Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1994 Jun 15;300(Pt 3):609–618. doi: 10.1042/bj3000609

Nucleocytoplasmic transport.

P S Agutter 1, D Prochnow 1
PMCID: PMC1138210  PMID: 8010940

Full text

PDF
610

Images in this article

Selected References

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

  1. Adam S. A., Lobl T. J., Mitchell M. A., Gerace L. Identification of specific binding proteins for a nuclear location sequence. Nature. 1989 Jan 19;337(6204):276–279. doi: 10.1038/337276a0. [DOI] [PubMed] [Google Scholar]
  2. Adams A., Fey E. G., Pike S. F., Taylorson C. J., White H. A., Rabin B. R. Preparation and properties of a complex from rat liver of polyribosomes with components of the cytoskeleton. Biochem J. 1983 Oct 15;216(1):215–226. doi: 10.1042/bj2160215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Agutter P. S., McArdle H. J., McCaldin B. Evidence for involvement of nuclear envelope nucleoside triphosphatase in nucleocytoplasmic translocation of ribonucleoprotein. Nature. 1976 Sep 9;263(5573):165–167. doi: 10.1038/263165a0. [DOI] [PubMed] [Google Scholar]
  4. Agutter P. S. Nucleocytoplasmic RNA transport. Subcell Biochem. 1984;10:281–357. doi: 10.1007/978-1-4613-2709-7_5. [DOI] [PubMed] [Google Scholar]
  5. Akey C. W., Goldfarb D. S. Protein import through the nuclear pore complex is a multistep process. J Cell Biol. 1989 Sep;109(3):971–982. doi: 10.1083/jcb.109.3.971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Akey C. W. Visualization of transport-related configurations of the nuclear pore transporter. Biophys J. 1990 Aug;58(2):341–355. doi: 10.1016/S0006-3495(90)82381-X. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Baglia F. A., Maul G. G. Nuclear ribonucleoprotein release and nucleoside triphosphatase activity are inhibited by antibodies directed against one nuclear matrix glycoprotein. Proc Natl Acad Sci U S A. 1983 Apr;80(8):2285–2289. doi: 10.1073/pnas.80.8.2285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Bailly E., Pines J., Hunter T., Bornens M. Cytoplasmic accumulation of cyclin B1 in human cells: association with a detergent-resistant compartment and with the centrosome. J Cell Sci. 1992 Mar;101(Pt 3):529–545. doi: 10.1242/jcs.101.3.529. [DOI] [PubMed] [Google Scholar]
  9. 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]
  10. Benditt J. O., Meyer C., Fasold H., Barnard F. C., Riedel N. Interaction of a nuclear location signal with isolated nuclear envelopes and identification of signal-binding proteins by photoaffinity labeling. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9327–9331. doi: 10.1073/pnas.86.23.9327. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Bernd A., Schröder H. C., Zahn R. K., Müller W. E. Modulation of the nuclear-envelope nucleoside triphosphatase by poly(A)-rich mRNA and by microtubule protein. Eur J Biochem. 1982 Dec;129(1):43–49. doi: 10.1111/j.1432-1033.1982.tb07018.x. [DOI] [PubMed] [Google Scholar]
  12. Berrios M., Blobel G., Fisher P. A. Characterization of an ATPase/dATPase activity associated with the Drosophila nuclear matrix-pore complex-lamina fraction. Identification of the putative enzyme polypeptide by direct ultraviolet photoaffinity labeling. J Biol Chem. 1983 Apr 10;258(7):4548–4555. [PubMed] [Google Scholar]
  13. Berrios M., Fisher P. A. A myosin heavy-chain-like polypeptide is associated with the nuclear envelope in higher eukaryotic cells. J Cell Biol. 1986 Sep;103(3):711–724. doi: 10.1083/jcb.103.3.711. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Blobel G. Gene gating: a hypothesis. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8527–8529. doi: 10.1073/pnas.82.24.8527. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Breeuwer M., Goldfarb D. S. Facilitated nuclear transport of histone H1 and other small nucleophilic proteins. Cell. 1990 Mar 23;60(6):999–1008. doi: 10.1016/0092-8674(90)90348-i. [DOI] [PubMed] [Google Scholar]
  16. Bürglin T. R., De Robertis E. M. The nuclear migration signal of Xenopus laevis nucleoplasmin. EMBO J. 1987 Sep;6(9):2617–2625. doi: 10.1002/j.1460-2075.1987.tb02552.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Carmo-Fonseca M., Kern H., Hurt E. C. Human nucleoporin p62 and the essential yeast nuclear pore protein NSP1 show sequence homology and a similar domain organization. Eur J Cell Biol. 1991 Jun;55(1):17–30. [PubMed] [Google Scholar]
  18. Cervera M., Dreyfuss G., Penman S. Messenger RNA is translated when associated with the cytoskeletal framework in normal and VSV-infected HeLa cells. Cell. 1981 Jan;23(1):113–120. doi: 10.1016/0092-8674(81)90276-2. [DOI] [PubMed] [Google Scholar]
  19. Company M., Arenas J., Abelson J. Requirement of the RNA helicase-like protein PRP22 for release of messenger RNA from spliceosomes. Nature. 1991 Feb 7;349(6309):487–493. doi: 10.1038/349487a0. [DOI] [PubMed] [Google Scholar]
  20. Cordes V., Waizenegger I., Krohne G. Nuclear pore complex glycoprotein p62 of Xenopus laevis and mouse: cDNA cloning and identification of its glycosylated region. Eur J Cell Biol. 1991 Jun;55(1):31–47. [PubMed] [Google Scholar]
  21. Dabauvalle M. C., Schulz B., Scheer U., Peters R. Inhibition of nuclear accumulation of karyophilic proteins in living cells by microinjection of the lectin wheat germ agglutinin. Exp Cell Res. 1988 Jan;174(1):291–296. doi: 10.1016/0014-4827(88)90163-2. [DOI] [PubMed] [Google Scholar]
  22. Dargemont C., Kühn L. C. Export of mRNA from microinjected nuclei of Xenopus laevis oocytes. J Cell Biol. 1992 Jul;118(1):1–9. doi: 10.1083/jcb.118.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Davis I., Ish-Horowicz D. Apical localization of pair-rule transcripts requires 3' sequences and limits protein diffusion in the Drosophila blastoderm embryo. Cell. 1991 Nov 29;67(5):927–940. doi: 10.1016/0092-8674(91)90366-7. [DOI] [PubMed] [Google Scholar]
  24. Davis L. I., Blobel G. Identification and characterization of a nuclear pore complex protein. Cell. 1986 Jun 6;45(5):699–709. doi: 10.1016/0092-8674(86)90784-1. [DOI] [PubMed] [Google Scholar]
  25. Davis L. I. Control of nucleocytoplasmic transport. Curr Opin Cell Biol. 1992 Jun;4(3):424–429. doi: 10.1016/0955-0674(92)90007-y. [DOI] [PubMed] [Google Scholar]
  26. Davis L. I., Fink G. R. The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell. 1990 Jun 15;61(6):965–978. doi: 10.1016/0092-8674(90)90062-j. [DOI] [PubMed] [Google Scholar]
  27. De Robertis E. M., Longthorne R. F., Gurdon J. B. Intracellular migration of nuclear proteins in Xenopus oocytes. Nature. 1978 Mar 16;272(5650):254–256. doi: 10.1038/272254a0. [DOI] [PubMed] [Google Scholar]
  28. Dessev G. N. Nuclear envelope structure. Curr Opin Cell Biol. 1992 Jun;4(3):430–435. doi: 10.1016/0955-0674(92)90008-z. [DOI] [PubMed] [Google Scholar]
  29. Dingwall C., Laskey R. A. Protein import into the cell nucleus. Annu Rev Cell Biol. 1986;2:367–390. doi: 10.1146/annurev.cb.02.110186.002055. [DOI] [PubMed] [Google Scholar]
  30. Dingwall C., Sharnick S. V., Laskey R. A. A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell. 1982 Sep;30(2):449–458. doi: 10.1016/0092-8674(82)90242-2. [DOI] [PubMed] [Google Scholar]
  31. Divecha N., Banfić H., Irvine R. F. The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J. 1991 Nov;10(11):3207–3214. doi: 10.1002/j.1460-2075.1991.tb04883.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Dworetzky S. I., Feldherr C. M. Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J Cell Biol. 1988 Mar;106(3):575–584. doi: 10.1083/jcb.106.3.575. [DOI] [PMC free article] [PubMed] [Google Scholar]
  33. Eckner R., Ellmeier W., Birnstiel M. L. Mature mRNA 3' end formation stimulates RNA export from the nucleus. EMBO J. 1991 Nov;10(11):3513–3522. doi: 10.1002/j.1460-2075.1991.tb04915.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Elledge S. J., Richman R., Hall F. L., Williams R. T., Lodgson N., Harper J. W. CDK2 encodes a 33-kDa cyclin A-associated protein kinase and is expressed before CDC2 in the cell cycle. Proc Natl Acad Sci U S A. 1992 Apr 1;89(7):2907–2911. doi: 10.1073/pnas.89.7.2907. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. FELDHERR C. M. The nuclear annuli as pathways for nucleocytoplasmic exchanges. J Cell Biol. 1962 Jul;14:65–72. doi: 10.1083/jcb.14.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. 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]
  37. Feldherr C. M., Kallenbach E., Schultz N. Movement of a karyophilic protein through the nuclear pores of oocytes. J Cell Biol. 1984 Dec;99(6):2216–2222. doi: 10.1083/jcb.99.6.2216. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Feldherr C. M., Ogburn J. A. Mechanism for the selection of nuclear polypeptides in Xenopus oocytes. II. Two-dimensional gel analysis. J Cell Biol. 1980 Dec;87(3 Pt 1):589–593. doi: 10.1083/jcb.87.3.589. [DOI] [PMC free article] [PubMed] [Google Scholar]
  39. Feldherr C. M., Pomerantz J. Mechanism for the selection of nuclear polypeptides in Xenopus oocytes. J Cell Biol. 1978 Jul;78(1):168–175. doi: 10.1083/jcb.78.1.168. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Fey E. G., Wan K. M., Penman S. Epithelial cytoskeletal framework and nuclear matrix-intermediate filament scaffold: three-dimensional organization and protein composition. J Cell Biol. 1984 Jun;98(6):1973–1984. doi: 10.1083/jcb.98.6.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Finlay D. R., Forbes D. J. Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell. 1990 Jan 12;60(1):17–29. doi: 10.1016/0092-8674(90)90712-n. [DOI] [PubMed] [Google Scholar]
  42. Finlay D. R., Meier E., Bradley P., Horecka J., Forbes D. J. A complex of nuclear pore proteins required for pore function. J Cell Biol. 1991 Jul;114(1):169–183. doi: 10.1083/jcb.114.1.169. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Finlay D. R., Newmeyer D. D., Price T. M., Forbes D. J. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores. J Cell Biol. 1987 Feb;104(2):189–200. doi: 10.1083/jcb.104.2.189. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Forbes D. J. Structure and function of the nuclear pore complex. Annu Rev Cell Biol. 1992;8:495–527. doi: 10.1146/annurev.cb.08.110192.002431. [DOI] [PubMed] [Google Scholar]
  45. Garcia-Bustos J. F., Wagner P., Hall M. N. Nuclear import substrates compete for a limited number of binding sites. Evidence for different classes of yeast nuclear import receptors. J Biol Chem. 1991 Nov 25;266(33):22303–22306. [PubMed] [Google Scholar]
  46. Georgatos S. D., Blobel G. Lamin B constitutes an intermediate filament attachment site at the nuclear envelope. J Cell Biol. 1987 Jul;105(1):117–125. doi: 10.1083/jcb.105.1.117. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Gerace L., Ottaviano Y., Kondor-Koch C. Identification of a major polypeptide of the nuclear pore complex. J Cell Biol. 1982 Dec;95(3):826–837. doi: 10.1083/jcb.95.3.826. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Goldfarb D. S. Are the cytosolic components of the nuclear, ER, and mitochondrial import apparatus functionally related? Cell. 1992 Jul 24;70(2):185–188. doi: 10.1016/0092-8674(92)90094-s. [DOI] [PubMed] [Google Scholar]
  49. Goldfarb D. S. Shuttling proteins go both ways. Curr Biol. 1991 Aug;1(4):212–214. doi: 10.1016/0960-9822(91)90059-6. [DOI] [PubMed] [Google Scholar]
  50. Goldfine I. D., Clawson G. A., Smuckler E. A., Purrello F., Vigneri Action of insulin at the nuclear envelope. Mol Cell Biochem. 1982 Oct 1;48(1):3–14. doi: 10.1007/BF00214816. [DOI] [PubMed] [Google Scholar]
  51. Greber U. F., Gerace L. Nuclear protein import is inhibited by an antibody to a lumenal epitope of a nuclear pore complex glycoprotein. J Cell Biol. 1992 Jan;116(1):15–30. doi: 10.1083/jcb.116.1.15. [DOI] [PMC free article] [PubMed] [Google Scholar]
  52. Greber U. F., Senior A., Gerace L. A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 1990 May;9(5):1495–1502. doi: 10.1002/j.1460-2075.1990.tb08267.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Hall M. N., Hereford L., Herskowitz I. Targeting of E. coli beta-galactosidase to the nucleus in yeast. Cell. 1984 Apr;36(4):1057–1065. doi: 10.1016/0092-8674(84)90055-2. [DOI] [PubMed] [Google Scholar]
  54. Hallberg E., Wozniak R. W., Blobel G. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J Cell Biol. 1993 Aug;122(3):513–521. doi: 10.1083/jcb.122.3.513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. 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]
  56. Hamm J., Mattaj I. W. Monomethylated cap structures facilitate RNA export from the nucleus. Cell. 1990 Oct 5;63(1):109–118. doi: 10.1016/0092-8674(90)90292-m. [DOI] [PubMed] [Google Scholar]
  57. Hesketh J. E., Campbell G. P., Reeds P. J. Rapid response of protein synthesis to insulin in 3T3 cells: effects of protein kinase C depletion and differences from the response to serum repletion. Biosci Rep. 1986 Sep;6(9):797–804. doi: 10.1007/BF01117102. [DOI] [PubMed] [Google Scholar]
  58. Hesketh J. E., Pryme I. F. Evidence that insulin increases the proportion of polysomes that are bound to the cytoskeleton in 3T3 fibroblasts. FEBS Lett. 1988 Apr 11;231(1):62–66. doi: 10.1016/0014-5793(88)80703-8. [DOI] [PubMed] [Google Scholar]
  59. Hesketh J. E., Pryme I. F. Interaction between mRNA, ribosomes and the cytoskeleton. Biochem J. 1991 Jul 1;277(Pt 1):1–10. doi: 10.1042/bj2770001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  60. Huang S., Spector D. L. Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors. Genes Dev. 1991 Dec;5(12A):2288–2302. doi: 10.1101/gad.5.12a.2288. [DOI] [PubMed] [Google Scholar]
  61. Huang S., Spector D. L. Nascent pre-mRNA transcripts are associated with nuclear regions enriched in splicing factors. Genes Dev. 1991 Dec;5(12A):2288–2302. doi: 10.1101/gad.5.12a.2288. [DOI] [PubMed] [Google Scholar]
  62. Imamoto-Sonobe N., Matsuoka Y., Semba T., Okada Y., Uchida T., Yoneda Y. A protein recognized by antibodies to Asp-Asp-Asp-Glu-Asp shows specific binding activity to heterogeneous nuclear transport signals. J Biol Chem. 1990 Sep 25;265(27):16504–16508. [PubMed] [Google Scholar]
  63. Imamoto N., Matsuoka Y., Kurihara T., Kohno K., Miyagi M., Sakiyama F., Okada Y., Tsunasawa S., Yoneda Y. Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins. J Cell Biol. 1992 Dec;119(5):1047–1061. doi: 10.1083/jcb.119.5.1047. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Izaurralde E., Stepinski J., Darzynkiewicz E., Mattaj I. W. A cap binding protein that may mediate nuclear export of RNA polymerase II-transcribed RNAs. J Cell Biol. 1992 Sep;118(6):1287–1295. doi: 10.1083/jcb.118.6.1287. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Jackson D. A., Hassan A. B., Errington R. J., Cook P. R. Visualization of focal sites of transcription within human nuclei. EMBO J. 1993 Mar;12(3):1059–1065. doi: 10.1002/j.1460-2075.1993.tb05747.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  66. Jessus C., Beach D. Oscillation of MPF is accompanied by periodic association between cdc25 and cdc2-cyclin B. Cell. 1992 Jan 24;68(2):323–332. doi: 10.1016/0092-8674(92)90473-p. [DOI] [PubMed] [Google Scholar]
  67. Kalderon D., Richardson W. D., Markham A. F., Smith A. E. Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature. 1984 Sep 6;311(5981):33–38. doi: 10.1038/311033a0. [DOI] [PubMed] [Google Scholar]
  68. Kleinschmidt J. A., Seiter A. Identification of domains involved in nuclear uptake and histone binding of protein N1 of Xenopus laevis. EMBO J. 1988 Jun;7(6):1605–1614. doi: 10.1002/j.1460-2075.1988.tb02986.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Kondor-Koch C., Riedel N., Valentin R., Fasold H., Fischer H. Characterization of an ATPase on the inside of rat-liver nuclear envelopes by affinity labeling. Eur J Biochem. 1982 Oct;127(2):285–289. doi: 10.1111/j.1432-1033.1982.tb06868.x. [DOI] [PubMed] [Google Scholar]
  70. Konings D. A., Mattaj I. W. Mutant U2 snRNAs of Xenopus which can form an altered higher order RNA structure are unable to enter the nucleus. Exp Cell Res. 1987 Oct;172(2):329–339. doi: 10.1016/0014-4827(87)90391-0. [DOI] [PubMed] [Google Scholar]
  71. Krug R. M. The regulation of export of mRNA from nucleus to cytoplasm. Curr Opin Cell Biol. 1993 Dec;5(6):944–949. doi: 10.1016/0955-0674(93)90074-z. [DOI] [PubMed] [Google Scholar]
  72. Lanford R. E., Kanda P., Kennedy R. C. Induction of nuclear transport with a synthetic peptide homologous to the SV40 T antigen transport signal. Cell. 1986 Aug 15;46(4):575–582. doi: 10.1016/0092-8674(86)90883-4. [DOI] [PubMed] [Google Scholar]
  73. Lanford R. E., White R. G., Dunham R. G., Kanda P. Effect of basic and nonbasic amino acid substitutions on transport induced by simian virus 40 T-antigen synthetic peptide nuclear transport signals. Mol Cell Biol. 1988 Jul;8(7):2722–2729. doi: 10.1128/mcb.8.7.2722. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Lawrence J. B., Singer R. H., Marselle L. M. Highly localized tracks of specific transcripts within interphase nuclei visualized by in situ hybridization. Cell. 1989 May 5;57(3):493–502. doi: 10.1016/0092-8674(89)90924-0. [DOI] [PubMed] [Google Scholar]
  75. Lee W. C., Mélèse T. Identification and characterization of a nuclear localization sequence-binding protein in yeast. Proc Natl Acad Sci U S A. 1989 Nov;86(22):8808–8812. doi: 10.1073/pnas.86.22.8808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  76. Lenk R., Ransom L., Kaufmann Y., Penman S. A cytoskeletal structure with associated polyribosomes obtained from HeLa cells. Cell. 1977 Jan;10(1):67–78. doi: 10.1016/0092-8674(77)90141-6. [DOI] [PubMed] [Google Scholar]
  77. Loeb J. D., Davis L. I., Fink G. R. NUP2, a novel yeast nucleoporin, has functional overlap with other proteins of the nuclear pore complex. Mol Biol Cell. 1993 Feb;4(2):209–222. doi: 10.1091/mbc.4.2.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Madsen P., Nielsen S., Celis J. E. Monoclonal antibody specific for human nuclear proteins IEF 8Z30 and 8Z31 accumulates in the nucleus a few hours after cytoplasmic microinjection of cells expressing these proteins. J Cell Biol. 1986 Dec;103(6 Pt 1):2083–2089. doi: 10.1083/jcb.103.6.2083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. 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]
  80. Maquat L. E. Nuclear mRNA export. Curr Opin Cell Biol. 1991 Dec;3(6):1004–1012. doi: 10.1016/0955-0674(91)90121-e. [DOI] [PubMed] [Google Scholar]
  81. Mattaj I. W., De Robertis E. M. Nuclear segregation of U2 snRNA requires binding of specific snRNP proteins. Cell. 1985 Jan;40(1):111–118. doi: 10.1016/0092-8674(85)90314-9. [DOI] [PubMed] [Google Scholar]
  82. Mattaj I. W. Splicing stories and poly(A) tales: an update on RNA processing and transport. Curr Opin Cell Biol. 1990 Jun;2(3):528–538. doi: 10.1016/0955-0674(90)90138-5. [DOI] [PubMed] [Google Scholar]
  83. Maul G. G. The nuclear and the cytoplasmic pore complex: structure, dynamics, distribution, and evolution. Int Rev Cytol Suppl. 1977;(6):75–186. [PubMed] [Google Scholar]
  84. McDonald J. R., Agutter P. S. The relationship between polyribonucleotide binding and the phosphorylation and dephosphorylation of nuclear envelope protein. FEBS Lett. 1980 Jul 28;116(2):145–148. doi: 10.1016/0014-5793(80)80629-6. [DOI] [PubMed] [Google Scholar]
  85. Mehlin H., Daneholt B., Skoglund U. Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell. 1992 May 15;69(4):605–613. doi: 10.1016/0092-8674(92)90224-z. [DOI] [PubMed] [Google Scholar]
  86. Meier U. T., Blobel G. Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell. 1992 Jul 10;70(1):127–138. doi: 10.1016/0092-8674(92)90539-o. [DOI] [PubMed] [Google Scholar]
  87. Michaud N., Goldfarb D. S. Multiple pathways in nuclear transport: the import of U2 snRNP occurs by a novel kinetic pathway. J Cell Biol. 1991 Jan;112(2):215–223. doi: 10.1083/jcb.112.2.215. [DOI] [PMC free article] [PubMed] [Google Scholar]
  88. Michaud N., Goldfarb D. Microinjected U snRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways. J Cell Biol. 1992 Feb;116(4):851–861. doi: 10.1083/jcb.116.4.851. [DOI] [PMC free article] [PubMed] [Google Scholar]
  89. Moffett R. B., Webb T. E. Characterization of a messenger RNA transport protein. Biochim Biophys Acta. 1983 Aug 2;740(3):231–242. doi: 10.1016/0167-4781(83)90131-8. [DOI] [PubMed] [Google Scholar]
  90. Moon R. T., Nicosia R. F., Olsen C., Hille M. B., Jeffery W. R. The cytoskeletal framework of sea urchin eggs and embryos: developmental changes in the association of messenger RNA. Dev Biol. 1983 Feb;95(2):447–458. doi: 10.1016/0012-1606(83)90046-5. [DOI] [PubMed] [Google Scholar]
  91. Moore M. S., Blobel G. The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cytosolic factors. Cell. 1992 Jun 12;69(6):939–950. doi: 10.1016/0092-8674(92)90613-h. [DOI] [PubMed] [Google Scholar]
  92. Newmeyer D. D., Forbes D. J. An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: requirement in signal-mediated binding to the nuclear pore. J Cell Biol. 1990 Mar;110(3):547–557. doi: 10.1083/jcb.110.3.547. [DOI] [PMC free article] [PubMed] [Google Scholar]
  93. 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]
  94. Newmeyer D. D., Lucocq J. M., Bürglin T. R., De Robertis E. M. Assembly in vitro of nuclei active in nuclear protein transport: ATP is required for nucleoplasmin accumulation. EMBO J. 1986 Mar;5(3):501–510. doi: 10.1002/j.1460-2075.1986.tb04239.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Newport J. W., Wilson K. L., Dunphy W. G. A lamin-independent pathway for nuclear envelope assembly. J Cell Biol. 1990 Dec;111(6 Pt 1):2247–2259. doi: 10.1083/jcb.111.6.2247. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Paine P. L. Diffusive and nondiffusive proteins in vivo. J Cell Biol. 1984 Jul;99(1 Pt 2):188s–195s. doi: 10.1083/jcb.99.1.188s. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. Paine P. L., Moore L. C., Horowitz S. B. Nuclear envelope permeability. Nature. 1975 Mar 13;254(5496):109–114. doi: 10.1038/254109a0. [DOI] [PubMed] [Google Scholar]
  98. Paine P. L. Nuclear protein accumulation by facilitated transport and intranuclear binding. Trends Cell Biol. 1993 Oct;3(10):325–329. doi: 10.1016/0962-8924(93)90096-j. [DOI] [PubMed] [Google Scholar]
  99. Paine P. L. Nuclear protein accumulation: envelope transport or phase affinity mechanisms? Cell Biol Int Rep. 1988 Sep;12(9):691–708. doi: 10.1016/0309-1651(88)90084-7. [DOI] [PubMed] [Google Scholar]
  100. Peters R. Fluorescence microphotolysis to measure nucleocytoplasmic transport and intracellular mobility. Biochim Biophys Acta. 1986 Dec 22;864(3-4):305–359. doi: 10.1016/0304-4157(86)90003-1. [DOI] [PubMed] [Google Scholar]
  101. Pfeifer K., Weiler B. E., Ugarkovic D., Bachmann M., Schröder H. C., Müller W. E. Evidence for a direct interaction of Rev protein with nuclear envelop mRNA-translocation system. Eur J Biochem. 1991 Jul 1;199(1):53–64. doi: 10.1111/j.1432-1033.1991.tb16091.x. [DOI] [PubMed] [Google Scholar]
  102. Picard D., Yamamoto K. R. Two signals mediate hormone-dependent nuclear localization of the glucocorticoid receptor. EMBO J. 1987 Nov;6(11):3333–3340. doi: 10.1002/j.1460-2075.1987.tb02654.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Piñol-Roma S., Dreyfuss G. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature. 1992 Feb 20;355(6362):730–732. doi: 10.1038/355730a0. [DOI] [PubMed] [Google Scholar]
  104. Prochnow D., Riedel N., Agutter P. S., Fasold H. Poly(A) binding proteins located at the inner surface of resealed nuclear envelopes. J Biol Chem. 1990 Apr 25;265(12):6536–6539. [PubMed] [Google Scholar]
  105. Ramaekers F. C., Benedetti E. L., Dunia I., Vorstenbosch P., Bloemendal H. Polyribosomes associated with microfilaments in cultured lens cells. Biochim Biophys Acta. 1983 Sep 9;740(4):441–448. doi: 10.1016/0167-4781(83)90093-3. [DOI] [PubMed] [Google Scholar]
  106. Reichelt R., Holzenburg A., Buhle E. L., Jr, Jarnik M., Engel A., Aebi U. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J Cell Biol. 1990 Apr;110(4):883–894. doi: 10.1083/jcb.110.4.883. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. 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]
  108. Rihs H. P., Peters R. Nuclear transport kinetics depend on phosphorylation-site-containing sequences flanking the karyophilic signal of the Simian virus 40 T-antigen. EMBO J. 1989 May;8(5):1479–1484. doi: 10.1002/j.1460-2075.1989.tb03531.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Roberts B. L., Richardson W. D., Smith A. E. The effect of protein context on nuclear location signal function. Cell. 1987 Jul 31;50(3):465–475. doi: 10.1016/0092-8674(87)90500-9. [DOI] [PubMed] [Google Scholar]
  110. Rosbash M., Singer R. H. RNA travel: tracks from DNA to cytoplasm. Cell. 1993 Nov 5;75(3):399–401. doi: 10.1016/0092-8674(93)90373-x. [DOI] [PubMed] [Google Scholar]
  111. Scherrer K. Prosomes, subcomplexes of untranslated mRNP. Mol Biol Rep. 1990 Feb;14(1):1–9. doi: 10.1007/BF00422709. [DOI] [PubMed] [Google Scholar]
  112. Schindler M., Jiang L. W. Epidermal growth factor and insulin stimulate nuclear pore-mediated macromolecular transport in isolated rat liver nuclei. J Cell Biol. 1987 Apr;104(4):849–853. doi: 10.1083/jcb.104.4.849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Schindler M., Jiang L. W. Nuclear actin and myosin as control elements in nucleocytoplasmic transport. J Cell Biol. 1986 Mar;102(3):859–862. doi: 10.1083/jcb.102.3.859. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Schröder H. C., Diehl-Seifert B., Rottmann M., Messer R., Bryson B. A., Agutter P. S., Müller W. E. Functional dissection of nuclear envelope mRNA translocation system: effects of phorbol ester and a monoclonal antibody recognizing cytoskeletal structures. Arch Biochem Biophys. 1988 Mar;261(2):394–404. doi: 10.1016/0003-9861(88)90355-4. [DOI] [PubMed] [Google Scholar]
  115. Schröder H. C., Facy P., Monsigny M., Pfeifer K., Bek A., Müller W. E. Purification of a glucose-binding protein from rat liver nuclei. Evidence for a role in targeting of nuclear mRNP to nuclear pore complex. Eur J Biochem. 1992 May 1;205(3):1017–1025. doi: 10.1111/j.1432-1033.1992.tb16869.x. [DOI] [PubMed] [Google Scholar]
  116. Schröder H. C., Friese U., Bachmann M., Zaubitzer T., Müller W. E. Energy requirement and kinetics of transport of poly(A)-free histone mRNA compared to poly(A)-rich mRNA from isolated L-cell nuclei. Eur J Biochem. 1989 Apr 15;181(1):149–158. doi: 10.1111/j.1432-1033.1989.tb14706.x. [DOI] [PubMed] [Google Scholar]
  117. Schröder H. C., Rottmann M., Bachmann M., Müller W. E. Purification and characterization of the major nucleoside triphosphatase from rat liver nuclear envelopes. J Biol Chem. 1986 Jan 15;261(2):663–668. [PubMed] [Google Scholar]
  118. Schröder H. C., Rottmann M., Wenger R., Bachmann M., Dorn A., Müller W. E. Studies on protein kinases involved in regulation of nucleocytoplasmic mRNA transport. Biochem J. 1988 Jun 15;252(3):777–790. doi: 10.1042/bj2520777. [DOI] [PMC free article] [PubMed] [Google Scholar]
  119. Schröder H. C., Trölltsch D., Friese U., Bachmann M., Müller W. E. Mature mRNA is selectively released from the nuclear matrix by an ATP/dATP-dependent mechanism sensitive to topoisomerase inhibitors. J Biol Chem. 1987 Jun 25;262(18):8917–8925. [PubMed] [Google Scholar]
  120. Schröder H. C., Trölltsch D., Wenger R., Bachmann M., Diehl-Seifert B., Müller W. E. Cytochalasin B selectively releases ovalbumin mRNA precursors but not the mature ovalbumin mRNA from hen oviduct nuclear matrix. Eur J Biochem. 1987 Sep 1;167(2):239–245. doi: 10.1111/j.1432-1033.1987.tb13329.x. [DOI] [PubMed] [Google Scholar]
  121. Schröder H. C., Wenger R., Ugarković D., Friese K., Bachmann M., Müller W. E. Differential effect of insulin and epidermal growth factor on the mRNA translocation system and transport of specific poly(A+) mRNA and poly(A-) mRNA in isolated nuclei. Biochemistry. 1990 Mar 6;29(9):2368–2378. doi: 10.1021/bi00461a022. [DOI] [PubMed] [Google Scholar]
  122. Schumm D. E., Morris H. P., Webb T. E. Cytosol-modulated transport of messenger RNA from isolated nuclei. Cancer Res. 1973 Aug;33(8):1821–1828. [PubMed] [Google Scholar]
  123. Schumm D. E., Webb T. E. Insulin-modulated transport of RNA from isolated live nuclei. Arch Biochem Biophys. 1981 Aug;210(1):275–279. doi: 10.1016/0003-9861(81)90190-9. [DOI] [PubMed] [Google Scholar]
  124. Schwabe J. W. Distinctly different...or really much the same? Curr Biol. 1992 May;2(5):237–239. doi: 10.1016/0960-9822(92)90360-m. [DOI] [PubMed] [Google Scholar]
  125. Sheehan M. A., Mills A. D., Sleeman A. M., Laskey R. A., Blow J. J. Steps in the assembly of replication-competent nuclei in a cell-free system from Xenopus eggs. J Cell Biol. 1988 Jan;106(1):1–12. doi: 10.1083/jcb.106.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  126. Shi Y., Thomas J. O. The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol Cell Biol. 1992 May;12(5):2186–2192. doi: 10.1128/mcb.12.5.2186. [DOI] [PMC free article] [PubMed] [Google Scholar]
  127. Silver P. A. How proteins enter the nucleus. Cell. 1991 Feb 8;64(3):489–497. doi: 10.1016/0092-8674(91)90233-o. [DOI] [PubMed] [Google Scholar]
  128. Silver P., Sadler I., Osborne M. A. Yeast proteins that recognize nuclear localization sequences. J Cell Biol. 1989 Sep;109(3):983–989. doi: 10.1083/jcb.109.3.983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  129. Singer R. H., Langevin G. L., Lawrence J. B. Ultrastructural visualization of cytoskeletal mRNAs and their associated proteins using double-label in situ hybridization. J Cell Biol. 1989 Jun;108(6):2343–2353. doi: 10.1083/jcb.108.6.2343. [DOI] [PMC free article] [PubMed] [Google Scholar]
  130. Snow C. M., Senior A., Gerace L. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J Cell Biol. 1987 May;104(5):1143–1156. doi: 10.1083/jcb.104.5.1143. [DOI] [PMC free article] [PubMed] [Google Scholar]
  131. Spector D. L., Fu X. D., Maniatis T. Associations between distinct pre-mRNA splicing components and the cell nucleus. EMBO J. 1991 Nov;10(11):3467–3481. doi: 10.1002/j.1460-2075.1991.tb04911.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  132. Starr C. M., D'Onofrio M., Park M. K., Hanover J. A. Primary sequence and heterologous expression of nuclear pore glycoprotein p62. J Cell Biol. 1990 Jun;110(6):1861–1871. doi: 10.1083/jcb.110.6.1861. [DOI] [PMC free article] [PubMed] [Google Scholar]
  133. Sterne-Marr R., Blevitt J. M., Gerace L. O-linked glycoproteins of the nuclear pore complex interact with a cytosolic factor required for nuclear protein import. J Cell Biol. 1992 Jan;116(2):271–280. doi: 10.1083/jcb.116.2.271. [DOI] [PMC free article] [PubMed] [Google Scholar]
  134. Stevens B. J., Swift H. RNA transport from nucleus to cytoplasm in Chironomus salivary glands. J Cell Biol. 1966 Oct;31(1):55–77. doi: 10.1083/jcb.31.1.55. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Stewart M. Nuclear pore structure and function. Semin Cell Biol. 1992 Aug;3(4):267–277. doi: 10.1016/1043-4682(92)90028-t. [DOI] [PubMed] [Google Scholar]
  136. Stochaj U., Silver P. A. A conserved phosphoprotein that specifically binds nuclear localization sequences is involved in nuclear import. J Cell Biol. 1992 May;117(3):473–482. doi: 10.1083/jcb.117.3.473. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Tobian J. A., Drinkard L., Zasloff M. tRNA nuclear transport: defining the critical regions of human tRNAimet by point mutagenesis. Cell. 1985 Dec;43(2 Pt 1):415–422. doi: 10.1016/0092-8674(85)90171-0. [DOI] [PubMed] [Google Scholar]
  138. Ueyama H., Nakayasu H., Ueda K. Nuclear actin and transport of RNA. Cell Biol Int Rep. 1987 Sep;11(9):671–677. doi: 10.1016/0309-1651(87)90102-0. [DOI] [PubMed] [Google Scholar]
  139. Vedeler A., Pryme I. F., Hesketh J. E. Insulin and step-up conditions cause a redistribution of polysomes among free, cytoskeletal-bound and membrane-bound fractions in Krebs II ascites cells. Cell Biol Int Rep. 1990 Mar;14(3):211–218. doi: 10.1016/s0309-1651(05)80003-7. [DOI] [PubMed] [Google Scholar]
  140. Vedeler A., Pryme I. F., Hesketh J. E. The characterization of free, cytoskeletal and membrane-bound polysomes in Krebs II ascites and 3T3 cells. Mol Cell Biochem. 1991 Feb 2;100(2):183–193. doi: 10.1007/BF00234167. [DOI] [PubMed] [Google Scholar]
  141. Vorbrodt A., Maul G. G. Cytochemical studies on the relation of nucleoside triphosphatase activity to ribonucleoproteins in isolated rat liver nuclei. J Histochem Cytochem. 1980 Jan;28(1):27–35. doi: 10.1177/28.1.6153190. [DOI] [PubMed] [Google Scholar]
  142. Wang J., Cao L. G., Wang Y. L., Pederson T. Localization of pre-messenger RNA at discrete nuclear sites. Proc Natl Acad Sci U S A. 1991 Aug 15;88(16):7391–7395. doi: 10.1073/pnas.88.16.7391. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Wente S. R., Rout M. P., Blobel G. A new family of yeast nuclear pore complex proteins. J Cell Biol. 1992 Nov;119(4):705–723. doi: 10.1083/jcb.119.4.705. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Whytock S., Moir R. D., Stewart M. Selective digestion of nuclear envelopes from Xenopus oocyte germinal vesicles: possible structural role for the nuclear lamina. J Cell Sci. 1990 Nov;97(Pt 3):571–580. doi: 10.1242/jcs.97.3.571. [DOI] [PubMed] [Google Scholar]
  145. Wimmer C., Doye V., Grandi P., Nehrbass U., Hurt E. C. A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 1992 Dec;11(13):5051–5061. doi: 10.1002/j.1460-2075.1992.tb05612.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  146. Wozniak R. W., Bartnik E., Blobel G. Primary structure analysis of an integral membrane glycoprotein of the nuclear pore. J Cell Biol. 1989 Jun;108(6):2083–2092. doi: 10.1083/jcb.108.6.2083. [DOI] [PMC free article] [PubMed] [Google Scholar]
  147. Wozniak R. W., Blobel G. The single transmembrane segment of gp210 is sufficient for sorting to the pore membrane domain of the nuclear envelope. J Cell Biol. 1992 Dec;119(6):1441–1449. doi: 10.1083/jcb.119.6.1441. [DOI] [PMC free article] [PubMed] [Google Scholar]
  148. Xing Y. G., Lawrence J. B. Preservation of specific RNA distribution within the chromatin-depleted nuclear substructure demonstrated by in situ hybridization coupled with biochemical fractionation. J Cell Biol. 1991 Mar;112(6):1055–1063. doi: 10.1083/jcb.112.6.1055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Xing Y., Johnson C. V., Dobner P. R., Lawrence J. B. Higher level organization of individual gene transcription and RNA splicing. Science. 1993 Feb 26;259(5099):1326–1330. doi: 10.1126/science.8446901. [DOI] [PubMed] [Google Scholar]
  150. Yamasaki L., Kanda P., Lanford R. E. Identification of four nuclear transport signal-binding proteins that interact with diverse transport signals. Mol Cell Biol. 1989 Jul;9(7):3028–3036. doi: 10.1128/mcb.9.7.3028. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Yamasaki L., Lanford R. E. Nuclear transport: a guide to import receptors. Trends Cell Biol. 1992 May;2(5):123–127. doi: 10.1016/0962-8924(92)90083-y. [DOI] [PubMed] [Google Scholar]
  152. Zachar Z., Kramer J., Mims I. P., Bingham P. M. Evidence for channeled diffusion of pre-mRNAs during nuclear RNA transport in metazoans. J Cell Biol. 1993 May;121(4):729–742. doi: 10.1083/jcb.121.4.729. [DOI] [PMC free article] [PubMed] [Google Scholar]
  153. 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]
  154. Zeitlin S., Parent A., Silverstein S., Efstratiadis A. Pre-mRNA splicing and the nuclear matrix. Mol Cell Biol. 1987 Jan;7(1):111–120. doi: 10.1128/mcb.7.1.111. [DOI] [PMC free article] [PubMed] [Google Scholar]
  155. van Eekelen C. A., van Venrooij W. J. hnRNA and its attachment to a nuclear protein matrix. J Cell Biol. 1981 Mar;88(3):554–563. doi: 10.1083/jcb.88.3.554. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. van Venrooij W. J., Sillekens P. T., van Eekelen C. A., Reinders R. J. On the association of mRNA with the cytoskeleton in uninfected and adenovirus-infected human KB cells. Exp Cell Res. 1981 Sep;135(1):79–91. doi: 10.1016/0014-4827(81)90301-3. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES