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Structure of the Nuclear Pore

  • Chapter
Nuclear Import and Export in Plants and Animals

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

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Abstract

The nucleus is a defining hallmark in cells of all the higher organisms: yeast, animals, and plants. As the repository of the genome, it both encloses the chromatin and regulates its accessibility. It is also the site of nucleic acid synthesis, including replica-tion of DNA, transcription and editing of messenger RNA, synthesis of ribosomal RNAs, and assembly of ribosomal subunits. By contrast, the cytoplasm is the site of protein synthesis, where functional ribosomes translate mRNA into polypeptides. The nuclear envelope defines the border between these two distina biochemical worlds. The nuclear pores (or nuclear pore complexes, NPCs) serve as guardians of this border, acting as the gateway for molecular ex-change between the two major cellular compartments. They are deeply integrated to the physi-ological function of every cellular pathway involving communication between enzymatic, sig-naling, or regtdatory activities on one hand, and gene expression on the other. The nuclear pore complex is also a fascinating molecular machine, facilitating the passage of specific macromol-ecules in one direction while ferrying others in the opposite sense.

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References

  1. Gorlich D, Kutay U. Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 1999; 15:607–660.

    PubMed  CAS  Google Scholar 

  2. Goldfarb DS, Gariepy J, Schoolnik G et al. Synthetic peptides as nuclear localization signals. Nature 1986; 322:641–644.

    PubMed  CAS  Google Scholar 

  3. Kalderon D, Roberts BL, Richardson WD et al. A short amino acid sequence able to specify nuclear location. Cell 1984; 39:499–509.

    PubMed  CAS  Google Scholar 

  4. Lanford RE, Butel JS. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell 1984; 37:801–13.

    PubMed  CAS  Google Scholar 

  5. Gorlich D, Mattaj IW. Nucleocytoplasmic transport. Science 1996; 271:1513–1518.

    PubMed  CAS  Google Scholar 

  6. Mattaj IW, Englmeier L. Nucleocytoplasmic transport: The soluble phase. Annu Rev Biochem 1998; 67:265–306.

    PubMed  CAS  Google Scholar 

  7. Yoneda Y. Nucleocytoplasmic protein traffic and its significance to cell function. Genes Cells 2000;5:777–87.

    PubMed  CAS  Google Scholar 

  8. Pante N, Aebi U. Toward the molecular dissection of protein import into nuclei. Curr Opin Cell Biol 1996; 8:397–406.

    PubMed  CAS  Google Scholar 

  9. Pante N, Aebi U. Molecular dissection of the nuclear pore complex. Crit Rev Biochem Mol Biol 1996; 31:153–99.

    PubMed  CAS  Google Scholar 

  10. Kiseleva E, Goldberg MW, Cronshaw J et al. The nuclear pore complex: Structure, function, and dynamics. Crit Rev Eukaryot Gene Expr 2000; 10:101–12.

    PubMed  CAS  Google Scholar 

  11. Stoffler D, Goldie KN, Feja B et al. Calcium-mediated structural changes of native nuclear pore complexes monitored by time-lapse atomic force microscopy. J Mol Biol 1999; 287:741–52.

    PubMed  CAS  Google Scholar 

  12. Rexach M, Blobel G. Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 1995; 83:683–92.

    PubMed  CAS  Google Scholar 

  13. Rout MP, Aitchison JD, Suprapto A et al. The yeast nuclear pore complex: Composition, architecture, and transport mechanism. J Cell Biol 2000; 148:635–51.

    PubMed  CAS  Google Scholar 

  14. Macara IG. Transport into and out of the nucleus. Microbiol Mol Biol Rev 2001; 65:570–94, table of contents.

    PubMed  CAS  Google Scholar 

  15. Ribbeck K, Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J 2002; 21:2664–71.

    PubMed  CAS  Google Scholar 

  16. Perez-Terzic C, Pyle J, Jaconi M et al. Conformational states of the nuclear pore complex induced by depletion of nuclear Ca2+ stores. Science 1996; 273:1875–7.

    PubMed  CAS  Google Scholar 

  17. Strubing C, Clapham DE. Active nuclear import and export is independent of lumenal Ca2+ stores in intact mammalian cells. J Gen Physiol 1999; 113:239–48.

    PubMed  CAS  Google Scholar 

  18. Wei X, Henke VG, Strubing C et al. Real-time imaging of nuclear permeation by EGFP in single intact cells. Biophys J 2003; 84:1317–27.

    PubMed  CAS  Google Scholar 

  19. Moore MS. Ran and nuclear transport. J Biol Chem 1998; 273:22857–60.

    PubMed  CAS  Google Scholar 

  20. Rout MP, Aitchison JD. The nuclear pore complex as a transport machine. J Biol Chem 2001;276:16593–6.

    PubMed  CAS  Google Scholar 

  21. Elbaum M. The nuclear pore complex: Biochemical machine or Maxwell demon? Paris: CR Acad Sci 2000; 2:681–807.

    Google Scholar 

  22. Weis K. Nucleocytoplasmic transport: Cargo trafficking across the border. Curr Opin Cell Biol 2002; 14:328–35.

    PubMed  CAS  Google Scholar 

  23. Gorlich D, Prehn S, Laskey RA et al. Isolation of a protein that is essential for the first step of nuclear protein import. Cell 1994; 79:767–78.

    PubMed  CAS  Google Scholar 

  24. Radu A, Blobel G, Moore MS. Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc Natl Acad Sci USA 1995; 92:1769–73.

    PubMed  CAS  Google Scholar 

  25. Iovine MK, Watkins JL, Wente SR. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J Cell Biol 1995; 131:1699–713.

    PubMed  CAS  Google Scholar 

  26. Chi NC, Adam EJ, Adam SA. Sequence and characterization of cytoplasmic nuclear protein import factor p97. J Cell Biol 1995; 130:265–74.

    PubMed  CAS  Google Scholar 

  27. Moore MS, Blobel G. The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 1993; 365:661–3.

    PubMed  CAS  Google Scholar 

  28. Melchior F, Paschal B, Evans J et al. Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J Cell Biol 1993; 123:1649–59.

    PubMed  CAS  Google Scholar 

  29. Paschal BM, Delphin C, Gerace L. Nucleotide-specific interaction of Ran/TC4 with nuclear trans port factors NTF2 and p97. Proc Natl Acad Sci USA 1996; 93:7679–83.

    PubMed  CAS  Google Scholar 

  30. Moroianu J, Blobel G, Radu A. Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta. Proc Natl Acad Sci USA 1996; 93:7059–62.

    PubMed  CAS  Google Scholar 

  31. Koepp DM, Silver PA. A GTPase controlling nuclear trafficking: Running the right way or walking RANdomly? Cell 1996; 87:1–4.

    PubMed  CAS  Google Scholar 

  32. Avis JM, Clarke PR. Ran, a GTPase involved in nuclear processes: Its regulators and effectors. J Cell Sci 1996; 109 (Pt 10):2423–7.

    PubMed  CAS  Google Scholar 

  33. Coutavas E, Ren M, Oppenheim JD et al. Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4. Nature 1993; 366:585–7.

    PubMed  CAS  Google Scholar 

  34. Bischoff FR, Klebe C, Kretschmer J et al. RanGAP1 induces GTPase activity of nuclear Ras-related Ran. Proc Natl Acad Sci USA 1994; 91:2587–91.

    PubMed  CAS  Google Scholar 

  35. Izaurralde E, Kutay U, von Kobbe C et al. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J 1997; 16:6535–47.

    PubMed  CAS  Google Scholar 

  36. Mahajan R, Delphin C, Guan T et al. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997; 88:97–107.

    PubMed  CAS  Google Scholar 

  37. Matunis MJ, Coutavas E, Blobel G. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 1996; 135:1457–70.

    PubMed  CAS  Google Scholar 

  38. Matunis MJ, Wu J, Blobel G. SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex. J Cell Biol 1998; 140:499–509.

    PubMed  CAS  Google Scholar 

  39. Kalab P, Weis K, Heald R. Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science 2002; 295:2452–6.

    PubMed  CAS  Google Scholar 

  40. Smith AE, Slepchenko BM, Schaff JC et al. Systems analysis of Ran transport. Science 2002;295:488–91.

    PubMed  CAS  Google Scholar 

  41. Gorlich D, Seewald MJ, Ribbeck K. Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J 2003; 22:1088–100.

    PubMed  Google Scholar 

  42. Nachury MV, Weis K. The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci USA 1999; 96:9622–7.

    PubMed  CAS  Google Scholar 

  43. Ossareh-Nazari B, Bachelerie F, Dargemont C. Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 1997; 278:141–4.

    PubMed  CAS  Google Scholar 

  44. Stade K, Ford CS, Guthrie C et al. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 1997; 90:1041–50.

    PubMed  CAS  Google Scholar 

  45. Fornerod M, Ohno M, Yoshida M et al. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997; 90:1051–60.

    PubMed  CAS  Google Scholar 

  46. Neville M, Stutz F, Lee L et al. The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr Biol 1997; 7:767–75.

    PubMed  CAS  Google Scholar 

  47. Fukuda M, Asano S, Nakamura T et al. CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 1997; 390:308–11.

    PubMed  CAS  Google Scholar 

  48. Pasquinelli AE, Powers MA, Lund E et al. Inhibition of mRNA export in vertebrate cells by nuclear export signal conjugates. Proc Natl Acad Sci USA 1997; 94:14394–9.

    PubMed  CAS  Google Scholar 

  49. Kudo NS, Khochbin K, Nishi K et al. Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J Biol Chem 1997; 272:29742–51.

    PubMed  CAS  Google Scholar 

  50. Kutay U, Bischoff FR, Kostka S et al. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell 1997; 90:1061–71.

    PubMed  CAS  Google Scholar 

  51. Arts GJ, Fornerod M, Mattaj IW. Identification of a nuclear export receptor for tRNA. Curr Biol 1998; 8:305–14.

    PubMed  CAS  Google Scholar 

  52. Kutay U, Lipowsky G, Izaurralde E et al. Identification of a tRNA-specific nuclear export receptor. Mol Cell 1998; 1:359–69.

    PubMed  CAS  Google Scholar 

  53. Kiseleva E, Goldberg MW, Allen TD et al. Active nuclear pore complexes in Chironomus: Visualization of transporter configurations related to mRNP export. J Cell Sci 1998; 111 (Pt 2):223–36.

    PubMed  CAS  Google Scholar 

  54. Wiese C, Wilde A, Moore MS et al. Role of importin-beta in coupling Ran to downstream targets in microtubule assembly. Science 2001; 291:653–6.

    PubMed  CAS  Google Scholar 

  55. Nachury MV, Maresca TJ, Salmon WC et al. Importin beta is a mitotic target of the small GTPase Ran in spindle assembly. Cell 2001; 104:95–106.

    PubMed  CAS  Google Scholar 

  56. Gruss OJ, Carazo-Salas RE, Schatz CA et al. Ran induces spindle assembly by reversing the inhibitory effect of importin alpha on TPX2 activity. Cell 2001; 104:83–93.

    PubMed  CAS  Google Scholar 

  57. Fagotto F, Gluck U, Gumbiner BM. Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of beta-catenin. Curr Biol 1998; 8:181–90.

    PubMed  CAS  Google Scholar 

  58. Yokoya F, Imamoto N, Tachibana T et al. Beta-catenin can be transported into the nucleus in a Ran-unassisted manner. Mol Biol Cell 1999; 10:1119–31.

    PubMed  CAS  Google Scholar 

  59. Xu L, Massague J. Nucleocytoplasmic shuttling of signal transducers. Nat Rev Mol Cell Biol 2004; 5:209–19.

    PubMed  CAS  Google Scholar 

  60. Callan HG, Tomlin SG. Experimental studies on amphibian oocyte nuclei. I. Investigation of the structure of the nuclear membrane by means of the electron microscope. Proc R Soc Lond B Biol Sci 1950; 137:367–78.

    PubMed  CAS  Google Scholar 

  61. Gall JG. Observations on the nuclear membrane with the electron microscope. Exp Cell Res 1954; 7:197–200.

    PubMed  CAS  Google Scholar 

  62. Watson ML. Further observations on the nuclear envelope of the animal cell. J Biophys Biochem Cytol 1959; 6:147–56.

    PubMed  CAS  Google Scholar 

  63. Gall JG. Octagonal nuclear pores. J Cell Biol 1967; 32:391–9.

    PubMed  CAS  Google Scholar 

  64. Daniels EW, McNiff JM, Longwell AC. Ultrastructure of oyster gametes. ANL-7635. ANL Rep 1969; 195–9.

    Google Scholar 

  65. Franke WW, Scheer U. The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. I. The mature oocyte. J Ultrastruct Res 1970; 30:288–316.

    PubMed  CAS  Google Scholar 

  66. Franke WW, Scheer U. The ultrastructure of the nuclear envelope of amphibian oocytes: A rein-vestigation. II. The immature oocyte and dynamic aspects. J Ultrastruct Res 1970; 30:317–27.

    PubMed  CAS  Google Scholar 

  67. Maul GG. On the octagonality of the nuclear pore complex. J Cell Biol 1971; 51:558–63.

    PubMed  CAS  Google Scholar 

  68. Feldherr CM. Structure and function of the nuclear envelope. Adv Cell Mol Biol 1972; 2.

    Google Scholar 

  69. Markovics J, Glass L, Maul GG. Pore patterns on nuclear membranes. Exp Cell Res 1974; 85:443–51.

    PubMed  CAS  Google Scholar 

  70. Kirschner RH, Rusli M, Martin TE. Characterization of the nuclear envelope, pore complexes, and dense lamina of mouse liver nuclei by high resolution scanning electron microscopy. J Cell Biol 1977; 72:118–32.

    PubMed  CAS  Google Scholar 

  71. Ris H. The three dimensional structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy. EMSA Bulletin 1991; 21:54–56.

    Google Scholar 

  72. 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 1992; 119:1429–40.

    PubMed  CAS  Google Scholar 

  73. Whytock S, Stewart M. Preparation of shadowed nuclear envelopes from Xenopus oocyte germinal vesicles for electron microscopy. J Microsc 1988; 151 (Pt 2):115–26.

    PubMed  CAS  Google Scholar 

  74. Jarnik M, Aebi U. Toward a more complete 3-D structure of the nuclear pore complex. J Struct Biol 1991; 107:291–308.

    PubMed  CAS  Google Scholar 

  75. Oberleithner H, Brinckmann E, Schwab A et al. Imaging nuclear pores of aldosterone-sensitive kidney cells by atomic force microscopy. Proc Natl Acad Sci USA 1994; 91:9784–8.

    PubMed  CAS  Google Scholar 

  76. Wang H, Clapham DE. Conformational changes of the in situ nuclear pore complex. Biophys J 1999; 77:241–7.

    PubMed  CAS  Google Scholar 

  77. Nevo R, Markiewicz P, Kapon R et al. High-resolution imaging of the nuclear pore complex by AC scanning force microscopy. Single Mol 2000; 1(1):109–114.

    CAS  Google Scholar 

  78. Jaggi RD, Franco-Obregon A, Muhlhausser P et al. Modulation of nuclear pore topology by transport modifiers. Biophys J 2003; 84:665–70.

    PubMed  CAS  Google Scholar 

  79. Unwin PN, Milligan RA. A large particle associated with the perimeter of the nuclear pore complex. J Cell Biol 1982; 93:63–75.

    PubMed  CAS  Google Scholar 

  80. Akey CW. Interactions and structure of the nuclear pore complex revealed by cryo-electron microscopy. J Cell Biol 1989; 109:955–70.

    PubMed  CAS  Google Scholar 

  81. Akey CW, Goldfarb DS. Protein import through the nuclear pore complex is a multistep process. J Cell Biol 1989; 109:971–82.

    PubMed  CAS  Google Scholar 

  82. Akey CW. Visualization of transport-related configurations of the nuclear pore transporter. Biophys J 1990; 58:341–55.

    PubMed  CAS  Google Scholar 

  83. Hinshaw JE, Carragher BO, Milligan RA. Architecture and design of the nuclear pore complex. Cell 1992; 69:1133–41.

    PubMed  CAS  Google Scholar 

  84. Akey CW, Radermacher M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J Cell Biol 1993; 122:1–19.

    PubMed  CAS  Google Scholar 

  85. Akey CW. Structural plasticity of the nuclear pore complex. J Mol Biol 1995; 248:273–93.

    PubMed  CAS  Google Scholar 

  86. Stoffler D, Feja B, Fahrenkrog B et al. Cryo-electron tomography provides novel insights into nuclear pore architecture: Implications for nucleocytoplasmic transport. J Mol Biol 2003; 328:119–30.

    PubMed  CAS  Google Scholar 

  87. Fahrenkrog B, Aebi U. The nuclear pore complex: Nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 2003; 4:757–66.

    PubMed  CAS  Google Scholar 

  88. Goldberg MW, Solovei I, Allen TD. Nuclear pore complex structure in birds. J Struct Biol 1997; 119:284–94.

    CAS  Google Scholar 

  89. Feldherr CM, Akin D. The location of the transport gate in the nuclear pore complex. J Cell Sci 1997; 110 (Pt 24):3065–70.

    PubMed  CAS  Google Scholar 

  90. Keminer O, Peters R. Permeability of single nuclear pores. Biophys J 1999; 77:217–28.

    PubMed  CAS  Google Scholar 

  91. Rout MP, Blobel G. Isolation of the yeast nuclear pore complex. J Cell Biol 1993; 123:771–83.

    PubMed  CAS  Google Scholar 

  92. Yang Q, Rout MP, Akey CW. Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications. Mol Cell 1998; 1:223–34.

    PubMed  CAS  Google Scholar 

  93. Kiseleva E, Allen TD, Rutherford S et al. Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments. J Struct Biol 2004; 145:272–88.

    PubMed  CAS  Google Scholar 

  94. Roberts K, Northcote DH. Structure of the nuclear pore in higher plants. Nature 1970; 228:385–6.

    PubMed  CAS  Google Scholar 

  95. Franke WW, Scheer U, Fritsch H. Intranuclear and cytoplasmic annulate lamellae in plant cells. J Cell Biol 1972; 53:823–7.

    PubMed  CAS  Google Scholar 

  96. Hicks GR, Raikhel NV. Specific binding of nuclear localization sequences to plant nuclei. Plant Cell 1993; 5:983–94.

    PubMed  CAS  Google Scholar 

  97. Reichelt R, Holzenburg A, Buhle Jr EL et al. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J Cell Biol 1990; 110:883–94.

    PubMed  CAS  Google Scholar 

  98. Krohne G, Franke WW, Scheer U. The major polypeptides of the nuclear pore complex. Exp Cell Res 1978; 116:85–102.

    PubMed  CAS  Google Scholar 

  99. Goldberg MW, Allen TD. The nuclear pore complex and lamina: Three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J Mol Biol 1996; 257:848–65.

    PubMed  CAS  Google Scholar 

  100. Goldberg MW, Allen TD. The nuclear pore complex: Three-dimensional surface structure revealed by field emission, in-lens scanning electron microscopy, with underlying structure uncovered by proteolysis. J Cell Sci 1993; 106:261–74.

    PubMed  CAS  Google Scholar 

  101. Hinshaw JE, Milligan RA. Nuclear pore complexes exceeding eightfold rotational symmetry. J Struct Biol 2003; 141:259–68.

    PubMed  CAS  Google Scholar 

  102. Wischnitzer S. The annulate lamellae. Int Rev Cytol 1970; 27:65–100.

    PubMed  CAS  Google Scholar 

  103. Stafstrom JP, Staehelin LA. Dynamics of the nuclear envelope and of nuclear pore complexes during mitosis in the Drosophila embryo. Eur J Cell Biol 1984; 34:179–89.

    PubMed  CAS  Google Scholar 

  104. Dabauvalle MC, Loos K, Merkert H et al. Spontaneous assembly of pore complex-containing membranes (“annulate lamellae”) in Xenopus egg extract in the absence of chromatin. J Cell Biol 1991; 112:1073–82.

    PubMed  CAS  Google Scholar 

  105. Kessel RG. Annulate lamellae: A last frontier in cellular organelles. Int Rev Cytol 1992; 133:43–120.

    PubMed  CAS  Google Scholar 

  106. Meier E, Miller BR, Forbes DJ. Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation. J Cell Biol 1995; 129:1459–72.

    PubMed  CAS  Google Scholar 

  107. Cordes VC, Reidenbach S, Franke W. Cytoplasmic annulate lamellae in cultured cells: Composition, distribution, and mitotic behavior. Cell Tissue Res 1996; 284:177–91.

    PubMed  CAS  Google Scholar 

  108. Ewald A, Hofbauer S, Dabauvalle MC et al. Preassembly of annulate lamellae in egg extracts inhibits nuclear pore complex formation, but not nuclear membrane assembly. Eur J Cell Biol 1997; 73:259–69.

    PubMed  CAS  Google Scholar 

  109. Ewald A, Kossner U, Scheer U et al. A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes. J Cell Sci 1996; 109 (Pt 7):1813–24.

    PubMed  CAS  Google Scholar 

  110. Miller BR, Forbes DJ. Purification of the vertebrate nuclear pore complex by biochemical criteria. Traffic 2000; 1:941–51.

    PubMed  CAS  Google Scholar 

  111. Onischenko EA, Gubanova NV, Kieselbach T et al. Annulate lamellae play only a minor role in the storage of excess nucleoporins in Drosophila embryos. Traffic 2004; 5:152–64.

    PubMed  CAS  Google Scholar 

  112. Maul GG. The nuclear and the cytoplasmic pore complex: Structure, dynamics, distribution, and evolution. Int Rev Cytol Suppl 1977; 75–186.

    Google Scholar 

  113. Stafstrom JP, Staehelin LA. Are annulate lamellae in the Drosophila embryo the result of overproduction of nuclear pore components? J Cell Biol 1984; 98:699–708.

    PubMed  CAS  Google Scholar 

  114. Harel A, Zlotkin E, Nainudel-Epszteyn S et al. Persistence of major nuclear envelope antigens in an envelope-like structure during mitosis in Drosophila melanogaster embryos. J Cell Sci 1989; 94 (Pt 3):463–70.

    PubMed  CAS  Google Scholar 

  115. Kiseleva E, Rutherford S, Cotter LM et al. Steps of nuclear pore complex disassembly and reassembly during mitosis in early Drosophila embryos. J Cell Sci 2001; 114:3607–18.

    PubMed  CAS  Google Scholar 

  116. Lohka MJ, Masui Y. Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 1983; 220:719–21.

    PubMed  CAS  Google Scholar 

  117. Zhang H, Ruderman JV. Differential replication capacities of Gl and S-phase extracts from sea urchin eggs. J Cell Sci 1993; 104 (Pt 2):565–72.

    PubMed  CAS  Google Scholar 

  118. Cameron LA, Poccia DL. In vitro development of the sea urchin male pronucleus. Dev Biol 1994; 162:568–78.

    PubMed  CAS  Google Scholar 

  119. Li CJ, Gui JF. Comparative studies on in vitro sperm decondensation and pronucleus formation in egg extracts between gynogenetic and bisexual fish. Cell Res 2003; 13:159–69.

    PubMed  Google Scholar 

  120. Ulitzur N, Gruenbaum Y. Nuclear envelope assembly around sperm chromatin in cell-free preparations from Drosophila embryos. FEBS Lett 1989; 259:113–6.

    PubMed  CAS  Google Scholar 

  121. Berrios M, Avilion AA. Nuclear formation in a Drosophila cell-free system. Exp Cell Res 1990; 191:64–70.

    PubMed  CAS  Google Scholar 

  122. Burke B, Gerace L. A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 1986; 44:639–52.

    PubMed  CAS  Google Scholar 

  123. Suprynowicz FA, Gerace L. A fractionated cell-free system for analysis of prophase nuclear disassembly. J Cell Biol 1986; 103:2073–81.

    PubMed  CAS  Google Scholar 

  124. Lohka MJ. The reconstitution of nuclear envelopes in cell-free extracts. Cell Biol Int Rep 1988; 12:833–48.

    PubMed  CAS  Google Scholar 

  125. Laskey RA, Leno GH. Assembly of the cell nucleus. Trends Genet 1990; 6:406–10.

    PubMed  CAS  Google Scholar 

  126. Zhao Y, Liu X, Wu M et al. In vitro nuclear reconstitution could be induced in a plant cell-free system. FEBS Lett 2000; 480:208–12.

    PubMed  CAS  Google Scholar 

  127. Lu P, Zhai ZH. Nuclear assembly of demembranated Xenopus sperm in plant cell-free extracts from Nicotiana ovules. Exp Cell Res 2001; 270:96–101.

    PubMed  CAS  Google Scholar 

  128. Newmeyer DD, Wilson KL. Egg extracts for nuclear import and nuclear assembly reactions. Meth ods Cell Biol 1991; 36:607–34.

    CAS  Google Scholar 

  129. Murray AW. Cell cycle extracts. Methods Cell Biol 1991; 36:581–605.

    PubMed  CAS  Google Scholar 

  130. Smythe C, Newport JW. Systems for the study of nuclear assembly, DNA replication, and nuclear breakdown in Xenopus laevis egg extracts. Methods Cell Biol 1991; 35:449–68.

    PubMed  CAS  Google Scholar 

  131. Lohka MJ. Analysis of nuclear envelope assembly using extracts of Xenopus eggs. Methods Cell Biol 1998; 53:367–95.

    PubMed  CAS  Google Scholar 

  132. Allan VJ. Organelle motility and membrane network formation in metaphase and interphase cell-free extracts. Methods Enzymol 1998; 298:339–53.

    PubMed  CAS  Google Scholar 

  133. Desai A, Murray A, Mitchison TJ et al. The use of Xenopus egg extracts to study mitotic spindle assembly and function in vitro. Methods Cell Biol 1999; 61:385–412.

    PubMed  CAS  Google Scholar 

  134. Newmeyer DD, Finlay DR, Forbes DJ. In vitro transport of a fluorescent nuclear protein and exclusion of nonnuclear proteins. J Cell Biol 1986; 103:2091–102.

    PubMed  CAS  Google Scholar 

  135. Macaulay C, Forbes DJ. Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA. J Cell Biol 1996; 132:5–20.

    PubMed  CAS  Google Scholar 

  136. Goldberg MW, Wiese C, Allen TD et al. Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: Evidence for structural intermediates in nuclear pore complex assembly. J Cell Sci 1997; 110 (Pt 4):409–20.

    PubMed  CAS  Google Scholar 

  137. Hetzer M, Bilbao-Cortes D, Walther TC et al. GTP hydrolysis by Ran is required for nuclear envelope assembly. Mol Cell 2000; 5:1013–24.

    PubMed  CAS  Google Scholar 

  138. Walther TC, Askjaer P, Gentzel M et al. RanGTP mediates nuclear pore complex assembly. Nature 2003; 424:689–94.

    PubMed  CAS  Google Scholar 

  139. Harel A, Chan RC, Lachish-Zalait A et al. Importin beta negatively regulates nuclear membrane fusion and nuclear pore complex assembly. Mol Biol Cell 2003; 14:4387–96.

    PubMed  CAS  Google Scholar 

  140. Dasso M, Seki T, Azuma Y et al. A mutant form of the Ran/TC4 protein disrupts nuclear function in Xenopus laevis egg extracts by inhibiting the RCC1 protein, a regulator of chromosome condensation. EMBO J 1994; 13:5732–44.

    PubMed  CAS  Google Scholar 

  141. Klebe C, Bischoff FR, Ponstingl H et al. Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAPl. Biochemistry. 1995; 34:639–47.

    PubMed  CAS  Google Scholar 

  142. Kutay U, Izaurralde E, Bischoff FR et al. Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. EMBO J 1997; 16:1153–63.

    PubMed  CAS  Google Scholar 

  143. Cronshaw JM, Krutchinsky AN, Zhang W et al. Proteomic analysis of the mammalian nuclear pore complex. J Cell Biol 2002; 158:915–27.

    PubMed  CAS  Google Scholar 

  144. Dabauvalle MC, Loos K, Scheer U. Identification of a soluble precursor complex essential for nuclear pore assembly in vitro. Chromosoma 1990; 100:56–66.

    PubMed  CAS  Google Scholar 

  145. Macaulay C, Meier E, Forbes DJ. Differential mitotic phosphorylation of proteins of the nuclear pore complex. J Biol Chem 1995; 270:254–62.

    PubMed  CAS  Google Scholar 

  146. Bodoor K, Shaikh S, Salina Det et al. Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis. J Cell Sci. 1999; 112 (Pt 13):2253–64.

    PubMed  CAS  Google Scholar 

  147. Matsuoka Y, Takagi M, Ban T et al. Identification and characterization of nuclear pore subcomplexes in mitotic extract of human somatic cells. Biochem Biophys Res Commun 1999; 254:417–23.

    PubMed  CAS  Google Scholar 

  148. Vasu S, Shah S, Orjalo A et al. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J Cell Biol 2001; 155:339–54.

    PubMed  CAS  Google Scholar 

  149. Belgareh N, Rabut G, Bai SW et al. An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells. J Cell Biol 2001; 154:1147–60.

    PubMed  CAS  Google Scholar 

  150. Drummond SP, Wilson KL. Interference with the cytoplasmic tail of gp210 disrupts “close apposition” of nuclear membranes and blocks nuclear pore dilation. J Cell Biol 2002; 158:53–62.

    PubMed  CAS  Google Scholar 

  151. Daigle N, Beaudouin J, Hartnell L et al. Nuclear pore complexes form immobile networks and have a very low turnover in live mammalian cells. J Cell Biol 2001; 154:71–84.

    PubMed  CAS  Google Scholar 

  152. Bucci M, Wente SR. In vivo dynamics of nuclear pore complexes in yeast. J Cell Biol 1997; 136:1185–99.

    PubMed  CAS  Google Scholar 

  153. Yokoyama N, Hayashi N, Seki T et al. A giant nucleopore protein that binds Ran/TC4. Nature 1995; 376:184–8.

    PubMed  CAS  Google Scholar 

  154. Wilken N, Senecal JL, Scheer U et al. Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. Eur J Cell Biol 1995; 68:211–9.

    PubMed  CAS  Google Scholar 

  155. Bischoff FR, Krebber H, Kempf T et al. Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rnalp involved in mRNA processing and transport. Proc Natl Acad Sci USA 1995; 92:1749–53.

    PubMed  CAS  Google Scholar 

  156. Walther TC, Pickersgill HS, Cordes VC et al. The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import. J Cell Biol 2002; 158:63–77.

    PubMed  CAS  Google Scholar 

  157. Sukegawa J, Blobel G. A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Ceil 1993; 72:29–38.

    CAS  Google Scholar 

  158. Shah S, Tugendreich S, Forbes D. Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J Cell Biol 1998; 141:31–49.

    PubMed  CAS  Google Scholar 

  159. Fahrenkrog B, Maco B, Fager AM et al. Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex. J Struct Biol 2002; 140:254–67.

    PubMed  CAS  Google Scholar 

  160. Cordes VC, Reidenbach S, Rackwitz HR et al. Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J Cell Biol 1997; 136:515–29.

    PubMed  CAS  Google Scholar 

  161. Zimowska G, Aris JP, Paddy MR. A Drosophila Tpr protein homolog is localized both in the extrachromosomal channel network and to nuclear pore complexes. J Cell Sci 1997; 110(Pt 8):927–44.

    PubMed  CAS  Google Scholar 

  162. Frosst P, Guan T, Subauste C et al. Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J Cell Biol 2002; 156:617–30.

    PubMed  CAS  Google Scholar 

  163. Krull S, Thyberg J, Bjorkroth B et al. Nucleoporins as components of the nuclear pore complex core structure and tpr as the architectural element of the nuclear basket. Mol Biol Cell 2004; 15:4261–77.

    PubMed  CAS  Google Scholar 

  164. Ullman KS, Shah S, Powers MA. The nucleoporin nup153 plays a critical role in multiple types of nuclear export. Mol Biol Cell 1999; 10:649–64.

    PubMed  CAS  Google Scholar 

  165. Walther TC, Fornerod M, Pickersgill H et al. The nucleoporin Nup153 is required for nuclear pore basket formation, nuclear pore complex anchoring and import of a subset of nuclear proteins. EMBO J 2001; 20:5703–14.

    PubMed  CAS  Google Scholar 

  166. Kolling R, Nguyen T, Chen EY et al. A new yeast gene with a myosin-like heptad repeat structure. Mol Gen Genet 1993; 237:359–69.

    PubMed  CAS  Google Scholar 

  167. Strambio-de-Castillia C, Blobel G, Rout MP. Proteins connecting the nuclear pore complex with the nuclear interior. J Cell Biol 1999; 144:839–55.

    PubMed  CAS  Google Scholar 

  168. Kosova B, Pante N, Rollenhagen C et al. Mlp2p, a component of nuclear pore attached intra nuclear filaments, associates with nic96p. J Biol Chem 2000; 275:343–50.

    PubMed  CAS  Google Scholar 

  169. Galy V, Olivo-Marin JC, Scherthan H et al. Nuclear pore complexes in the organization of silent telomeric chromatin. Nature 2000; 403:108–12.

    PubMed  CAS  Google Scholar 

  170. Feuerbach F, Galy V, Trelles-Sticken E et al. Nuclear architecture and spatial positioning help establish transcriptional states of telomeres in yeast. Nat Cell Biol 2002; 4:214–21.

    PubMed  CAS  Google Scholar 

  171. Hediger F, Dubrana K, Gasser SM. Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tell pathway of telomere length control. J Struct Biol 2002; 140:79–91.

    PubMed  CAS  Google Scholar 

  172. Galy V, Gadal O, Fromont-Racine M et al. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell 2004; 116:63–73.

    PubMed  CAS  Google Scholar 

  173. Harel A, Orjalo AV, Vincent T et al. Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores. Mol Cell 2003; 11:853–64.

    PubMed  CAS  Google Scholar 

  174. Walther TC, Alves A, Pickersgill H et al. The conserved Nup107–160 complex is critical for nuclear pore complex assembly. Cell 2003; 113:195–206.

    PubMed  CAS  Google Scholar 

  175. Loiodice I, Alves A, Rabut G et al. The entire Nup107–160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol Biol Cell 2004; 15:3333–44.

    PubMed  CAS  Google Scholar 

  176. Siniossoglou S, Wimmer C, Rieger M et al. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 1996; 84:265–75.

    PubMed  CAS  Google Scholar 

  177. Boehmer T, Enninga J, Dales S et al. Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex. Proc Natl Acad Sci USA 2003; 100:981–5.

    PubMed  CAS  Google Scholar 

  178. Grandi P, Dang T, Pane N et al. Nup93, a vertebrate homologue of yeast Nic96p, forms a com plex with a novel 205-kDa protein and is required for correct nuclear pore assembly. Mol Biol Cell 1997; 8:2017–38.

    PubMed  CAS  Google Scholar 

  179. Zabel U, Doye V, Tekotte H et al. Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J Cell Biol 1996; 133:1141–52.

    PubMed  CAS  Google Scholar 

  180. Finlay DR, Meier E, Bradley P et al. A complex of nuclear pore proteins required for pore function. J Cell Biol 1991; 114:169–83.

    PubMed  CAS  Google Scholar 

  181. Finlay DR, Newmeyer DD, Price TM et al. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol 1987; 104:189–200.

    PubMed  CAS  Google Scholar 

  182. Hanover JA, Cohen CK, Willingham MC et al. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. J Biol Chem 1987; 262:9887–94.

    PubMed  CAS  Google Scholar 

  183. Schlaich NL, Haner M, Lustig A et al. In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsp1p, Nup49p, and Nup57p. Mol Biol Cell 1997; 8:33–46.

    PubMed  CAS  Google Scholar 

  184. Dabauvalle MC, Schulz B, Scheer U et al. Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin. Exp Cell Res 1988; 174:291–6.

    PubMed  CAS  Google Scholar 

  185. Wolff B, Willingham MC, Hanover JA. Nuclear protein import: Specificity for transport across the nuclear pore. Exp Cell Res 1988; 178:318–34.

    PubMed  CAS  Google Scholar 

  186. Miller MW. Hanover JA. Functional nuclear pores reconstituted with beta 1–4 galactose-modified O-linked N-acetylglucosamine glycoproteins. J Biol Chem 1994; 269:9289–97.

    PubMed  CAS  Google Scholar 

  187. Miller MW, Caracciolo MR, Berlin WK et al. Phosphorylation and glycosylation of nucleoporins. Arch Biochem Biophys 1999; 367:51–60.

    PubMed  CAS  Google Scholar 

  188. Heese-Peck A, Cole RN, Borkhsenious ON et al. Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. Plant Cell 1995; 7:1459–71.

    PubMed  CAS  Google Scholar 

  189. Kraemer D, Wozniak RW, Blobel G et al. The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc Nad Acad Sci USA 1994; 91:1519–23.

    CAS  Google Scholar 

  190. Fornerod M, van Deursen J, van Baal S et al. The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J 1997; 16:807–16.

    PubMed  CAS  Google Scholar 

  191. Bastos R, Ribas de Pouplana L, Enarson M et al. Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex. J Cell Biol 1997; 137:989–1000.

    PubMed  CAS  Google Scholar 

  192. von Lindern M, van Baal S, Wiegant J et al. Can, a putative oncogene associated with myeloid leukemogenesis, may be activated by fusion of its 3′ half to different genes: Characterization of the set gene. Mol Cell Biol 1992; 12:3346–55.

    Google Scholar 

  193. von Lindern M, Fornerod M, van Baal S et al. The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA. Mol Cell Biol 1992; 12:1687–97.

    Google Scholar 

  194. van Deursen J, Boer J, Kasper L et al. G2 arrest and impaired nucleocytoplasmic transport in mouse embryos lacking the proto-oncogene CAN/Nup214. EMBO J 1996; 15:5574–83.

    PubMed  Google Scholar 

  195. Katahira J, Strasser K, Podtelejnikov A et al. The Mex67p-mediated nuclear mRNA export path way is conserved from yeast to human. EMBO J 1999; 18:2593–609.

    PubMed  CAS  Google Scholar 

  196. Segref A, Sharma K, Doye V et al. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J 1997; 16:3256–71.

    PubMed  CAS  Google Scholar 

  197. Gruter P, Tabernero C, von Kobbe C et al. TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from the nucleus. Mol Cell 1998; 1:649–59.

    PubMed  CAS  Google Scholar 

  198. Trotman LC, Mosberger N, Fornerod M et al. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat Cell Biol 2001; 3:1092–100.

    PubMed  CAS  Google Scholar 

  199. Fontoura BM, Blobel G, Matunis MJ. A conserved biogenesis pathway for nucleoporins: Proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96. J Cell Biol 1999; 144:1097–112.

    PubMed  CAS  Google Scholar 

  200. Hodel AE, Hodel MR, Griffis ER et al. The three-dimensional structure of the autoproteolytic, nuclear poretargeting domain of the human nucleoporin Nup98. Mol Cell 2002; 10:347–58.

    PubMed  CAS  Google Scholar 

  201. Powers MA, Forbes DJ, Dahlberg JE et al. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J Cell Biol 1997; 136:241–50.

    PubMed  CAS  Google Scholar 

  202. Griffis ER, Altan N, Lippincott-Schwartz J et al. Nup98 is a mobile nucleoporin with transcription-dependent dynamics. Mol Biol Cell 2002; 13:1282–97.

    PubMed  CAS  Google Scholar 

  203. Griffis ER, Xu S, Powers MA. Nup98 localizes to both nuclear and cytoplasmic sides of the nuclear pore and binds to two distinct nucleoporin subcomplexes. Mol Biol Cell 2003; 14:600–10.

    PubMed  CAS  Google Scholar 

  204. Gilchrist D, Mykytka B, Rexach M. Accelerating the rate of disassembly of karyopherin cargo complexes. J Biol Chem 2002; 277:18161–72.

    PubMed  CAS  Google Scholar 

  205. Ben-Erraim I, Gerace L. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J Cell Biol 2001; 152:411–7.

    Google Scholar 

  206. Pyhtila B, Rexach M. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J Biol Chem 2003; 278:42699–709.

    PubMed  CAS  Google Scholar 

  207. Denning DP, Uversky V, Patel SS et al. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J Biol Chem 2002; 277:33447–55.

    PubMed  CAS  Google Scholar 

  208. Denning DP, Patel SS, Uversky V et al. Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci USA 2003; 100:2450–5.

    PubMed  CAS  Google Scholar 

  209. Chook YM, Blobel G. Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature 1999; 399:230–7.

    PubMed  CAS  Google Scholar 

  210. Cingolani G, Bednenko J, Gillespie MT et al. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin beta. Mol Cell 2002; 10:1345–53.

    PubMed  CAS  Google Scholar 

  211. Vetter IR, Arndt A, Kutay U et al. Structural view of the Ran-importin beta interaction at 2.3 A resolution. Cell 1999; 97:635–46.

    PubMed  CAS  Google Scholar 

  212. Bayliss R, Kent HM, Corbett AH et al. Crystallization and initial X-ray diffraction characterization of complexes of FxFG nucleoporin repeats with nuclear transport factors. J Struct Biol 2000; 131:240–7.

    PubMed  CAS  Google Scholar 

  213. Bayliss R, Littlewood T, Strawn LA et al. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. J Biol Chem 2002; 277:50597–606.

    PubMed  CAS  Google Scholar 

  214. Bednenko J, Cingolani G, Gerace L. Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport. J Cell Biol 2003; 162:391–401.

    PubMed  CAS  Google Scholar 

  215. Bednenko J, Cingolani G, Gerace L. Nucleocytoplasmic transport: Navigating the channel. Traffic 2003; 4:127–35.

    PubMed  CAS  Google Scholar 

  216. Schwoebel ED, Talcott B, Cushman I et al. Ran-dependent signal-mediated nuclear import does not require GTP hydrolysis by Ran. J Biol Chem 1998; 273:35170–5.

    PubMed  CAS  Google Scholar 

  217. Schwoebel ED, Ho TH, Moore MS. The mechanism of inhibition of Ran-dependent nuclear transport by cellular ATP depletion. J Cell Biol 2002; 157:963–74.

    PubMed  CAS  Google Scholar 

  218. Lyman SK, Guan T, Bednenko J et al. Influence of cargo size on Ran and energy requirements for nuclear protein import. J Cell Biol 2002; 159:55–67.

    PubMed  CAS  Google Scholar 

  219. Feldherr CM, Kallenbach E, Schultz N. Movement of a karyophilic protein through the nuclear pores of oocytes. J Cell Biol 1984; 99:2216–22.

    PubMed  CAS  Google Scholar 

  220. Dworetzky SI, Feldherr CM. Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J Cell Biol 1988; 106:575–84.

    PubMed  CAS  Google Scholar 

  221. Peters R. Nuclear envelope permeability measured by fluorescence microphotolysis of single liver cell nuclei. J Biol Chem 1983; 258:11427–9.

    PubMed  CAS  Google Scholar 

  222. Peters R. Nucleo-cytoplasmic flux and intracellular mobility in single hepatocytes measured by fluorescence microphotolysis. EMBO J 1984; 3:1831–6.

    PubMed  CAS  Google Scholar 

  223. Peters R. Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility. Biochim Biophys Acta 1986; 864:305–59.

    PubMed  CAS  Google Scholar 

  224. Peters R, Lang I, Scholz M et al. Fluorescence microphotolysis to measure nucleocy0toplasmic trans port in vivo and in vitro. Biochem Soc Trans 1986; 14:821–2.

    PubMed  CAS  Google Scholar 

  225. Lang I, Scholz M, Peters R. Molecular mobility and nucleocytoplasmic flux in hepatoma cells. J Cell Biol 1986; 102:1183–90.

    PubMed  CAS  Google Scholar 

  226. Schulz B, Peters R. Nucleocytoplasmic protein traffic in single mammalian cells studied by fluorescence microphotolysis. Biochim Biophys Acta 1987; 930:419–31.

    PubMed  CAS  Google Scholar 

  227. Astumian RD, Derenyi I. Fluctuation driven transport and models of molecular motors and pumps. Eur Biophys J 1998; 27:474–89.

    PubMed  CAS  Google Scholar 

  228. Ribbeck K, Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J 2001; 20:1320–30.

    PubMed  CAS  Google Scholar 

  229. Bickel T, Bruinsma R. The nuclear pore complex mystery and anomalous diffusion in reversible gels. Biophys J 2002; 83:3079–87.

    PubMed  CAS  Google Scholar 

  230. Kustanovich T, Rabin Y. Metastable network model of protein transport through nuclear pores. Biophys J 2004; 86:2008–16.

    PubMed  CAS  Google Scholar 

  231. Strawn LA, Shen T, Shulga N et al. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat Cell Biol 2004; 6:197–206.

    PubMed  CAS  Google Scholar 

  232. Belanger KD, Kenna MA, Wei S et al. Genetic and physical interactions between Srplp and nuclear pore complex proteins Nuplp and Nup2p. J Cell Biol 1994; 126:619–30.

    PubMed  CAS  Google Scholar 

  233. Hood JK, Casolari JM, Silver PA. Nup2p is located on the nuclear side of the nuclear pore complex and coordinates Srplp/importin-alpha export. J Cell Sci 2000; 113(Pt 8):1471–80.

    PubMed  CAS  Google Scholar 

  234. Dilworth DJ, Suprapto A, Padovan JC et al. Nup2p dynamically associates with the distal regions of the yeast nuclear pore complex. J Cell Biol 2001; 153:1465–78.

    PubMed  CAS  Google Scholar 

  235. Haraguchi T, Koujin T, Hayakawa T et al. Live fluorescence imaging reveals early recruitment of emerin, LBR, RanBP2, and Nup153 to reforming functional nuclear envelopes. J Cell Sci 2000; 113(Pt 5):779–94.

    PubMed  CAS  Google Scholar 

  236. Lam DH, Apian PD. NUP98 gene fusions in hematologic malignancies. Leukemia 2001; 15:1689–1695.

    PubMed  CAS  Google Scholar 

  237. Cronshaw JM, Matunis MJ. The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome. Proc Natl Acad Sci USA 2003; 100:5823–7.

    PubMed  CAS  Google Scholar 

  238. Cronshaw JM, Matunis MJ. The nuclear pore complex: Disease associations and functional correlations. Trends Endocrinol Metab 2004; 15:34–9.

    PubMed  CAS  Google Scholar 

  239. Enarson P, Rattner JB, Ou Y et al. Autoantigens of the nuclear pore complex. J Mol Med 2004; 82:423–33.

    PubMed  CAS  Google Scholar 

  240. Kau TR, Way JC, Silver PA. Nuclear transport and cancer: From mechanism to intervention. Nat Rev Cancer 2004; 4:106–17.

    PubMed  CAS  Google Scholar 

  241. Cohen M, Wilson KL, Gruenbaum Y. Membrane proteins of the nuclear pore complex: Gp210 is conserved in Drosophila, C. elegans, and A. thaliana. Gen Ther Mol Biol 2001; 4:47–55.

    Google Scholar 

  242. Rose A, Patel S, Meier I. The plant nuclear envelope. Planta 2004; 218:327–336.

    PubMed  CAS  Google Scholar 

  243. Hubner S, Smith HM, Hu W et al. Plant importin alpha binds nuclear localization sequences with high affinity and can mediate nuclear import independent of importin beta. J Biol Chem 1999; 274:22610–7.

    PubMed  CAS  Google Scholar 

  244. Merkle T, Leclerc D, Marshallsay C et al. A plant in vitro system for the nuclear import of proteins. Plant J 1996; 10:1177–86.

    PubMed  Google Scholar 

  245. Hicks GR, Smith HM, Lobreaux S et al. Nuclear import in permeabilized protoplasts from higher plants has unique features. Plant Cell 1996; 8:1337–52.

    PubMed  CAS  Google Scholar 

  246. Allen TD, Cronshaw JM, Bagley S et al. The nuclear pore complex: Mediator of translocation between nucleus and cytoplasm. J Cell Sci 2000; 113(Pt 10):1651–9.

    PubMed  CAS  Google Scholar 

  247. Suntharalingam M, Wente SR. Peering through the Pore: Nuclear pore complex structure, assembly, and function. Developmental Cell 2003; 4:775–789.

    PubMed  CAS  Google Scholar 

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Elbaum, M. (2005). Structure of the Nuclear Pore. In: Nuclear Import and Export in Plants and Animals. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-27747-1_1

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