching to be mobile, and to the nuclear envelope, where it was immobilized. At prometaphase, the nuclear envelope LBR - GFP was redistributed to the endoplasmic reticulum network, where it was now highly mobile. No vesiculation of LBR - GFP-containing membranes was seen at mitosis. The relocalization of LBR - GFP to the inner membrane after mitosis was shown to be via diffusion followed by immobilization.
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J Cell Biol
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Ellenberg, J.1
Siggia, E.D.2
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Ris H. High-resolution field-emission scanning electron microscopy of nuclear pore complex. Scanning. 19:1997;368-375.
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Ris, H.1
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Macromolecular substructure in nuclear pore complexes by in-lens field-emission scanning electron microscopy
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Allen TD, Bennion GR, Rutherpord SA, Reipert S, Ramalho A, Kiseleva E, Goldberg MW. Macromolecular substructure in nuclear pore complexes by in-lens field-emission scanning electron microscopy. Scanning. 19:1997;403-410.
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Allen, T.D.1
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Kiseleva, E.6
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7
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0031056904
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Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: Evidence for structural intermediates in nuclear pore complex assembly
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of outstanding interest. FEISEM was used to examine early stages of nuclear assembly in Xenopus egg extracts, with the goal of observing pore complex intermediates. Several structures found only rarely on assembling nuclei were seen in greater abundance when agents that affect nuclear pore assembly were added to the assembly reaction (see text for further discussion).
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Goldberg MW, Wiese C, Allen TD, Wilson KL. Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. of outstanding interest J Cell Sci. 110:1997;409-420 FEISEM was used to examine early stages of nuclear assembly in Xenopus egg extracts, with the goal of observing pore complex intermediates. Several structures found only rarely on assembling nuclei were seen in greater abundance when agents that affect nuclear pore assembly were added to the assembly reaction (see text for further discussion).
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Goldberg, M.W.1
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0027287349
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Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
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Akey CW, Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J Cell Biol. 122:1993;1-19.
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Akey, C.W.1
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9
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0031604505
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Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
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of special interest. The yeast NPC is modeled using cryoelectron microscopy and image processing. Overall, the yeast NPC is smaller than the vertebrate NPC, but several key features of the vertebrate NPC are conserved: eightfold symmetry, the inner spoke ring, the transporter, and a transmembrane spoke domain. The most notable difference is the absence of the luminal spoke domain, which was not detected in yeast; thin cytoplasmic and nuclear thin rings also appear to be absent in yeast. The authors speculate that some peripheral structures of the vertebrate NPC, such as the cytoplasmic filaments and the nuclear basket, do exist in yeast though they were not visualized here. The implications of the similarities and differences between yeast and vertebrate NPCs are insightfully and extensively discussed.
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Yang O, Rout MP, Akey CW. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. of special interest Mol Cell. 1:1998;223-234 The yeast NPC is modeled using cryoelectron microscopy and image processing. Overall, the yeast NPC is smaller than the vertebrate NPC, but several key features of the vertebrate NPC are conserved: eightfold symmetry, the inner spoke ring, the transporter, and a transmembrane spoke domain. The most notable difference is the absence of the luminal spoke domain, which was not detected in yeast; thin cytoplasmic and nuclear thin rings also appear to be absent in yeast. The authors speculate that some peripheral structures of the vertebrate NPC, such as the cytoplasmic filaments and the nuclear basket, do exist in yeast though they were not visualized here. The implications of the similarities and differences between yeast and vertebrate NPCs are insightfully and extensively discussed.
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Mol Cell
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Yang, O.1
Rout, M.P.2
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10
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0029028753
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Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore complex
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Bustamante JO, Liepins A, Prendergast RA, Hanover JA, Oberleithner H. Patch clamp and atomic force microscopy demonstrate TATA-binding protein (TBP) interactions with the nuclear pore complex. J Membr Biol. 146:1995;263-272.
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Goldberg MW, Allen TD. Structural and functional organization of the nuclear envelope. Curr Opin Cell Biol. 7:1995;301-309.
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Moir RD, Spann TP, Goldman RD. The dynamic properties and possible functions of nuclear lamins. Int Rev Cytol. 162:1995;141-182.
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Foisner R. Dynamic organisation of intermediate filaments and associated proteins during the cell cycle. Bioessays. 19:1997;297-305.
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Foisner, R.1
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High resolution scanning electron microscopy of the nuclear envelope: Demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
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Goldberg MW, Allen TD. High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J Cell Biol. 119:1992;1429-1440.
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Pante N, Aebi U. Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol. 31:1996;153-199.
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Rout MP, Wente SR. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4:1994;357-365.
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Davis LI. The nuclear pore complex. Annu Rev Biochem. 64:1995;865-896.
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The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy
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of outstanding interest. of special interest. FEISEM images are presented here which provide a detailed description of the components of the NPC, confirming previous 3D reconstructions (see Goldberg, 1997 [7]). Dismantling of NPCs led to the identification of underlying structures such as the star-ring, which could also be seen as an assembly intermediate (see Allen, 1997 [6]).
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of outstanding interest Goldberg MW, Allen TD. The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. of special interest J Mol Biol. 257:1996;848-865 FEISEM images are presented here which provide a detailed description of the components of the NPC, confirming previous 3D reconstructions (see Goldberg, 1997 [7]). Dismantling of NPCs led to the identification of underlying structures such as the star-ring, which could also be seen as an assembly intermediate (see Allen, 1997 [6]).
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Active nuclear pore complexes in Chironomus: Visualization of transporter configurations related to mRNA export
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Kiseleva E, Goldberg MW, Allen TD, Akey CW. Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNA export. J Cell Sci. 111:1998;223-236.
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Akey CW. Structural plasticity of the nuclear pore complex. J Mol Biol. 248:1995;273-293.
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0029070074
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Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region
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Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E. Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J Biol Chem. 270:1995;14209-14213.
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23
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0030696935
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RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex
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Delphin C, Guan T, Melchior F, Gerace L. RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex. Mol Biol Cell. 8:1997;2379-2390.
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Delphin, C.1
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24
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0028832520
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GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import
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Melchior F, Guan T, Yokoyama N, Nishimoto T, Gerace L. GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import. J Cell Biol. 131:1995;571-581.
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Gorlich D. Nuclear protein import. Curr Opin Cell Biol. 9:1997;412-419.
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Corbett AH, Silver PA. Nucleocytoplasmic transport of macromolecules. Microbiol Mol Biol Rev. 61:1997;193-211.
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28
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0030951880
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Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex
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Bastos R, Ribas de Pouplana L, Enarson M, Bodoor K, Burke B. Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex. J Cell Biol. 137:1997;989-1000.
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Rutherford SA, Goldberg MW, Allen TD. Three-dimensional visualization of the route of protein import: the role of nuclear pore complex substructures. Exp Cell Res. 232:1997;146-160.
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Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
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Guan T, Muller S, Klier G, Pante N, Blevitt JM, Haner M, Paschal B, Aebi U, Gerace L. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol Biol Cell. 6:1995;1591-1603.
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Pante N, Jarmolowski A, Izaurralde E, Sauder U, Baschong W, Mattaj IW. Visualizing nuclear export of different classes of RNA by electron microscopy. RNA. 3:1997;498-513.
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Cordes VC, Reidenbach S, Rackwitz HR, Franke WW. Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J Cell Biol. 136:1997;515-529.
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Assembly of the nuclear pore - Biochemically distinct steps revealed with NEM, GTPγS, and BAPTA
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of outstanding interest. Steps in NPC and nuclear envelope assembly were determined in cell-free extracts by the use of inhibitors. Assembly was followed by immunofluorescence using an anti-nucleoporin antibody and by TEM. It was shown that NPC assembly depended on prior nuclear membrane fusion, which is inhibited both by the alkylating agent NEM and GTPγS. It was shown that NPCs are inserted in the double-membraned nuclear envelope, and that NPC assembly is inhibited at separate, early steps by GTPγS and the calcium chelator BAPTA.
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Macaulay C, Forbes DJ. Assembly of the nuclear pore - biochemically distinct steps revealed with NEM, GTPγS, and BAPTA. of outstanding interest J Cell Biol. 132:1996;5-20 Steps in NPC and nuclear envelope assembly were determined in cell-free extracts by the use of inhibitors. Assembly was followed by immunofluorescence using an anti-nucleoporin antibody and by TEM. It was shown that NPC assembly depended on prior nuclear membrane fusion, which is inhibited both by the alkylating agent NEM and GTPγS. It was shown that NPCs are inserted in the double-membraned nuclear envelope, and that NPC assembly is inhibited at separate, early steps by GTPγS and the calcium chelator BAPTA.
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Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event
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of outstanding interest. The steps of nuclear assembly in vitro were followed by FEISEM. These steps included nuclear vesicle binding to chromatin, followed by fusion and flattening. NPCs were then assembled, the convoluted nuclear surface became smooth, and then the nuclei grew. Two morphologically distinct classes of vesicles were involved, one with ribosomes and one without. Inhibition of NPC assembly prevented the smoothing step.
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Wiese C, Goldberg MW, Allen TD, Wilson KL. Nuclear envelope assembly in Xenopus extracts visualized by scanning EM reveals a transport-dependent 'envelope smoothing' event. of outstanding interest J Cell Sci. 110:1997;1489-1502 The steps of nuclear assembly in vitro were followed by FEISEM. These steps included nuclear vesicle binding to chromatin, followed by fusion and flattening. NPCs were then assembled, the convoluted nuclear surface became smooth, and then the nuclei grew. Two morphologically distinct classes of vesicles were involved, one with ribosomes and one without. Inhibition of NPC assembly prevented the smoothing step.
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J Cell Sci
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Wiese, C.1
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0030793799
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In vivo dynamics of nuclear pore complexes in yeast
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