Skip to main content
NCBI home page
RNA logoLink to RNA
. 1998 Apr;4(4):351–364.

Transport of macromolecules between the nucleus and the cytoplasm.

E Izaurralde 1, S Adam 1
PMCID: PMC1369623  PMID: 9630243

Abstract

Nuclear transport is an energy-dependent process mediated by saturable receptors. Import and export receptors are thought to recognize and bind to nuclear localization signals or nuclear export signals, respectively, in the transported molecules. The receptor-substrate interaction can be direct or mediated by an additional adapter protein. The transport receptors dock their cargoes to the nuclear pore complexes (NPC) and facilitate their translocation through the NPC. After delivering their cargoes, the receptors are recycled to initiate additional rounds of transport. Because a transport event for a cargo molecule is unidirectional, the transport receptors engage in asymmetric cycles of translocation across the NPC. The GTPase Ran acts as a molecular switch for receptor-cargo interaction and imparts directionality to the transport process. Recently, the combined use of different in vitro and in vivo approaches has led to the characterization of novel import and export signals and to the identification of the first nuclear import and export receptors.

Full Text

The Full Text of this article is available as a PDF (204.5 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Adachi Y., Yanagida M. Higher order chromosome structure is affected by cold-sensitive mutations in a Schizosaccharomyces pombe gene crm1+ which encodes a 115-kD protein preferentially localized in the nucleus and its periphery. J Cell Biol. 1989 Apr;108(4):1195–1207. doi: 10.1083/jcb.108.4.1195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Adam E. J., Adam S. A. Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J Cell Biol. 1994 May;125(3):547–555. doi: 10.1083/jcb.125.3.547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Aitchison J. D., Blobel G., Rout M. P. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science. 1996 Oct 25;274(5287):624–627. doi: 10.1126/science.274.5287.624. [DOI] [PubMed] [Google Scholar]
  4. Bastos R., Lin A., Enarson M., Burke B. Targeting and function in mRNA export of nuclear pore complex protein Nup153. J Cell Biol. 1996 Sep;134(5):1141–1156. doi: 10.1083/jcb.134.5.1141. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bataillé N., Helser T., Fried H. M. Cytoplasmic transport of ribosomal subunits microinjected into the Xenopus laevis oocyte nucleus: a generalized, facilitated process. J Cell Biol. 1990 Oct;111(4):1571–1582. doi: 10.1083/jcb.111.4.1571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Bischoff F. R., Klebe C., Kretschmer J., Wittinghofer A., Ponstingl H. RanGAP1 induces GTPase activity of nuclear Ras-related Ran. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2587–2591. doi: 10.1073/pnas.91.7.2587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Bischoff F. R., Krebber H., Kempf T., Hermes I., Ponstingl H. Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. Proc Natl Acad Sci U S A. 1995 Feb 28;92(5):1749–1753. doi: 10.1073/pnas.92.5.1749. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bischoff F. R., Krebber H., Smirnova E., Dong W., Ponstingl H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 1995 Feb 15;14(4):705–715. doi: 10.1002/j.1460-2075.1995.tb07049.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bogerd H. P., Fridell R. A., Benson R. E., Hua J., Cullen B. R. Protein sequence requirements for function of the human T-cell leukemia virus type 1 Rex nuclear export signal delineated by a novel in vivo randomization-selection assay. Mol Cell Biol. 1996 Aug;16(8):4207–4214. doi: 10.1128/mcb.16.8.4207. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Bogerd H. P., Fridell R. A., Madore S., Cullen B. R. Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins. Cell. 1995 Aug 11;82(3):485–494. doi: 10.1016/0092-8674(95)90437-9. [DOI] [PubMed] [Google Scholar]
  11. Brinkmann U., Brinkmann E., Gallo M., Scherf U., Pastan I. Role of CAS, a human homologue to the yeast chromosome segregation gene CSE1, in toxin and tumor necrosis factor mediated apoptosis. Biochemistry. 1996 May 28;35(21):6891–6899. doi: 10.1021/bi952829+. [DOI] [PubMed] [Google Scholar]
  12. Cheng Y., Dahlberg J. E., Lund E. Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport. Science. 1995 Mar 24;267(5205):1807–1810. doi: 10.1126/science.7534442. [DOI] [PubMed] [Google Scholar]
  13. Chi N. C., Adam E. J., Visser G. D., Adam S. A. RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import. J Cell Biol. 1996 Nov;135(3):559–569. doi: 10.1083/jcb.135.3.559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Colot H. V., Stutz F., Rosbash M. The yeast splicing factor Mud13p is a commitment complex component and corresponds to CBP20, the small subunit of the nuclear cap-binding complex. Genes Dev. 1996 Jul 1;10(13):1699–1708. doi: 10.1101/gad.10.13.1699. [DOI] [PubMed] [Google Scholar]
  15. Coutavas E., Ren M., Oppenheim J. D., D'Eustachio P., Rush M. G. Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4. Nature. 1993 Dec 9;366(6455):585–587. doi: 10.1038/366585a0. [DOI] [PubMed] [Google Scholar]
  16. Cullen B. R., Malim M. H. The HIV-1 Rev protein: prototype of a novel class of eukaryotic post-transcriptional regulators. Trends Biochem Sci. 1991 Sep;16(9):346–350. doi: 10.1016/0968-0004(91)90141-h. [DOI] [PubMed] [Google Scholar]
  17. Daneholt B. A look at messenger RNP moving through the nuclear pore. Cell. 1997 Mar 7;88(5):585–588. doi: 10.1016/s0092-8674(00)81900-5. [DOI] [PubMed] [Google Scholar]
  18. DeLeon D. V., Cox K. H., Angerer L. M., Angerer R. C. Most early-variant histone mRNA is contained in the pronucleus of sea urchin eggs. Dev Biol. 1983 Nov;100(1):197–206. doi: 10.1016/0012-1606(83)90211-7. [DOI] [PubMed] [Google Scholar]
  19. Del Priore V., Snay C. A., Bahr A., Cole C. N. 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. 1996 Oct;7(10):1601–1621. doi: 10.1091/mbc.7.10.1601. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Dingwall C., Laskey R. A. Nuclear targeting sequences--a consensus? Trends Biochem Sci. 1991 Dec;16(12):478–481. doi: 10.1016/0968-0004(91)90184-w. [DOI] [PubMed] [Google Scholar]
  21. Doye V., Hurt E. From nucleoporins to nuclear pore complexes. Curr Opin Cell Biol. 1997 Jun;9(3):401–411. doi: 10.1016/s0955-0674(97)80014-2. [DOI] [PubMed] [Google Scholar]
  22. Dreyfuss G., Matunis M. J., Piñol-Roma S., Burd C. G. hnRNP proteins and the biogenesis of mRNA. Annu Rev Biochem. 1993;62:289–321. doi: 10.1146/annurev.bi.62.070193.001445. [DOI] [PubMed] [Google Scholar]
  23. Ernst R. K., Bray M., Rekosh D., Hammarskjöld M. L. A structured retroviral RNA element that mediates nucleocytoplasmic export of intron-containing RNA. Mol Cell Biol. 1997 Jan;17(1):135–144. doi: 10.1128/mcb.17.1.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Featherstone C., Darby M. K., Gerace L. A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo. J Cell Biol. 1988 Oct;107(4):1289–1297. doi: 10.1083/jcb.107.4.1289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Fischer U., Huber J., Boelens W. C., Mattaj I. W., Lührmann R. The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell. 1995 Aug 11;82(3):475–483. doi: 10.1016/0092-8674(95)90436-0. [DOI] [PubMed] [Google Scholar]
  26. Fischer U., Lührmann R. An essential signaling role for the m3G cap in the transport of U1 snRNP to the nucleus. Science. 1990 Aug 17;249(4970):786–790. doi: 10.1126/science.2143847. [DOI] [PubMed] [Google Scholar]
  27. Fischer U., Sumpter V., Sekine M., Satoh T., Lührmann R. Nucleo-cytoplasmic transport of U snRNPs: definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap. EMBO J. 1993 Feb;12(2):573–583. doi: 10.1002/j.1460-2075.1993.tb05689.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Flach J., Bossie M., Vogel J., Corbett A., Jinks T., Willins D. A., Silver P. A. A yeast RNA-binding protein shuttles between the nucleus and the cytoplasm. Mol Cell Biol. 1994 Dec;14(12):8399–8407. doi: 10.1128/mcb.14.12.8399. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Fornerod M., Ohno M., Yoshida M., Mattaj I. W. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997 Sep 19;90(6):1051–1060. doi: 10.1016/s0092-8674(00)80371-2. [DOI] [PubMed] [Google Scholar]
  30. Fornerod M., van Deursen J., van Baal S., Reynolds A., Davis D., Murti K. G., Fransen J., Grosveld G. The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J. 1997 Feb 17;16(4):807–816. doi: 10.1093/emboj/16.4.807. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Fresco L. D., Buratowski S. Conditional mutants of the yeast mRNA capping enzyme show that the cap enhances, but is not required for, mRNA splicing. RNA. 1996 Jun;2(6):584–596. [PMC free article] [PubMed] [Google Scholar]
  32. Fridell R. A., Fischer U., Lührmann R., Meyer B. E., Meinkoth J. L., Malim M. H., Cullen B. R. Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type 1 Rev. Proc Natl Acad Sci U S A. 1996 Apr 2;93(7):2936–2940. doi: 10.1073/pnas.93.7.2936. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Fridell R. A., Truant R., Thorne L., Benson R. E., Cullen B. R. Nuclear import of hnRNP A1 is mediated by a novel cellular cofactor related to karyopherin-beta. J Cell Sci. 1997 Jun;110(Pt 11):1325–1331. doi: 10.1242/jcs.110.11.1325. [DOI] [PubMed] [Google Scholar]
  34. Fritz C. C., Green M. R. HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs. Curr Biol. 1996 Jul 1;6(7):848–854. doi: 10.1016/s0960-9822(02)00608-5. [DOI] [PubMed] [Google Scholar]
  35. Fritz C. C., Zapp M. L., Green M. R. A human nucleoporin-like protein that specifically interacts with HIV Rev. Nature. 1995 Aug 10;376(6540):530–533. doi: 10.1038/376530a0. [DOI] [PubMed] [Google Scholar]
  36. Fukuda M., Gotoh I., Gotoh Y., Nishida E. Cytoplasmic localization of mitogen-activated protein kinase kinase directed by its NH2-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export signal. J Biol Chem. 1996 Aug 16;271(33):20024–20028. doi: 10.1074/jbc.271.33.20024. [DOI] [PubMed] [Google Scholar]
  37. Goldfarb D. S. Whose finger is on the switch? Science. 1997 Jun 20;276(5320):1814–1816. doi: 10.1126/science.276.5320.1814. [DOI] [PubMed] [Google Scholar]
  38. Guddat U., Bakken A. H., Pieler T. Protein-mediated nuclear export of RNA: 5S rRNA containing small RNPs in xenopus oocytes. Cell. 1990 Feb 23;60(4):619–628. doi: 10.1016/0092-8674(90)90665-2. [DOI] [PubMed] [Google Scholar]
  39. Görlich D., Dabrowski M., Bischoff F. R., Kutay U., Bork P., Hartmann E., Prehn S., Izaurralde E. A novel class of RanGTP binding proteins. J Cell Biol. 1997 Jul 14;138(1):65–80. doi: 10.1083/jcb.138.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Görlich D., Henklein P., Laskey R. A., Hartmann E. A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus. EMBO J. 1996 Apr 15;15(8):1810–1817. [PMC free article] [PubMed] [Google Scholar]
  41. Görlich D., Kostka S., Kraft R., Dingwall C., Laskey R. A., Hartmann E., Prehn S. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr Biol. 1995 Apr 1;5(4):383–392. doi: 10.1016/s0960-9822(95)00079-0. [DOI] [PubMed] [Google Scholar]
  42. Görlich D., Kraft R., Kostka S., Vogel F., Hartmann E., Laskey R. A., Mattaj I. W., Izaurralde E. Importin provides a link between nuclear protein import and U snRNA export. Cell. 1996 Oct 4;87(1):21–32. doi: 10.1016/s0092-8674(00)81319-7. [DOI] [PubMed] [Google Scholar]
  43. Görlich D., Mattaj I. W. Nucleocytoplasmic transport. Science. 1996 Mar 15;271(5255):1513–1518. doi: 10.1126/science.271.5255.1513. [DOI] [PubMed] [Google Scholar]
  44. Görlich D. Nuclear protein import. Curr Opin Cell Biol. 1997 Jun;9(3):412–419. doi: 10.1016/s0955-0674(97)80015-4. [DOI] [PubMed] [Google Scholar]
  45. Görlich D., Panté N., Kutay U., Aebi U., Bischoff F. R. Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 1996 Oct 15;15(20):5584–5594. [PMC free article] [PubMed] [Google Scholar]
  46. Hamm J., Darzynkiewicz E., Tahara S. M., Mattaj I. W. The trimethylguanosine cap structure of U1 snRNA is a component of a bipartite nuclear targeting signal. Cell. 1990 Aug 10;62(3):569–577. doi: 10.1016/0092-8674(90)90021-6. [DOI] [PubMed] [Google Scholar]
  47. Hopper A. K., Traglia H. M., Dunst R. W. The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus. J Cell Biol. 1990 Aug;111(2):309–321. doi: 10.1083/jcb.111.2.309. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Iovine M. K., Watkins J. L., Wente S. R. The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J Cell Biol. 1995 Dec;131(6 Pt 2):1699–1713. doi: 10.1083/jcb.131.6.1699. [DOI] [PMC free article] [PubMed] [Google Scholar]
  49. Izaurralde E., Jarmolowski A., Beisel C., Mattaj I. W., Dreyfuss G., Fischer U. A role for the M9 transport signal of hnRNP A1 in mRNA nuclear export. J Cell Biol. 1997 Apr 7;137(1):27–35. doi: 10.1083/jcb.137.1.27. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Izaurralde E., Kutay U., von Kobbe C., Mattaj I. W., Görlich D. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 1997 Nov 3;16(21):6535–6547. doi: 10.1093/emboj/16.21.6535. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Izaurralde E., Lewis J., Gamberi C., Jarmolowski A., McGuigan C., Mattaj I. W. A cap-binding protein complex mediating U snRNA export. Nature. 1995 Aug 24;376(6542):709–712. doi: 10.1038/376709a0. [DOI] [PubMed] [Google Scholar]
  52. Izaurralde E., Lewis J., McGuigan C., Jankowska M., Darzynkiewicz E., Mattaj I. W. A nuclear cap binding protein complex involved in pre-mRNA splicing. Cell. 1994 Aug 26;78(4):657–668. doi: 10.1016/0092-8674(94)90530-4. [DOI] [PubMed] [Google Scholar]
  53. Jarmolowski A., Boelens W. C., Izaurralde E., Mattaj I. W. Nuclear export of different classes of RNA is mediated by specific factors. J Cell Biol. 1994 Mar;124(5):627–635. doi: 10.1083/jcb.124.5.627. [DOI] [PMC free article] [PubMed] [Google Scholar]
  54. Kalderon D., Roberts B. L., Richardson W. D., Smith A. E. A short amino acid sequence able to specify nuclear location. Cell. 1984 Dec;39(3 Pt 2):499–509. doi: 10.1016/0092-8674(84)90457-4. [DOI] [PubMed] [Google Scholar]
  55. Kambach C., Mattaj I. W. Intracellular distribution of the U1A protein depends on active transport and nuclear binding to U1 snRNA. J Cell Biol. 1992 Jul;118(1):11–21. doi: 10.1083/jcb.118.1.11. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Kataoka N., Ohno M., Kangawa K., Tokoro Y., Shimura Y. Cloning of a complementary DNA encoding an 80 kilodalton nuclear cap binding protein. Nucleic Acids Res. 1994 Sep 25;22(19):3861–3865. doi: 10.1093/nar/22.19.3861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  57. Klebe C., Bischoff F. R., Ponstingl H., Wittinghofer A. Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry. 1995 Jan 17;34(2):639–647. doi: 10.1021/bi00002a031. [DOI] [PubMed] [Google Scholar]
  58. Kutay U., Bischoff F. R., Kostka S., Kraft R., Görlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell. 1997 Sep 19;90(6):1061–1071. doi: 10.1016/s0092-8674(00)80372-4. [DOI] [PubMed] [Google Scholar]
  59. Lanford R. E., Butel J. S. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell. 1984 Jul;37(3):801–813. doi: 10.1016/0092-8674(84)90415-x. [DOI] [PubMed] [Google Scholar]
  60. Lee M. S., Henry M., Silver P. A. A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Genes Dev. 1996 May 15;10(10):1233–1246. doi: 10.1101/gad.10.10.1233. [DOI] [PubMed] [Google Scholar]
  61. Legrain P., Rosbash M. Some cis- and trans-acting mutants for splicing target pre-mRNA to the cytoplasm. Cell. 1989 May 19;57(4):573–583. doi: 10.1016/0092-8674(89)90127-x. [DOI] [PubMed] [Google Scholar]
  62. Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell. 1997 Jan 10;88(1):97–107. doi: 10.1016/s0092-8674(00)81862-0. [DOI] [PubMed] [Google Scholar]
  63. Malim M. H., Hauber J., Le S. Y., Maizel J. V., Cullen B. R. The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature. 1989 Mar 16;338(6212):254–257. doi: 10.1038/338254a0. [DOI] [PubMed] [Google Scholar]
  64. Matunis M. J., 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 Dec;135(6 Pt 1):1457–1470. doi: 10.1083/jcb.135.6.1457. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. 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. 1995 Nov;131(3):571–581. doi: 10.1083/jcb.131.3.571. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Melchior F., Weber K., Gerke V. A functional homologue of the RNA1 gene product in Schizosaccharomyces pombe: purification, biochemical characterization, and identification of a leucine-rich repeat motif. Mol Biol Cell. 1993 Jun;4(6):569–581. doi: 10.1091/mbc.4.6.569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Michael W. M., Choi M., Dreyfuss G. A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell. 1995 Nov 3;83(3):415–422. doi: 10.1016/0092-8674(95)90119-1. [DOI] [PubMed] [Google Scholar]
  68. Michael W. M., Eder P. S., Dreyfuss G. The K nuclear shuttling domain: a novel signal for nuclear import and nuclear export in the hnRNP K protein. EMBO J. 1997 Jun 16;16(12):3587–3598. doi: 10.1093/emboj/16.12.3587. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Moore M. S., Blobel G. The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature. 1993 Oct 14;365(6447):661–663. doi: 10.1038/365661a0. [DOI] [PubMed] [Google Scholar]
  70. Moreland R. B., Nam H. G., Hereford L. M., Fried H. M. Identification of a nuclear localization signal of a yeast ribosomal protein. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6561–6565. doi: 10.1073/pnas.82.19.6561. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Moroianu J., Hijikata M., Blobel G., Radu A. Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. Proc Natl Acad Sci U S A. 1995 Jul 3;92(14):6532–6536. doi: 10.1073/pnas.92.14.6532. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Murphy R., Wente S. R. An RNA-export mediator with an essential nuclear export signal. Nature. 1996 Sep 26;383(6598):357–360. doi: 10.1038/383357a0. [DOI] [PubMed] [Google Scholar]
  73. Nakielny S., Dreyfuss G. Nuclear export of proteins and RNAs. Curr Opin Cell Biol. 1997 Jun;9(3):420–429. doi: 10.1016/s0955-0674(97)80016-6. [DOI] [PubMed] [Google Scholar]
  74. Nakielny S., Dreyfuss G. The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals. J Cell Biol. 1996 Sep;134(6):1365–1373. doi: 10.1083/jcb.134.6.1365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  75. Nakielny S., Siomi M. C., Siomi H., Michael W. M., Pollard V., Dreyfuss G. Transportin: nuclear transport receptor of a novel nuclear protein import pathway. Exp Cell Res. 1996 Dec 15;229(2):261–266. doi: 10.1006/excr.1996.0369. [DOI] [PubMed] [Google Scholar]
  76. Nehrbass U., Blobel G. Role of the nuclear transport factor p10 in nuclear import. Science. 1996 Apr 5;272(5258):120–122. doi: 10.1126/science.272.5258.120. [DOI] [PubMed] [Google Scholar]
  77. Neuman de Vegvar H. E., Dahlberg J. E. Nucleocytoplasmic transport and processing of small nuclear RNA precursors. Mol Cell Biol. 1990 Jul;10(7):3365–3375. doi: 10.1128/mcb.10.7.3365. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Neville M., Stutz F., Lee L., Davis L. I., Rosbash M. The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr Biol. 1997 Oct 1;7(10):767–775. doi: 10.1016/s0960-9822(06)00335-6. [DOI] [PubMed] [Google Scholar]
  79. Newmeyer D. D., Forbes D. J. Nuclear import can be separated into distinct steps in vitro: nuclear pore binding and translocation. Cell. 1988 Mar 11;52(5):641–653. doi: 10.1016/0092-8674(88)90402-3. [DOI] [PubMed] [Google Scholar]
  80. Nigg E. A. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature. 1997 Apr 24;386(6627):779–787. doi: 10.1038/386779a0. [DOI] [PubMed] [Google Scholar]
  81. Nishi K., Yoshida M., Fujiwara D., Nishikawa M., Horinouchi S., Beppu T. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J Biol Chem. 1994 Mar 4;269(9):6320–6324. [PubMed] [Google Scholar]
  82. Ohtsubo M., Okazaki H., Nishimoto T. The RCC1 protein, a regulator for the onset of chromosome condensation locates in the nucleus and binds to DNA. J Cell Biol. 1989 Oct;109(4 Pt 1):1389–1397. doi: 10.1083/jcb.109.4.1389. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Palacios I., Hetzer M., Adam S. A., Mattaj I. W. Nuclear import of U snRNPs requires importin beta. EMBO J. 1997 Nov 17;16(22):6783–6792. doi: 10.1093/emboj/16.22.6783. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Panté N., Aebi U. Sequential binding of import ligands to distinct nucleopore regions during their nuclear import. Science. 1996 Sep 20;273(5282):1729–1732. doi: 10.1126/science.273.5282.1729. [DOI] [PubMed] [Google Scholar]
  85. Panté N., Aebi U. The nuclear pore complex. J Cell Biol. 1993 Sep;122(5):977–984. doi: 10.1083/jcb.122.5.977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Paschal B. M., Gerace L. Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J Cell Biol. 1995 May;129(4):925–937. doi: 10.1083/jcb.129.4.925. [DOI] [PMC free article] [PubMed] [Google Scholar]
  87. Pasquinelli A. E., Ernst R. K., Lund E., Grimm C., Zapp M. L., Rekosh D., Hammarskjöld M. L., Dahlberg J. E. The constitutive transport element (CTE) of Mason-Pfizer monkey virus (MPMV) accesses a cellular mRNA export pathway. EMBO J. 1997 Dec 15;16(24):7500–7510. doi: 10.1093/emboj/16.24.7500. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Piñol-Roma S., Dreyfuss G. Transcription-dependent and transcription-independent nuclear transport of hnRNP proteins. Science. 1991 Jul 19;253(5017):312–314. doi: 10.1126/science.1857966. [DOI] [PubMed] [Google Scholar]
  89. Pokrywka N. J., Goldfarb D. S. Nuclear export pathways of tRNA and 40 S ribosomes include both common and specific intermediates. J Biol Chem. 1995 Feb 24;270(8):3619–3624. doi: 10.1074/jbc.270.8.3619. [DOI] [PubMed] [Google Scholar]
  90. Pollard V. W., Michael W. M., Nakielny S., Siomi M. C., Wang F., Dreyfuss G. A novel receptor-mediated nuclear protein import pathway. Cell. 1996 Sep 20;86(6):985–994. doi: 10.1016/s0092-8674(00)80173-7. [DOI] [PubMed] [Google Scholar]
  91. Powers M. A., Forbes D. J., Dahlberg J. E., Lund E. The vertebrate GLFG nucleoporin, Nup98, is an essential component of multiple RNA export pathways. J Cell Biol. 1997 Jan 27;136(2):241–250. doi: 10.1083/jcb.136.2.241. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Radu A., Moore M. S., Blobel G. The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell. 1995 Apr 21;81(2):215–222. doi: 10.1016/0092-8674(95)90331-3. [DOI] [PubMed] [Google Scholar]
  93. Rexach M., Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 1995 Dec 1;83(5):683–692. doi: 10.1016/0092-8674(95)90181-7. [DOI] [PubMed] [Google Scholar]
  94. Richards S. A., Carey K. L., Macara I. G. Requirement of guanosine triphosphate-bound ran for signal-mediated nuclear protein export. Science. 1997 Jun 20;276(5320):1842–1844. doi: 10.1126/science.276.5320.1842. [DOI] [PubMed] [Google Scholar]
  95. Richards S. A., Lounsbury K. M., Carey K. L., Macara I. G. A nuclear export signal is essential for the cytosolic localization of the Ran binding protein, RanBP1. J Cell Biol. 1996 Sep;134(5):1157–1168. doi: 10.1083/jcb.134.5.1157. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Richardson W. D., Mills A. D., Dilworth S. M., Laskey R. A., Dingwall C. Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translocation through nuclear pores. Cell. 1988 Mar 11;52(5):655–664. doi: 10.1016/0092-8674(88)90403-5. [DOI] [PubMed] [Google Scholar]
  97. Rout M. P., Blobel G., Aitchison J. D. A distinct nuclear import pathway used by ribosomal proteins. Cell. 1997 May 30;89(5):715–725. doi: 10.1016/s0092-8674(00)80254-8. [DOI] [PubMed] [Google Scholar]
  98. Rout M. P., Blobel G. Isolation of the yeast nuclear pore complex. J Cell Biol. 1993 Nov;123(4):771–783. doi: 10.1083/jcb.123.4.771. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Russell I., Tollervey D. Yeast Nop3p has structural and functional similarities to mammalian pre-mRNA binding proteins. Eur J Cell Biol. 1995 Mar;66(3):293–301. [PubMed] [Google Scholar]
  100. Russo G., Ricciardelli G., Pietropaolo C. Different domains cooperate to target the human ribosomal L7a protein to the nucleus and to the nucleoli. J Biol Chem. 1997 Feb 21;272(8):5229–5235. doi: 10.1074/jbc.272.8.5229. [DOI] [PubMed] [Google Scholar]
  101. Saavedra C. A., Hammell C. M., Heath C. V., Cole C. N. Yeast heat shock mRNAs are exported through a distinct pathway defined by Rip1p. Genes Dev. 1997 Nov 1;11(21):2845–2856. doi: 10.1101/gad.11.21.2845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  102. Saavedra C., Felber B., Izaurralde E. The simian retrovirus-1 constitutive transport element, unlike the HIV-1 RRE, uses factors required for cellular mRNA export. Curr Biol. 1997 Sep 1;7(9):619–628. doi: 10.1016/s0960-9822(06)00288-0. [DOI] [PubMed] [Google Scholar]
  103. Saavedra C., Tung K. S., Amberg D. C., Hopper A. K., Cole C. N. Regulation of mRNA export in response to stress in Saccharomyces cerevisiae. Genes Dev. 1996 Jul 1;10(13):1608–1620. doi: 10.1101/gad.10.13.1608. [DOI] [PubMed] [Google Scholar]
  104. Saitoh H., Pu R., Cavenagh M., Dasso M. RanBP2 associates with Ubc9p and a modified form of RanGAP1. Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3736–3741. doi: 10.1073/pnas.94.8.3736. [DOI] [PMC free article] [PubMed] [Google Scholar]
  105. Schaap P. J., van't Riet J., Woldringh C. L., Raué H. A. Identification and functional analysis of the nuclear localization signals of ribosomal protein L25 from Saccharomyces cerevisiae. J Mol Biol. 1991 Sep 5;221(1):225–237. doi: 10.1016/0022-2836(91)80216-h. [DOI] [PubMed] [Google Scholar]
  106. Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U., Görlich D., Ponstingl H., Bischoff F. R. Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal protein L25 into the nucleus. EMBO J. 1997 Oct 15;16(20):6237–6249. doi: 10.1093/emboj/16.20.6237. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Schmidt C., Lipsius E., Kruppa J. Nuclear and nucleolar targeting of human ribosomal protein S6. Mol Biol Cell. 1995 Dec;6(12):1875–1885. doi: 10.1091/mbc.6.12.1875. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Segref A., Sharma K., Doye V., Hellwig A., Huber J., Lührmann R., Hurt E. Mex67p, a novel factor for nuclear mRNA export, binds to both poly(A)+ RNA and nuclear pores. EMBO J. 1997 Jun 2;16(11):3256–3271. doi: 10.1093/emboj/16.11.3256. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Showman R. M., Wells D. E., Anstrom J., Hursh D. A., Raff R. A. Message-specific sequestration of maternal histone mRNA in the sea urchin egg. Proc Natl Acad Sci U S A. 1982 Oct;79(19):5944–5947. doi: 10.1073/pnas.79.19.5944. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Singleton D. R., Chen S., Hitomi M., Kumagai C., Tartakoff A. M. A yeast protein that bidirectionally affects nucleocytoplasmic transport. J Cell Sci. 1995 Jan;108(Pt 1):265–272. doi: 10.1242/jcs.108.1.265. [DOI] [PubMed] [Google Scholar]
  111. Siomi H., Dreyfuss G. A nuclear localization domain in the hnRNP A1 protein. J Cell Biol. 1995 May;129(3):551–560. doi: 10.1083/jcb.129.3.551. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Stade K., Ford C. S., Guthrie C., Weis K. Exportin 1 (Crm1p) is an essential nuclear export factor. Cell. 1997 Sep 19;90(6):1041–1050. doi: 10.1016/s0092-8674(00)80370-0. [DOI] [PubMed] [Google Scholar]
  113. Stutz F., Izaurralde E., Mattaj I. W., Rosbash M. A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus. Mol Cell Biol. 1996 Dec;16(12):7144–7150. doi: 10.1128/mcb.16.12.7144. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Stutz F., Kantor J., Zhang D., McCarthy T., Neville M., Rosbash M. The yeast nucleoporin rip1p contributes to multiple export pathways with no essential role for its FG-repeat region. Genes Dev. 1997 Nov 1;11(21):2857–2868. doi: 10.1101/gad.11.21.2857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. Stutz F., Neville M., Rosbash M. Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell. 1995 Aug 11;82(3):495–506. doi: 10.1016/0092-8674(95)90438-7. [DOI] [PubMed] [Google Scholar]
  116. Sweet D. J., Gerace L. A GTPase distinct from Ran is involved in nuclear protein import. J Cell Biol. 1996 Jun;133(5):971–983. doi: 10.1083/jcb.133.5.971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Tabernero C., Zolotukhin A. S., Valentin A., Pavlakis G. N., Felber B. K. The posttranscriptional control element of the simian retrovirus type 1 forms an extensive RNA secondary structure necessary for its function. J Virol. 1996 Sep;70(9):5998–6011. doi: 10.1128/jvi.70.9.5998-6011.1996. [DOI] [PMC free article] [PubMed] [Google Scholar]
  118. Terns M. P., Dahlberg J. E. Retention and 5' cap trimethylation of U3 snRNA in the nucleus. Science. 1994 May 13;264(5161):959–961. doi: 10.1126/science.8178154. [DOI] [PubMed] [Google Scholar]
  119. Terns M. P., Lund E., Dahlberg J. E. A pre-export U1 snRNP in Xenopus laevis oocyte nuclei. Nucleic Acids Res. 1993 Sep 25;21(19):4569–4573. doi: 10.1093/nar/21.19.4569. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Underwood M. R., Fried H. M. Characterization of nuclear localizing sequences derived from yeast ribosomal protein L29. EMBO J. 1990 Jan;9(1):91–99. doi: 10.1002/j.1460-2075.1990.tb08084.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  121. Weis K., Dingwall C., Lamond A. I. Characterization of the nuclear protein import mechanism using Ran mutants with altered nucleotide binding specificities. EMBO J. 1996 Dec 16;15(24):7120–7128. [PMC free article] [PubMed] [Google Scholar]
  122. Weis K., Ryder U., Lamond A. I. The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import. EMBO J. 1996 Apr 15;15(8):1818–1825. [PMC free article] [PubMed] [Google Scholar]
  123. Wen W., Meinkoth J. L., Tsien R. Y., Taylor S. S. Identification of a signal for rapid export of proteins from the nucleus. Cell. 1995 Aug 11;82(3):463–473. doi: 10.1016/0092-8674(95)90435-2. [DOI] [PubMed] [Google Scholar]
  124. Wilson S. M., Datar K. V., Paddy M. R., Swedlow J. R., Swanson M. S. Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae. J Cell Biol. 1994 Dec;127(5):1173–1184. doi: 10.1083/jcb.127.5.1173. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Wolff B., Sanglier J. J., Wang Y. Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cytoplasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem Biol. 1997 Feb;4(2):139–147. doi: 10.1016/s1074-5521(97)90257-x. [DOI] [PubMed] [Google Scholar]
  126. Wu J., Matunis M. J., 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. 1995 Jun 9;270(23):14209–14213. doi: 10.1074/jbc.270.23.14209. [DOI] [PubMed] [Google Scholar]
  127. Yokoyama N., Hayashi N., Seki T., Panté N., Ohba T., Nishii K., Kuma K., Hayashida T., Miyata T., Aebi U. A giant nucleopore protein that binds Ran/TC4. Nature. 1995 Jul 13;376(6536):184–188. doi: 10.1038/376184a0. [DOI] [PubMed] [Google Scholar]
  128. Zasloff M. tRNA transport from the nucleus in a eukaryotic cell: carrier-mediated translocation process. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6436–6440. doi: 10.1073/pnas.80.21.6436. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Zolotukhin A. S., Felber B. K. Mutations in the nuclear export signal of human ran-binding protein RanBP1 block the Rev-mediated posttranscriptional regulation of human immunodeficiency virus type 1. J Biol Chem. 1997 Apr 25;272(17):11356–11360. doi: 10.1074/jbc.272.17.11356. [DOI] [PubMed] [Google Scholar]
  130. Zolotukhin A. S., Valentin A., Pavlakis G. N., Felber B. K. Continuous propagation of RRE(-) and Rev(-)RRE(-) human immunodeficiency virus type 1 molecular clones containing a cis-acting element of simian retrovirus type 1 in human peripheral blood lymphocytes. J Virol. 1994 Dec;68(12):7944–7952. doi: 10.1128/jvi.68.12.7944-7952.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from RNA are provided here courtesy of The RNA Society

RESOURCES