The thermolability of nuclear protein import in tsBN2 cells is suppressed by microinjected Ran-GTP or Ran-GDP, but not by RanQ69L or RanT24N

Journal of Cell Science

Volumn 109, Issue 6, 1996, Pages 1449-1457

  Dickmanns, Achim ^a,b   Bischoff, F Ralf ^c   Marshallsay, C ^d   Luhrmann R ^d   Ponstingl, Herwig ^c   Fanning, Ellen ^a,b  

^a VANDERBILT UNIVERSITY   (United States)

^b UNIVERSITY OF MUNICH   (Germany)

^c GERMAN CANCER RESEARCH CENTER DKFZ   (Germany)

^d PHILIPPS UNIVERSITY MARBURG   (Germany)

Author keywords

Nuclear protein import; Ran; Ran mutant; RCC1

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MUTANT PROTEIN; NUCLEAR PROTEIN;

ANIMAL CELL; ARTICLE; CHROMOSOME CONDENSATION; CONTROLLED STUDY; HYDROLYSIS; MICROINJECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION; PROTEIN TRANSPORT; TEMPERATURE;

ANIMALS; BIOLOGICAL TRANSPORT, ACTIVE; CELL CYCLE PROTEINS; CELL LINE; CRICETINAE; DNA-BINDING PROTEINS; GTP PHOSPHOHYDROLASES; GTP-BINDING PROTEINS; GUANINE NUCLEOTIDE EXCHANGE FACTORS; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MICROINJECTIONS; NUCLEAR PROTEINS; POINT MUTATION; RAN GTP-BINDING PROTEIN; RIBONUCLEOPROTEIN, U1 SMALL NUCLEAR; TEMPERATURE;

EID: 0029975651     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (59)

1. Adam, E. J. H. and Adam, S. A. (1994). Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555.
2. Adam, S. A., Lobl, T. J., Mitchell, M. A. and Gerace, L. (1990) Identification of specific binding proteins for a nuclear localisation sequence. Nature 337, 276-279
3. Amberg, D. C., Fleischmann, M., Stagljar, I., Cole, C. N. and Aebi, M. (1993). Nuclear PRP20 protein is required for mRNA export. EMBO J. 12, 233-241
4. Belhumeur, P., Lee, A., Tam, R., DiPaolo, T., Fortin, N. and Clark, M. (1993). GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces cerevisiae: GTP-binding proteins involved in the maintenance of nuclear organization. Mol. Cell. Biol. 13, 2152-2161.
5. Bischoff, F. R. and Ponstingl, H. (1991a). Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide. Proc. Nat. Acad. Sci. USA 88, 10830-10834.
6. Bischoff, F. R. and Ponstingl, H. (1991b). Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature 354, 80-82.
7. Bischoff, F. R., Klebe, C., Kretschmer, J., Wittinghofer, A. and Ponstingl, H. (1994). RanGAP1 induces GTPase activity of nuclear Ras-related Ran Proc. Nat. Acad Sci. USA 91, 2587-2591.
8. Bischoff, F. R., Krebber, H., Kempf, T., Hermes, I. and Ponstingl, H. (1995a). Human RanGTPase activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. Proc. Nat. Acad. Sci USA 92, 1749-1753.
9. Bischoff, F. R., Krebber, H., Smirnova, E., Dong, W. and Ponstingl, H. (1995b). Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14, 705-715.
10. Cheng, Y., Dahlberg, J. E. and Lund, E. (1995). Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport Science 267, 1807-1810.
11. Corbett, A. H., Koepp, D. M., Schlenstedt, G., Lee, M. S., Hopper, A. K., Silver, P. A. (1995). Rna1p, a Ran/TC4GTPase activating protein, is required for nuclear import. J. Cell Biol. 130, 1017-1026.
12. Dasso, M. (1993). RCC1 in the cell cycle: the regulator of chromosome condensation takes on new roles. Trends Biochem. Sci. 18, 96-101.
13. Dasso, M., Seki, T., Azuma, Y., Ohba, T. and Nishimoto, T. (1994). A mutant form of the Ran/TC4 protein disrupts nuclear function in Xenopus laevis egg extracts by inhibiting the RCC1 protein, a regulator of chromosome condensation. EMBO J. 13, 5732-5744.
14. Dickmanns, A., Zeitvogel, A., Simmersbach, F., Weber, R., Arthur, A. K., Dehde, S., Wildeman, A. G. and Fanning, E. (1994). The kinetics of SV40-induced progression of quiescent cells into S-phase depend on four independent functions of large tumor antigen. J. Virol. 68, 5496-5508.
15. Dingwall, C. and Laskey, R. A. (1991). Nuclear targeting sequences - a consensus? Trends Biol. Sci. 16, 478-481.
16. Forbes, D. J. (1992). Structure and function of the nuclear pore. Annu Rev. Cell Biol. 8, 495-527.
17. Garcia-Bustos, J. F., Heitman, J. and Hall, M. (1991). Nuclear protein localization. Biochim. Biophys. Acta 1071, 83-101.
18. Görlich, D., Prehn, S., Laskey, R. A. and Hartmann, E. (1994). Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778.
19. Görlich, D., Kostka, S., Kraft, R., Dingwall, C., Laskey, R. A., Hartmann, E. and Prehn, S. (1995). Two different subunits of importin cooperate to recognize nuclear location signals and bind them to the nuclear envelope. Curr. Biol. 5, 383-392.
20. Graessmann, M. and Graessmann, A. (1983). Microinjection of tissue culture cells. Meth. Enzymol. 101, 482-512.
21. Gurney, E. G., Harrison, R. O. and Fenno, J. (1980). Monoclonal antibodies against simian virus T antigens: evidence for distinct subclasses of large T antigen and similarities among nonviral T antigens. J. Virol. 34, 752-763.
22. Harlow, E., Crawford, L. V., Pim, D. C. and Williamson, N. (1981) Monoclonal antibodies specific for simian virus 40 tumor antigens. J. Virol. 39, 861-869.
23. Imamoto, N., Shimamoto, T., Takao, T., Tachibana, T., Kose, S., Matsubae, M., Sekimoto, T., Shimonshi, Y. and Yoneda, Y. (1995a). In vivo evidence for involvement of a 58 kDa component of nuclear pore targeting complex in nuclear protein import EMBO J. 14, 3617-3626.
24. Imamoto, N., Tachibana, T., Matsubae, M. and Yoneda, Y. (1995b). A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding. J. Biol. Chem. 270, 8559-8565.
25. Johnson, D. G. and Nogueira Araujo, G. M. de C. (1981). A simple method of reducing the fading of immunofluorescence during microscopy J. Immunol. Meth. 43, 349-350.
26. Kadowaki, T., Goldfarb, D., Spitz, L. M., Tartakoff, A. M. and Ohno, M. (1993). Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily. EMBO J. 12, 2929-2937
27. Klebe, C., Bischoff, F. R., Ponstingl, H. and Wittinghofer, A. (1995). Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry 34, 639-647
28. Kornbluth, S., Dasso, M. and Newport, J. (1994). Evidence for a dual role for TC4 protein in regulating nuclear structure and cell cycle progression. J Cell Biol. 125, 705-719.
29. 3G-cap dependence of U1 and U2 snRNP. EMBO J. 13, 222-231.
30. Matsumoto, T. and Beach, D. (1991). Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase. Cell 66, 347-360
31. Melchior, F., Pascal, B., Evans, J. and Gerace, L. (1993). Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J. Cell Biol. 123, 1649-1659
32. Melchior, F. and Gerace, L. (1995). Mechanisms of nuclear protein import. Curr. Opin. Biol. 7, 310-318.
33. Melchior, F., Guan, T., Yokoyama, N., Nishimito, T. and Gerace, L. (1995). GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import. J. Cell Biol. 131, 571-582.
34. Michaud, N. and Goldfarb, D. (1992). Microinjected UsnRNAs are imported to oocyte nuclei via the nuclear pore complex by three distinguishable targeting pathways. J. Cell Biol. 116, 851-861
35. Mole, S., Gannon, J. V., Ford, M. J. and Lane, D. P. (1987). Structure and function of SV40 large T antigen. Phil. Trans. R. Soc. Lond. B 317, 455-469.
36. Moore, M. S. and Blobel, G. (1992). The two steps of nuclear import, targeting to the nuclear envelope and translocation through the nuclear pore, require different cellular cytosolic factors. Cell 69, 939-950
37. Moore, M. S. and Blobel, G. (1993). The GTP-binding protein Ran/TC4 is required for protein import into the nucleus. Nature 365, 661-663.
38. Moore, M. S. and Blobel, G. (1994a). A G-protein and nucleocytoplasmic transport: the role of Ran. Trends Biochem. Sci. 19, 211-217.
39. Moore, M. S. and Blobel, G. (1994b). Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc. Nat. Acad. Sci USA 91, 10212-10216.
40. Moroianu, J., Blobel, G. and Radu, A. (1995a). Previously identified protein of uncertain function is karyopherin α and together with karyopherin β docks import substrates at nuclear pore complexes. Proc. Nat. Acad. Sci. USA 92, 2008-2011.
41. Moroianu, J., Hijikata, M., Blobel, G. and Radu, R. (1995b). Mammalian karyopherin α1β and α2β heterodimers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins. Proc. Nat. Acad. Sci. USA 92, 6532-6536.
42. Newmeyer, D. D. and Forbes, D. J. (1990). An N-ethylmaleimide-sensitive cytosolic factor for nuclear protein import: requirement in signal-mediated binding to the nuclear pore. J. Cell Biol. 110, 547-557.
43. Nishimoto, T. and Basilico, C. (1978). Analysis of a method for selecting temperature-sensitive mutants of BHK cells. Somat. Cell Genet. 4, 323-340.
44. Nishimoto, T., Eilen, E. and Basilico, C. (1978). Premature chromosome condensation in a ts DNA-mutant of BHK cells. Cell 15, 475-483.
45. Nishitani, H., Ohtsubo, M., Yamashita, K., Iida, H., Pines, J., Yasudo, H., Shibata, Y., Hunter, T. and Nishimoto, T. (1991). Loss of RCC1, a nuclear DNA-binding protein, uncouples the completion of DNA replication from the activation of cdc2 protein kinase and mitosis. EMBO J 10, 1555-1564.
46. Paschal, B. and Gerace, L. (1995). Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J. Cell Biol. 129, 925-937.
47. Radu, A., Blobel, G. and Moore, M. S. (1995) Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Nat. Acad. Sci USA 92, 1769-1773.
48. Ren, M., Drivas, G., D'Eustachio, P. and Rush, M. G. (1993) Ran/TC4. A small nuclear GTP-binding protein that regulates DNA synthesis. J. Cell Biol 120, 313-323.
49. Rout, M. and Wente, S. (1994). Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4, 357-365.
50. Sazer, S. and Nurse, P. (1994). A fission yeast RCC1-related protein is required for the mitosis to interphase transition. EMBO J. 13, 606-615.
51. Schlenstedt, G., Saavedra, S., Loeb, J. D. J., Cole, C. N. and Silver, P. A. (1995). The GTP-bound form of the yeast Ran/TC4 homologue blocks nuclear protein import and appearance of poly (A)+ RNA in the cytoplasm. Proc. Nat. Acad. Sci. USA 92, 225-229.
52. Schneider, C., Weißhart, K., Guarino, L. A., Dornreiter, I. and Fanning, E. (1994). Species specific functional interactions of DNA polymerase a-primase with SV40 T antigen require SV40 origin DNA. Mol. Cell Biol. 14, 3176-3185.
53. Simos, G. and Hurt, E. C. (1995) Nucleocytoplasmic transport: factors and mechanisms. FEBS Lett. 369, 107-112.
54. Stoker, M. P. G. and MacPherson, I. A. (1964). Syrian hamster fibroblast cell line BHK21 and its derivatives. Nature 203, 1355-1357.
55. Tachibana, T., Imamoto, N., Seino, H., Nishimoto, T. and Yoneda, Y. (1994). Loss of RCC1 leads to suppression of nuclear protein import in living cells. J Biol. Chem. 269, 24542-24545
56. Tucker, J., Sczakiel, G., Feuerstein, J., John, J., Goody, R. S. and Wittinghofer, A. (1986). Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site. EMBO J. 5, 1351-1358.
57. van Zee, K., Dickmanns, A., Fischer, U., Lührmann, R. and Fanning, E. (1993). A cytoplasmically anchored nuclear protein interferes specifically with the import of nuclear proteins but not U1snRNA. J. Cell Biol. 121, 229-240.
58. Weis, K., Mattaj, I. and Lamond, A. (1995). Identification of hSRP1α as a functional receptor for nuclear localisation sequences. Science 268, 1049-1053.
59. Zacksenhaus, E., Bremner, R., Phillips, R. A. and Gallie, B. L. (1993) A bipartite nuclear localization signal in the retinoblastoma gene product and its importance for biological activity. Mol. Cell. Biol 18, 4588-4599