Advertisement

The Structure and Composition of the Yeast NPC

  • Caterina Strambio-de-Castillia
  • Michael P. Rout
Part of the Results and Problems in Cell Differentiation book series (RESULTS, volume 35)

Abstract

The double-membraned nuclear envelope (NE) behaves as a selective barrier that segregates the genome from all cytosolic processes. A highly regulated exchange system between these two compartments is essential for proper cell growth, progression through the cell cycle, accurate responses to developmental and extracellular signals and to maintain the functional integrity of the nucleus. The sole mediators of controlled nucleocytoplasmic transport are the nuclear pore complexes (NPCs), large proteinaceous machineries embedded within specialized circular pores that traverse the NE. In actively growing cells it is estimated that every minute hundreds of proteins and ribonucleoprotein particles (RNPs) traverse each NPC in both directions. The basic mechanisms of nuclear transport appear to be highly conserved across distantly related species (reviewed in Nigg 1997; Mattaj and Englmeier 1998; Gorlich and Kutay 1999; Wente 2000). Although metabolites, water, ions and small macromolecules can freely diffuse through aqueous channels of 10 nm in the NPC, large macromolecular particles with a diameter of up to 30 nm are selectively transported across the NPC via a highly regulated energy-dependent process. Active transport requires specific soluble transport factors that recognize individual substrates both inside and outside the nucleus and mediate their interaction with the stationary phase of the NPC translocation machinery. Specifically, the translocation of transport substrates is known to require the docking of the transport complex to the NPC, the active translocation of the docked complexes across the NPC and the release of the substrate into the target compartment. Various models have been proposed to explain how this docked complex is actively translocated across the 50–60 nm long NPC transporter and then subsequently released into the nucleoplasm, and the matter is still highly controversial (see below). All models agree in attributing a crucial importance to the protein Ran in maintaining vectorial cargo transport and regulating the binding and release steps that take place during translocation. As a member of the Ras superfamily of small GTPases, Ran exists within the cell in a GDP-bound and in a GTP-bound form. The balance between these two forms is regulated by a variety of Ran cofactors that are asymmetrically distributed within the cell. As a consequence cytoplasmic Ran is thought to exist prevalently in the GDP-bound form, while Ran-GTP is thought to predominate in the nucleus. This differential distribution of Ran-GTP versus Ran-GDP would establish directional transport by ensuring that transport complexes are formed in one compartment and disassembled in the other (reviewed in Cole and Hammell 1998; Mattaj and Englmeier 1998; Pemberton et al. 1998; Wozniak et al. 1998; Gorlich and Kutay 1999). Understanding this regulated transport demands an understanding of the detailed three-dimensional map of the NPC and of the interactions and relationships between the soluble and stationary phases of nuclear transport.

Keywords

Nuclear Pore Complex mRNA Export Nucleocytoplasmic Transport Transport Factor Nuclear Interior 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Adams IR, Kilmartin JV (1999) Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae. J Cell Biol 145: 809–823PubMedCrossRefGoogle Scholar
  2. Aitchison JD, Blobel G, Rout MP (1995a) Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transport. J Cell Biol 131: 1659–1675PubMedCrossRefGoogle Scholar
  3. Aitchison JD, Rout MP, Marelli M, Blobel G, Wozniak RW (1995b) Two novel related yeast nucleoporins Nup170p and Nup157p: complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. J Cell Biol 131: 1133–1148PubMedCrossRefGoogle Scholar
  4. Aitchison JD, Blobel G, Rout MP (1996) Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science 274: 624–627PubMedCrossRefGoogle Scholar
  5. Akey CW (1990) Visualization of transport-related configurations of the nuclear pore transporter. Biophys J 58: 341–355PubMedCrossRefGoogle Scholar
  6. Akey CW, Goldfarb DS (1989) Protein import through the nuclear pore complex is a multistep process. J Cell Biol 109: 971–982PubMedCrossRefGoogle Scholar
  7. Akey CW, Radermacher M (1993) Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J Cell Biol 122: 1–19PubMedCrossRefGoogle Scholar
  8. Andrulis ED, Neiman AM, Zappulla DC, Sternglanz R (1998) Perinuclear localization of chromatin facilitates transcriptional silencing [published erratum appears in Nature, 1 October 1998, 395(6701):5251. Nature 394: 592–595Google Scholar
  9. Bailer SM, Siniossoglou S, Podtelejnikov A, Hellwig A, Mann M, Hurt E (1998) Nup116p and nup100p are interchangeable through a conserved motif which constitutes a docking site for the mRNA transport factor gle2p. EMBO J 17: 1107–1119PubMedCrossRefGoogle Scholar
  10. Bailer SM, Balduf C, Katahira J, Podtelejnikov A, Rollenhagen C, Mann M, Pante N, Hurt E (2000) Nup116p associates with the Nup82p-Nsplp-Nup159p Nucleoporin Complex. J Biol Chem: 23540–23548Google Scholar
  11. Bangs PL, Sparks CA, Odgren PR, Fey EG (1996) Product of the oncogene-activating gene Tpr is a phosphorylated protein of the nuclear pore complex. J Cell Biochem 61: 48–60PubMedCrossRefGoogle Scholar
  12. Bangs P, Burke B, Powers C, Craig R, Purohit A, Doxsey S (1998) Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export. J Cell Biol 143: 1801–1812PubMedCrossRefGoogle Scholar
  13. Bayliss R, Ribbeck K, Akin D, Kent HM, Feldherr CM, Gorlich D, Stewart M (1999) Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP. J Mol Biol 293: 579–593PubMedCrossRefGoogle Scholar
  14. Belanger KD, Kenna MA, Wei S, Davis LI (1994) Genetic and physical interactions between Srplp and nuclear pore complex proteins Nuplp and Nup2p. J Cell Biol 126: 619–630PubMedCrossRefGoogle Scholar
  15. Belgareh N, Doye V (1997) Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J Cell Biol 136: 747–749PubMedCrossRefGoogle Scholar
  16. Belgareh N, Snay-Hodge C, Pasteau F, Dagher S, Cole CN, Doye V (1998) Functional characterization of a Nup159p-containing nuclear pore subcomplex. Mol Biol Cell 9: 34753492Google Scholar
  17. Berezney R, Mortillaro MJ, Ma H, Wei X, Samarabandu J (1995) The nuclear matrix: a structural milieu for genomic function. Int Rev Cytol 162 A: 1–65Google Scholar
  18. Blobel G (1995) Unidirectional and bidirectional protein traffic across membranes. Cold Spring Harbor Symp Quant Biol 60: 1–10PubMedCrossRefGoogle Scholar
  19. Boulton SJ, Jackson SP (1996) Identification of a Saccharomyces cerevisiae Ku80 homologue: roles in DNA double strand break rejoining and in telomeric maintenance. Nucleic Acids Res 24: 4639–4648PubMedCrossRefGoogle Scholar
  20. Bucci M, Wente SR (1997) In vivo dynamics of nuclear pore complexes in yeast. J Cell Biol 136: 1185–1199PubMedCrossRefGoogle Scholar
  21. Bucci M, Wente SR (1998) A novel fluorescence-based genetic strategy identifies mutants of Sac- charomyces cerevisiae defective for nuclear pore complex assembly. Mol Biol Cell 9: 2439–2461PubMedGoogle Scholar
  22. Buss F, Kent H, Stewart M, Bailer SM, Hanover JA (1994) Role of different domains in the self-association of rat nucleoporin p62. J Cell Sci 107: 631–638PubMedGoogle Scholar
  23. Byrd DA, Sweet DJ, Pante N, Konstantinov KN, Guan T, Saphire AC, Mitchell PJ, Cooper CS, Aebi U, Gerace L (1994) Tpr, a large coiled coil protein whose amino terminus is involved in activation of oncogenic kinases, is localized to the cytoplasmic surface of the nuclear pore complex. J Cell Biol 127: 1515–1526PubMedCrossRefGoogle Scholar
  24. Chiai HJ, Rout MP, Giddings TH, Winey M (1998) Saccharomyces cerevisiae Ndclp is a shared component of nuclear pore complexes and spindle pole bodies. J Cell Biol 143: 1789–1800Google Scholar
  25. Cole CN, Hammell CM (1998) Nucleocytoplasmic transport: driving and directing transport. Curr Biol 8: R368–372PubMedCrossRefGoogle Scholar
  26. Cordes VC, Reidenbach S, Rackwitz HR, Franke WW (1997) Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J Cell Biol 136: 515–529PubMedCrossRefGoogle Scholar
  27. Del Priore V, Snay CA, Bahr A, Cole CN (1996) The product of the Saccharomyces cerevisiae RSS1 gene, identified as a high-copy suppressor of the rat7–1 temperature-sensitive allele of the RAT7/NUP159 nucleoporin, is required for efficient mRNA export. Mol Biol Cell 7: 1601–1621PubMedGoogle Scholar
  28. Delphin C, Guan T, Melchior F, Gerace L (1997) RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex. Mol Biol Cell 8: 2379–2390PubMedGoogle Scholar
  29. Doye V, Hurt EC (1995) Genetic approaches to nuclear pore structure and function. Trends Genet 11: 235–241PubMedCrossRefGoogle Scholar
  30. Doye V, Hurt E (1997) From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol 9: 401–411PubMedCrossRefGoogle Scholar
  31. Doye V, Wepf R, Hurt EC (1994) A novel nuclear pore protein Nup133p with distinct roles in poly(A)+ RNA transport and nuclear pore distribution. EMBO J 13: 6062–6075PubMedGoogle Scholar
  32. Dworetzky SI, Feldherr CM (1988) Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J Cell Biol 106: 575–584PubMedCrossRefGoogle Scholar
  33. Englmeier L, Olivo JC, Mattaj IW (1999) Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr Biol 9: 30–41PubMedCrossRefGoogle Scholar
  34. Fabre E, Hurt E (1997) Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu Rev Genet 31: 277–313PubMedCrossRefGoogle Scholar
  35. Fabre E, Boelens WC, Wimmer C, Mattaj IW, Hurt EC (1994) Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 78: 275–289PubMedCrossRefGoogle Scholar
  36. Fabre E, Schlaich NL, Hurt EC (1995) Nucleocytoplasmic trafficking: what role for repeated motifs in nucleoporins? Cold Spring Harbor Symp Quant Biol 60: 677–685PubMedCrossRefGoogle Scholar
  37. Fahrenkrog B, Hurt EC, Aebi U, Pante N (1998) Molecular architecture of the yeast nuclear pore complex: localization of Nsplp subcomplexes. J Cell Biol 143: 577–588PubMedCrossRefGoogle Scholar
  38. Feldherr CM, Akin D (1991) Signal-mediated nuclear transport in proliferating and growth-arrested BALB/c 3T3 cells. J Cell Biol 115: 933–939PubMedCrossRefGoogle Scholar
  39. Feldherr CM, Akin D (1993) Regulation of nuclear transport in proliferating and quiescent cells. Exp Cell Res 205: 179–186PubMedCrossRefGoogle Scholar
  40. Feldherr CM, Akin D (1994a) Role of nuclear trafficking in regulating cellular activity. Int Rev Cytol 151: 183–228PubMedCrossRefGoogle Scholar
  41. Feldherr CM, Akin D (1994b) Variations in signal-mediated nuclear transport during the cell cycle in BALB/c 3T3 cells. Exp Cell Res 215: 206–210PubMedCrossRefGoogle Scholar
  42. Feldherr CM, Akin D (1997) The location of the transport gate in the nuclear pore complex. J Cell Sci 110: 3065–3070PubMedGoogle Scholar
  43. Feldherr CM, Kallenbach E, Schultz N (1984) Movement of a karyophilic protein through the nuclear pores of oocytes. J Cell Biol 99: 2216–2222PubMedCrossRefGoogle Scholar
  44. Feldherr C, Akin D, Moore MS (1998) The nuclear import factor p10 regulates the functional size of the nuclear pore complex during oogenesis. J Cell Sci 111: 1889–1896PubMedGoogle Scholar
  45. Floer M, Blobel G (1996) The nuclear transport factor karyopherin beta binds stoichiometrically to Ran-GTP and inhibits the Ran GTPase activating protein. J Biol Chem 271: 5313–5316PubMedCrossRefGoogle Scholar
  46. Floer M, Blobel G (1999) Putative reaction intermediates in Crml-mediated nuclear protein export. J Biol Chem 274: 16279–16286PubMedCrossRefGoogle Scholar
  47. Floer M, Blobel G, Rexach M (1997) Disassembly of RanGTP-karyopherin beta complex, an intermediate in nuclear protein import. J Biol Chem 272: 19538–19546PubMedCrossRefGoogle Scholar
  48. Franke WW, Scheer U (1974) Structures and functions of the nuclear envelope. In: Busch H (ed) The cell nucleus. Academic Press, New York, pp 219–347Google Scholar
  49. Galy V, Olivo-Marin JC, Scherthan H, Doye V, Rascalou N, Nehrbass U (2000) Nuclear pore complexes in the organization of silent telomeric chromatin (see comments). Nature 403: 108–112PubMedCrossRefGoogle Scholar
  50. Goldberg MW, Allen TD (1992) High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nudeoplasmic face of the nuclear pores. J Cell Biol 119: 1429–1440PubMedCrossRefGoogle Scholar
  51. Goldberg MW, Allen TD (1996) The nuclear pore complex and lamina: three-dimensional structures and interactions determined by field emission in-lens scanning electron microscopy. J Mol Biol 257: 848–865PubMedCrossRefGoogle Scholar
  52. Goldberg MW, Wiese C, Allen TD, Wilson KL (1997) Dimples, pores, star-rings, and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. J Cell Sci 110: 409–420PubMedGoogle Scholar
  53. Goldstein AL, Snay CA, Heath CV, Cole CN (1996) Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p. Mol Biol Cell 7: 917–934PubMedGoogle Scholar
  54. Gorlich D, Kutay U (1999) Transport between the cell nucleus and the cytoplasm. Annu Rev Cell Dev Biol 15: 607–660PubMedCrossRefGoogle Scholar
  55. Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15: 5584–5594PubMedGoogle Scholar
  56. Gorsch LC, Dockendorff TC, Cole CN (1995) A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J Cell Biol 129: 939–955PubMedCrossRefGoogle Scholar
  57. Gottschling DE, Aparicio OM, Billington BL, Zakian VA (1990) Position effect at S. cerevisiae telomeres: reversible repression of Pol II transcription. Cell 63: 751–762PubMedCrossRefGoogle Scholar
  58. Grandi P, Doye V, Hurt EC (1993) Purification of NSP1 reveals complex formation with “GLFG” nucleoporins and a novel nuclear pore protein NIC96. EMBO J 12: 3061–3071PubMedGoogle Scholar
  59. Grandi P, Emig S, Weise C, Hucho F, Pohl T, Hurt EC (1995a) A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsplp. J Cell Biol 130: 1263–1273PubMedCrossRefGoogle Scholar
  60. Grandi P, Schlaich N, Tekotte H, Hurt EC (1995b) Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsplp, Nup49p and a novel protein Nup57p. EMBO J 14: 76–87PubMedGoogle Scholar
  61. Grandi P, Dang T, Pane N, Shevchenko A, Mann M, Forbes D, Hurt E (1997) Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly. Mol Biol Cell 8: 2017–2038PubMedGoogle Scholar
  62. Guan T, Muller S, Klier G, Pante N, Blevitt JM, Haner M, Paschal B, Aebi U, Gerace L (1995) Structural analysis of the p62 complex, an assembly of 0-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol Biol Cell 6: 1591–1603PubMedGoogle Scholar
  63. Heath CV, Copeland CS, Amberg DC, Del Priore V, Snyder M, Cole CN (1995) Nuclear pore complex clustering and nuclear accumulation of poly(A)+ RNA associated with mutation of the Saccharomyces cerevisiae RAT2/NUP120 gene. J Cell Biol 131: 1677–1697PubMedCrossRefGoogle Scholar
  64. Hinshaw JE, Carragher BO, Milligan RA (1992) Architecture and design of the nuclear pore complex. Cell 69: 1133–1141PubMedCrossRefGoogle Scholar
  65. Ho AK, Raczniak GA, Ives EB, Wente SR (1998) The integral membrane protein snllp is genetically linked to yeast nuclear pore complex function. Mol Biol Cell 9: 355–373PubMedGoogle Scholar
  66. Hood JK, Silver PA (1998) Cselp is required for export of Srplp/Importin-alpha from the nucleus in Saccharomyces cerevisiae (in process citation). J Biol Chem 273: 35142–35146PubMedCrossRefGoogle Scholar
  67. Hu T, Guan T, Gerace L (1996) Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. J Cell Biol 134: 589–601PubMedCrossRefGoogle Scholar
  68. Hurt E, Strasser K, Segref A, Bailer S, Schlaich N, Presutti C, Tollervey D, Jansen R (2000) Mex67p mediates nuclear export of a variety of RNA polymerase II transcripts. J Biol Chem 275: 8361–8368PubMedCrossRefGoogle Scholar
  69. Hurwitz ME, Blobel G (1995) NUP82 is an essential yeast nucleoporin required for poly(A)+ RNA export. J Cell Biol 130: 1275–1281PubMedCrossRefGoogle Scholar
  70. Hurwitz ME, Strambio-de-Castillia C, Blobel G (1998) Two yeast nuclear pore complex proteins involved in mRNA export form a cytoplasmically oriented subcomplex. Proc Natl Acad Sci USA 95: 11241–11245PubMedCrossRefGoogle Scholar
  71. Iovine MK, Wente SR (1997) A nuclear export signal in Kap95p is required for both recycling the import factor and interaction with the nucleoporin GLFG repeat regions of Nup116p and Nup100p. J Cell Biol 137: 797–811PubMedCrossRefGoogle Scholar
  72. Kaffman A, Rank NM, O’Shea EK (1998) Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Psel/Kap121. Genes Dev 12: 2673–2683PubMedCrossRefGoogle Scholar
  73. Katahira J, Strasser K, Podtelejnikov A, Mann M, Jung JU, Hurt E (1999) The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J 18: 2593–2609PubMedCrossRefGoogle Scholar
  74. Kehlenbach RH, Dickmanns A, Kehlenbach A, Guan T, Gerace L (1999) A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export (in process citation). J Cell Biol 145: 645–657PubMedCrossRefGoogle Scholar
  75. Keminer O, Siebrasse JP, Zerf K, Peters R (1999) Optical recording of signal-mediated protein transport through single nuclear pore complexes. Proc Natl Acad Sci USA 96: 1184211847Google Scholar
  76. Kenna MA, Petranka JG, Reilly JL, Davis LI (1996) Yeast Nle3p/Nup170p is required for normal stoichiometry of FG nucleoporins within the nuclear pore complex. Mol Cell Biol 16: 2025–2036PubMedGoogle Scholar
  77. Kiseleva E, Goldberg MW, Daneholt B, Allen TD (1996) RNP export is mediated by structural reorganization of the nuclear pore basket. J Mol Biol 260: 304–311PubMedCrossRefGoogle Scholar
  78. Kiseleva E, Goldberg M, Allen T, Akey C (1998) Active nuclear pore complexes in chironomous: mvisualization of transporter configurations related to mRNP export. J Cell Sci 111: 223–236PubMedGoogle Scholar
  79. Koepp DM, Silver PA (1996) A GTPase controlling nuclear trafficking: running the right way or walking randomly? Cell 87: 1–4CrossRefGoogle Scholar
  80. Kolling R, Nguyen T, Chen EY, Botstein D (1993) A new yeast gene with a myosin-like heptad repeat structure. Mol Gen Genet 237: 359–369PubMedGoogle Scholar
  81. Kosova B, Pante N, Rollenhagen C, Hurt E (1999) Nup192p is a conserved nucleoporin with a pref- erential location at the inner site of the nuclear membrane. J Biol Chem 274: 22646–22651PubMedCrossRefGoogle Scholar
  82. Kosova B, Pante N, Rollenhagen C, Podtelejnikov A, Mann M, Aebi U, Hurt E (2000) Mlp2p, a component of nuclear pore attached intranuclear filaments, associates with nic96p. J Biol Chem 275: 343–350PubMedCrossRefGoogle Scholar
  83. Kraemer DM, Strambio-de-Castillia C, Blobel G, Rout MP (1995) The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate. J Biol Chem 270: 19017–19021PubMedCrossRefGoogle Scholar
  84. Laroche T, Martin SG, Gotta M, Gorham HC, Pryde FE, Louis EJ, Gasser SM (1998) Mutation of yeast Ku genes disrupts the subnuclear organization of telomeres. Curr Biol 8: 653–656PubMedCrossRefGoogle Scholar
  85. Lawrence JB, Singer RH, Marselle LM (1989) Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell 57: 493–502PubMedCrossRefGoogle Scholar
  86. Li O, Heath CV, Amberg DC, Dockendorff TC, Copeland CS, Snyder M, Cole CN (1995) Mutation or deletion of the Saccharomyces cerevisiae RAT3/NUP133 gene causes temperature-dependent nuclear accumulation of poly(A)+ RNA and constitutive clustering of nuclear pore complexes. Mol Biol Cell 6: 401–417PubMedGoogle Scholar
  87. Macaulay C, Forbes DJ (1996) Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA. J Cell Biol 132: 5–20Google Scholar
  88. Maillet L, Boscheron C, Gotta M, Marcand S, Gilson E, Gasser SM (1996) Evidence for silencing compartments within the yeast nucleus: a role for telomere proximity and Sir protein concentration in silencer-mediated repression. Genes Dev 10: 1796–1811PubMedCrossRefGoogle Scholar
  89. Marelli M, Aitchison JD, Wozniak RW (1998) Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J Cell Biol 143: 1813–1830PubMedCrossRefGoogle Scholar
  90. Martin SG, Laroche T, Suka N, Grunstein M, Gasser SM (1999) Relocalization of telomeric Ku and SIR proteins in response to DNA strand breaks in yeast. Cell 97: 621–633PubMedCrossRefGoogle Scholar
  91. Mattaj IW, Englmeier L (1998) Nucleocytoplasmic transport: the soluble phase. Annu Rev Biochem 67: 265–306PubMedCrossRefGoogle Scholar
  92. Maul GG (1977) The nuclear and cytoplasmic pore complex: structure, dynamics, distribution and evolution. Int Rev Cytol Suppl 5: 75–186Google Scholar
  93. Milne GT, Jin S, Shannon KB, Weaver DT (1996) Mutations in two Ku homologs define a DNA end-joining repair pathway in Saccharomyces cerevisiae. Mol Cell Biol 16: 4189–4198PubMedGoogle Scholar
  94. Mishra K, Shore D (1999) Yeast Ku protein plays a direct role in telomeric silencing and coun- teracts inhibition by rif proteins. Curr Biol 9: 1123–1126PubMedCrossRefGoogle Scholar
  95. Murphy R, Watkins JL, Wente SR (1996) GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function. Mol Biol Cell 7: 1921–1937PubMedGoogle Scholar
  96. Mutvei A, Dihlmann S, Herth W, Hurt EC (1992) NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation. Eur J Cell Biol 59: 280–295PubMedGoogle Scholar
  97. Nachury MV, Weis K (1999) The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci USA 96: 9622–9627PubMedCrossRefGoogle Scholar
  98. Nehrbass U, Blobel G (1996) Role of the nuclear transport factor p10 in nuclear import. Science 272: 120–122PubMedCrossRefGoogle Scholar
  99. Nehrbass U, Kern H, Mutvei A, Horstmann H, Marshallsay B, Hurt EC (1990) NSP1: a yeast nuclear envelope protein localized at the nuclear pores exerts its essential function by its carboxyterminal domain. Cell 61: 979–989PubMedCrossRefGoogle Scholar
  100. Nehrbass U, Fabre E, Dihlmann S, Herth W, Hurt EC (1993) Analysis of nucleo-cytoplasmic trans- port in a thermosensitive mutant of nuclear pore protein NSP1. Eur J Cell Biol 62: 1–12PubMedGoogle Scholar
  101. Nehrbass U, Rout MP, Maguire S, Blobel G, Wozniak RW (1996) The yeast nucleoporin Nup 188p interacts genetically and physically with the core structures of the nuclear pore complex. J Cell Biol 133: 1153–1162PubMedCrossRefGoogle Scholar
  102. Neville M, Stutz F, Lee L, Davis LI, Rosbash M (1997) The importin b family member Crmlp bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr Biol 7: 767–775Google Scholar
  103. Nigg EA (1997) Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386: 779–787PubMedCrossRefGoogle Scholar
  104. Ohno M, Fornerod M, Mattaj IW (1998) Nucleocytoplasmic transport: the last 200 nanometers. Cell 92: 327–336PubMedCrossRefGoogle Scholar
  105. Paddy MR (1998) The Tpr protein: linking structure and function in the nuclear interior? Am J Hum Genet 63: 305–310PubMedCrossRefGoogle Scholar
  106. Paine PL, Moore LC, Horowitz SB (1975) Nuclear envelope permeability. Nature 254: 109–114PubMedCrossRefGoogle Scholar
  107. Pemberton LF, Rout MP, Blobel G (1995) Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexes. Proc Natl Acad Sci USA 92: 1187–1191PubMedCrossRefGoogle Scholar
  108. Pemberton LF, Rosenblum JS, Blobel G (1997) A distinct and parallel pathway for the nuclear import of an mRNA-binding protein. J Cell Biol 139: 1645–1653PubMedCrossRefGoogle Scholar
  109. Pemberton LF, Blobel G, Rosenblum IS (1998) Transport routes through the nuclear pore complex. Curr Opin Cell Biol 10: 392–399PubMedCrossRefGoogle Scholar
  110. Radu A, Blobel G, Moore MS (1995) 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 92: 1769–1773PubMedCrossRefGoogle Scholar
  111. Rexach M, Blobel G (1995) Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83: 683–692PubMedCrossRefGoogle Scholar
  112. Ris H (1991) The three dimensional structure of the nuclear pore complexes as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy. EMSA Bull 21: 54–56Google Scholar
  113. Ris H (1997) High-resolution field-emission scanning electron microscopy of nuclear pore complex. Scanning 19: 368–375PubMedCrossRefGoogle Scholar
  114. Rout MP, Blobel G (1993) Isolation of the nuclear pore complex. J Cell Biol 123: 771–783PubMedCrossRefGoogle Scholar
  115. Rout MP, Wente SR (1994) Pores for thought: nuclear pore complex proteins. Trends Cell Biol 4: 357–365PubMedCrossRefGoogle Scholar
  116. Rout MP, Blobel G, Aitchison JD (1997) A distinct nuclear import pathway used by ribosomal proteins. Cell 89: 715–725PubMedCrossRefGoogle Scholar
  117. Rout MP, Aitchison JD, Suprapto A, Hjertaas K, Zhao Y, Chait BT (2000) The yeast nuclear pore complex: composition, architecture, and transport mechanism. J Cell Biol 148: 635–651PubMedCrossRefGoogle Scholar
  118. Ryan KJ, Wente SR (2000) The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm [In process citation]. Curr Opin Cell Biol 12: 361–371PubMedCrossRefGoogle Scholar
  119. Schlaich NL, Hurt EC (1995) Analysis of nucleocytoplasmic transport and nuclear envelope structure in yeast disrupted for the gene encoding the nuclear pore protein Nuplp. Eur J Cell Biol 67: 8–14PubMedGoogle Scholar
  120. Schlaich NL, Haner M, Lustig A, Aebi U, Hurt EC (1997) In vitro reconstitution of a heterotrimeric nucleoporin complex consisting of recombinant Nsplp, Nup49p, and Nup57p. Mol Biol Cell 8: 33–46PubMedGoogle Scholar
  121. Schwoebel ED, Talcott B, Cushman I, Moore MS (1998) Ran-dependent signal-mediated nuclear import does not require GTP hydrolysis by Ran. J Biol Chem 273: 35170–35175PubMedCrossRefGoogle Scholar
  122. Seedorf M, Damelin M, Kahana J, Taura T, Silver P (1999) Interactions between a nuclear transporter and a subset of nuclear pore complex proteins depend on Ran GTPase. Mol Cell Biol 19: 1547–1557PubMedGoogle Scholar
  123. Shah S, Tugendreich S, Forbes D (1998) Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J Cell Biol 141: 31–49PubMedCrossRefGoogle Scholar
  124. Shulga N, Mosammaparast N, Wozniak R, Goldfarb DS (2000) Yeast nucleoporins involved in passive nuclear envelope permeability (in process citation). J Cell Biol 149: 1027–1038PubMedCrossRefGoogle Scholar
  125. Siniossoglou S, Wimmer C, Rieger M, Doye V, Tekotte H, Weise C, Emig S, Segref A, Hurt EC (1996) A novel complex of nucleoporins, which includes Secl3p and a Secl3p homolog, is essential for normal nuclear pores. Cell 84: 265–275PubMedCrossRefGoogle Scholar
  126. Siniossoglou S, Santos-Rosa H, Rappsilber J, Mann M, Hurt E (1998) A novel complex of membrane proteins required for formation of a spherical nucleus. EMBO J 17: 6449–6464PubMedCrossRefGoogle Scholar
  127. Siniossoglou S, Lutzmann M, Santos-Rosa H, Leonard K, Mueller S, Aebi U, Hurt E (2000)Google Scholar
  128. Structure and assembly of the Nup84p complex. J Cell Biol 149:41–54Google Scholar
  129. Solsbacher J, Maurer P, Bischoff FR, Schlenstedt G (1998) Cselp is involved in export of yeast importin alpha from the nucleus. Mol Cell Biol 18: 6805–6815PubMedGoogle Scholar
  130. Strahm Y, Fahrenkrog B, Zenklusen D, Rychner E, Kantor J, Rosbach M, Stutz F (1999) The RNA export factor Glelp is located on the cytoplasmic fibrils of the NPC and physically interacts with the FG-nucleoporin Riplp, the DEAD-box protein Rat8p/Dbp5p and a new protein Ymr 255p. EMBO J 18: 5761–5777PubMedCrossRefGoogle Scholar
  131. Strambio-de-Castillia C, Blobel G, Rout MP (1995) Isolation and characterization of nuclear envelopes from the yeast Saccharomyces. J Cell Biol 131: 19–31Google Scholar
  132. Strambio-de-Castillia C, Blobel G, Rout MP (1999) Proteins connecting the nuclear pore complex with the nuclear interior. J Cell Biol 144: 839–855PubMedCrossRefGoogle Scholar
  133. Stutz F, Kantor J, Zhang D, McCarthy T, Neville M, Rosbash M (1997) The yeast nucleoporin rip 1p contributes to multiple export pathways with no essential role for its FG-repeat region. Genes Dev 11: 2857–2868PubMedCrossRefGoogle Scholar
  134. Tcheperegine SE, Marelli M, Wozniak RW (1999) Topology and functional domains of the yeast pore membrane protein Pom152p. J Biol Chem 274: 5252–5258PubMedCrossRefGoogle Scholar
  135. Titov AA, Blobel G (1999) The karyopherin Kap122p/Pdr6p imports both subunits of the transcription factor IIA into the nucleus. J Cell Biol 147: 235–246PubMedCrossRefGoogle Scholar
  136. Unwin PN, Milligan RA (1982) A large particle associated with the perimeter of the nuclear pore complex. J Cell Biol 93: 63–75PubMedCrossRefGoogle Scholar
  137. Wente SR (2000) Gatekeepers of the nucleus. Science 288: 1374–1377PubMedCrossRefGoogle Scholar
  138. Wente SR, Blobel G (1994) NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine ( GLFG) nucleoporin required for nuclear envelope structure. J Cell Biol 125: 955–969Google Scholar
  139. Wente SR, Gasser SM, Caplan AJ (1998) The nucleus and nucleocytoplasmic transport in Saccharomyces cerevisiae. In: Broach JR, Jones E, Pringle J (eds) The molecular and cellular biology of the yeast Saccharomyces. Cold Spring Harbor Press, Cold Spring Harbor, NYGoogle Scholar
  140. Winey M, Hoyt MA, Chan C, Goetsch L, Botstein D (1993) NDC1: a nuclear periphery component required for yeast spindle pole body duplication. J Cell Biol 122: 743–751PubMedCrossRefGoogle Scholar
  141. Winey M, Yarar D, Giddings TH Jr, Mastronarde DN (1997) Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes. Mol Biol Cell 8: 2119–2132PubMedGoogle Scholar
  142. Winzeler EA, Shoemaker DD, Astromoff A, Liang H, Anderson K, Andre B, Bangham R, Benito R, Boeke JD, Bussey H, Chu AM, Connelly C, Davis K, Dietrich F, Dow SW, El Bakkoury M, Foury F, Friend SH, Gentalen E, Giaever G, Hegemann JH, Jones T, Laub M, Liao H, Davis RW et al. (1999) Functional characterization of the S. cerevisiae genome by gene deletion and parallel analysis. Science 285: 901–906PubMedCrossRefGoogle Scholar
  143. Wozniak RW, Blobel G, Rout MP (1994) P0M152 is an integral membrane protein of the pore membrane domain of the nuclear envelope. J Cell Biol 125: 31–42PubMedCrossRefGoogle Scholar
  144. Wozniak RW, Rout MP, Aitchison JD (1998) Karyopherins and kissing cousins. Trends Cell Biol 8: 184–188PubMedCrossRefGoogle Scholar
  145. Xing Y, Johnson CV, Dobner PR, Lawrence JB (1993) Higher level organization of individual gene transcription and RNA splicing. Science 259: 1326–1330PubMedCrossRefGoogle Scholar
  146. Yang Q, Rout MP, Akey CW (1998) Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol Cell 1: 223–234PubMedCrossRefGoogle Scholar
  147. Zabel U, Doye V, Tekotte H, Wepf R, Grandi P, Hurt EC (1996) Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J Cell Biol 133: 1141–1152PubMedCrossRefGoogle Scholar
  148. Zachar Z, Kramer J, Mims IP, Bingham PM (1993) Evidence for channeled diffusion of pre-mRNAs during nuclear RNA transport in metazoans. J Cell Biol 121: 729–742PubMedCrossRefGoogle Scholar
  149. Zimowska G, Aris JP, Paddy MR (1997) A Drosophila Tpr protein homolog is localized both in the extrachromosomal channel network and to nuclear pore complexes. J Cell Sci 110: 927–944PubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2002

Authors and Affiliations

  • Caterina Strambio-de-Castillia
    • 1
  • Michael P. Rout
    • 1
  1. 1.The Laboratory of Cellular and Structural BiologyThe Rockefeller UniversityNew YorkUSA

Personalised recommendations