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Volumn 112, Issue 14, 1999, Pages 2369-2380

Nuclear pore localization and nucleocytoplasmic transport of eIF-5A: Evidence for direct interaction with the export receptor CRM1

Author keywords

CRM1; eLF 5A; HIV 1; Nuclear export; Nuclear pore complex; Rev

Indexed keywords

HYPUSINE; INITIATION FACTOR 5A; LEPTOMYCIN B;

EID: 0032809085     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (127)

References (86)
  • 1
    • 0024438224 scopus 로고
    • Protein import through the nuclear pore complex is a multistep process
    • Akey, C. W. and Goldfarb, D. S. (1989). Protein import through the nuclear pore complex is a multistep process. J. Cell Biol. 109, 971-982.
    • (1989) J. Cell Biol. , vol.109 , pp. 971-982
    • Akey, C.W.1    Goldfarb, D.S.2
  • 2
    • 0027287349 scopus 로고
    • Architecture of the xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey, C. W. and Radermacher, M. (1993). Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1-19.
    • (1993) J. Cell Biol. , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 3
    • 0031057644 scopus 로고    scopus 로고
    • Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm
    • Arenzana Seisdedos, F., Turpin, P., Rodriguez, M., Thomas, D., Hay, R. T., Virelizier, J. L. and Dargemont, C. (1997). Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm. J. Cell Sci. 110, 369-378.
    • (1997) J. Cell Sci. , vol.110 , pp. 369-378
    • Arenzana Seisdedos, F.1    Turpin, P.2    Rodriguez, M.3    Thomas, D.4    Hay, R.T.5    Virelizier, J.L.6    Dargemont, C.7
  • 4
    • 0032509524 scopus 로고    scopus 로고
    • The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP
    • Askjaer, P., Jensen, T. H., Nilsson, J., Englmeier, L. and Kjems, J. (1998). The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J. Biol. Chem. 273, 33414-33422.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33414-33422
    • Askjaer, P.1    Jensen, T.H.2    Nilsson, J.3    Englmeier, L.4    Kjems, J.5
  • 5
    • 0029197670 scopus 로고
    • Nuclear pore complex proteins
    • Bastos, R., Pante, N. and Burke, B. (1995). Nuclear pore complex proteins. Int. Rev. Cytol. 162B, 257-302.
    • (1995) Int. Rev. Cytol. , vol.162 B , pp. 257-302
    • Bastos, R.1    Pante, N.2    Burke, B.3
  • 6
    • 0029743063 scopus 로고    scopus 로고
    • Targeting and function in mRNA export of nuclear pore complex protein Nup153
    • Bastos, R., Lin, A., Enarson, M. and Burke, B. (1996). Targeting and function in mRNA export of nuclear pore complex protein Nup153. J. Cell Biol. 134, 1141-1156.
    • (1996) J. Cell Biol. , vol.134 , pp. 1141-1156
    • Bastos, R.1    Lin, A.2    Enarson, M.3    Burke, B.4
  • 7
    • 0021842623 scopus 로고
    • Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis
    • Benavente, R., Krohne, G. and Franke, W. W. (1985). Cell type-specific expression of nuclear lamina proteins during development of Xenopus laevis. Cell 41, 177-190.
    • (1985) Cell , vol.41 , pp. 177-190
    • Benavente, R.1    Krohne, G.2    Franke, W.W.3
  • 8
    • 0027947377 scopus 로고
    • Induced gene expression of the hypusine-containing protein eukaryotic initiation factor 5A in activated human T lymphocytes
    • Bevec, D., Klier, H., Holter, W., Tschachler, E., Valent, P., Lottspeich, F., Baumruker, T. and Hauber, J. (1994). Induced gene expression of the hypusine-containing protein eukaryotic initiation factor 5A in activated human T lymphocytes. Proc. Nat. Acad. Sci. USA 91, 10829-10833.
    • (1994) Proc. Nat. Acad. Sci. USA , Issue.91 , pp. 10829-10833
    • Bevec, D.1    Klier, H.2    Holter, W.3    Tschachler, E.4    Valent, P.5    Lottspeich, F.6    Baumruker, T.7    Hauber, J.8
  • 10
    • 0031562701 scopus 로고    scopus 로고
    • The nucleoporin CAN/Nup214 binds to both the cytoplasmic and the nucleoplasmic sides of the nuclear pore complex in overexpressing cells
    • Boer, J. M., van Deursen, J. M., Croes, H. J., Fransen, J. A. and Grosveld, G. C. (1997). The nucleoporin CAN/Nup214 binds to both the cytoplasmic and the nucleoplasmic sides of the nuclear pore complex in overexpressing cells. Exp. Cell Res. 232, 182-185.
    • (1997) Exp. Cell Res. , vol.232 , pp. 182-185
    • Boer, J.M.1    Van Deursen, J.M.2    Croes, H.J.3    Fransen, J.A.4    Grosveld, G.C.5
  • 11
    • 0029149833 scopus 로고
    • Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins
    • Bogerd, H. P., Fridell, R. A., Madore, S. and Cullen, B. R. (1995). Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins. Cell 82, 485-494.
    • (1995) Cell , vol.82 , pp. 485-494
    • Bogerd, H.P.1    Fridell, R.A.2    Madore, S.3    Cullen, B.R.4
  • 12
    • 0020162215 scopus 로고
    • Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth
    • Cooper, H. L., Park, M. H. and Folk, J. E. (1982). Posttranslational formation of hypusine in a single major protein occurs generally in growing cells and is associated with activation of lymphocyte growth. Cell 29, 791-797.
    • (1982) Cell , vol.29 , pp. 791-797
    • Cooper, H.L.1    Park, M.H.2    Folk, J.E.3
  • 13
    • 0029744973 scopus 로고    scopus 로고
    • The NTF2 gene encodes an essential, highly conserved protein that functions in nuclear transport in vivo
    • Corbett, A. H. and Silver, P. A. (1996). The NTF2 gene encodes an essential, highly conserved protein that functions in nuclear transport in vivo. J. Biol. Chem. 271, 18477-18484.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18477-18484
    • Corbett, A.H.1    Silver, P.A.2
  • 14
    • 0030793194 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport of macromolecules
    • Corbett, A. H. and Silver, P. A. (1997). Nucleocytoplasmic transport of macromolecules. Microbiol. Mol. Biol. Rev. 61, 193-211.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 193-211
    • Corbett, A.H.1    Silver, P.A.2
  • 16
    • 0031043895 scopus 로고    scopus 로고
    • Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments
    • Cordes, V. C., Reidenbach, S., Rackwitz, H. R. and Franke, W. W. (1997). Identification of protein p270/Tpr as a constitutive component of the nuclear pore complex-attached intranuclear filaments. J. Cell Biol. 136, 515-529.
    • (1997) J. Cell Biol. , vol.136 , pp. 515-529
    • Cordes, V.C.1    Reidenbach, S.2    Rackwitz, H.R.3    Franke, W.W.4
  • 17
    • 0023823395 scopus 로고
    • Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes
    • Dabauvalle, M. C., Benavente, R. and Chaly, N. (1988). Monoclonal antibodies to a Mr 68,000 pore complex glycoprotein interfere with nuclear protein uptake in Xenopus oocytes. Chromosoma 97, 193-197.
    • (1988) Chromosoma , vol.97 , pp. 193-197
    • Dabauvalle, M.C.1    Benavente, R.2    Chaly, N.3
  • 18
    • 0026099941 scopus 로고
    • Spontaneous assembly of pore complex-containing membranes ('annulate lamellae') in Xenopus egg extract in the absence of chromatin
    • Dabauvalle, M. C., Loos, K., Merkert, H. and Scheer, U. (1991). Spontaneous assembly of pore complex-containing membranes ('annulate lamellae') in Xenopus egg extract in the absence of chromatin. J. Cell Biol. 112, 1073-1082.
    • (1991) J. Cell Biol. , vol.112 , pp. 1073-1082
    • Dabauvalle, M.C.1    Loos, K.2    Merkert, H.3    Scheer, U.4
  • 19
    • 0029060051 scopus 로고
    • The nuclear pore complex
    • Davis, L. I. (1995). The nuclear pore complex. Annu. Rev. Biochem. 64, 865-896.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 865-896
    • Davis, L.I.1
  • 20
    • 0015292069 scopus 로고
    • Oogenesis in Xenopus leavis (Daudin)
    • Dumont, J. N. (1972). Oogenesis in Xenopus leavis (Daudin). J. Morphol. 136, 153-180.
    • (1972) J. Morphol. , vol.136 , pp. 153-180
    • Dumont, J.N.1
  • 21
    • 0029888702 scopus 로고    scopus 로고
    • A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes
    • Ewald, A., Kossner, U., Scheer, U. and Dabauvalle, M. C. (1996). A biochemical and immunological comparison of nuclear and cytoplasmic pore complexes. J. Cell Sci. 109, 1813-1824.
    • (1996) J. Cell Sci. , vol.109 , pp. 1813-1824
    • Ewald, A.1    Kossner, U.2    Scheer, U.3    Dabauvalle, M.C.4
  • 22
    • 0031454975 scopus 로고    scopus 로고
    • The location of the transport gate in the nuclear pore complex
    • Feldherr, C. M. and Akin, D. (1997). The location of the transport gate in the nuclear pore complex. J. Cell Sci. 3065-3070
    • (1997) J. Cell Sci. , pp. 3065-3070
    • Feldherr, C.M.1    Akin, D.2
  • 23
    • 0027981916 scopus 로고
    • Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA
    • Fischer, U., Meyer, S., Teufel, M., Heckel, C., Lührmann, R. and Rautmann, G. (1994). Evidence that HIV-1 Rev directly promotes the nuclear export of unspliced RNA. EMBO J. 13, 4105-4112.
    • (1994) EMBO J. , vol.13 , pp. 4105-4112
    • Fischer, U.1    Meyer, S.2    Teufel, M.3    Heckel, C.4    Lührmann, R.5    Rautmann, G.6
  • 24
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., Huber, J., Boelens, W. C., Mattaj, I. W. and Lührmann, R. (1995). The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 25
    • 0029008267 scopus 로고
    • Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements
    • Fornerod, M., Boer, J., van Baal, S., Jaegle, M., von Lindern, M., Murti, K. G., Davis, D., Bonten, J., Buijs, A. and Grosveld, G. (1995). Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements. Oncogene 10, 1739-1748.
    • (1995) Oncogene , vol.10 , pp. 1739-1748
    • Fornerod, M.1    Boer, J.2    Van Baal, S.3    Jaegle, M.4    Von Lindern, M.5    Murti, K.G.6    Davis, D.7    Bonten, J.8    Buijs, A.9    Grosveld, G.10
  • 26
    • 0029860596 scopus 로고    scopus 로고
    • Interaction of cellular proteins with the leukemia specific fusion proteins DEK-CAN and SET-CAN and their normal counterpart, the nucleoporin CAN
    • Fornerod, M., Boer, J., van Baal, S., Morreau, H. and Grosveld, G. (1996). Interaction of cellular proteins with the leukemia specific fusion proteins DEK-CAN and SET-CAN and their normal counterpart, the nucleoporin CAN. Oncogene 13, 1801-1808.
    • (1996) Oncogene , vol.13 , pp. 1801-1808
    • Fornerod, M.1    Boer, J.2    Van Baal, S.3    Morreau, H.4    Grosveld, G.5
  • 27
    • 0030924190 scopus 로고    scopus 로고
    • CRMI is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M. and Mattaj, I. W. (1997a). CRMI is an export receptor for leucine-rich nuclear export signals. Cell 90, 1051-1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 28
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRMI is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • Fornerod, M., van Deursen, J., van Baal, S., Reynolds, A., Davis, D., Murti, K. G., Fransen, J. and Grosveld, G. (1997b). The human homologue of yeast CRMI is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J. 16, 807-816.
    • (1997) EMBO J. , vol.16 , pp. 807-816
    • Fornerod, M.1    Van Deursen, J.2    Van Baal, S.3    Reynolds, A.4    Davis, D.5    Murti, K.G.6    Fransen, J.7    Grosveld, G.8
  • 29
    • 0014736825 scopus 로고
    • The ultrastructure of the nuclear envelope of amphibian oocytes: A reinvestigation. I. The mature oocyte
    • Franke, W. W. and Scheer, U. (1970). The ultrastructure of the nuclear envelope of amphibian oocytes: a reinvestigation. I. The mature oocyte. J Ultrastruct. Res. 30, 288-316.
    • (1970) J Ultrastruct. Res. , vol.30 , pp. 288-316
    • Franke, W.W.1    Scheer, U.2
  • 30
    • 0001976037 scopus 로고
    • Structures and functions of the nuclear envelope
    • ed. H. Busch, New York: Academic Press
    • Franke, W. W. and Scheer, U. (1974). Structures and functions of the nuclear envelope. In The Cell Nucleus (ed. H. Busch), p. 219. New York: Academic Press.
    • (1974) The Cell Nucleus , pp. 219
    • Franke, W.W.1    Scheer, U.2
  • 31
    • 0029880471 scopus 로고    scopus 로고
    • Nuclear export of late HIV-1 mRNAs occurs via a cellular protein export pathway
    • Fridell, R. A., Bogerd, H. P. and Cullen, B. R. (1996a). Nuclear export of late HIV-1 mRNAs occurs via a cellular protein export pathway. Proc. Nat. Acad. Sci. USA 93, 4421-4424.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 4421-4424
    • Fridell, R.A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 32
    • 0029963140 scopus 로고    scopus 로고
    • Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type I Rev
    • Fridell, R. A., Fischer, U., Lührmann, R., Meyer, B. E., Meinkoth, J. L., Malim, M. H. and Cullen, B. R. (1996b). Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type I Rev. Proc. Nat. Acad. Sci. USA 93, 2936-2940.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 2936-2940
    • Fridell, R.A.1    Fischer, U.2    Lührmann, R.3    Meyer, B.E.4    Meinkoth, J.L.5    Malim, M.H.6    Cullen, B.R.7
  • 33
    • 0029098538 scopus 로고
    • A human nucleoporin-like protein that specifically interacts with HIV Rev
    • Fritz, C. C., Zapp, M. L. and Green, M. R. (1995). A human nucleoporin-like protein that specifically interacts with HIV Rev. Nature 376, 530-533.
    • (1995) Nature , vol.376 , pp. 530-533
    • Fritz, C.C.1    Zapp, M.L.2    Green, M.R.3
  • 34
    • 0030198504 scopus 로고    scopus 로고
    • HIV rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs
    • Fritz, C. C. and Green, M. R. (1996). HIV Rev uses a conserved cellular protein export pathway for the nucleocytoplasmic transport of viral RNAs. Curr. Biol. 6, 848-854.
    • (1996) Curr. Biol. , vol.6 , pp. 848-854
    • Fritz, C.C.1    Green, M.R.2
  • 35
    • 0029786994 scopus 로고    scopus 로고
    • 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
    • Fukuda, M., Gotoh, I., Gotoh, Y. and Nishida, E. (1996). 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. 271, 20024-20028.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3    Nishida, E.4
  • 36
    • 0030831534 scopus 로고    scopus 로고
    • CRMI is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M. and Nishida, E. (1997). CRMI is responsible for intracellular transport mediated by the nuclear export signal. Nature 390, 308-311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 38
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Görlich, D. (1998). Transport into and out of the cell nucleus. EMBO J. 17, 2721-2727.
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Görlich, D.1
  • 39
    • 0020645064 scopus 로고
    • The use of Xenopus oocytes for the expression of cloned genes
    • Gurdon, J. P. and Wickens, M. P. (1983). The use of Xenopus oocytes for the expression of cloned genes. Meth. Enzymol. 101, 370-386.
    • (1983) Meth. Enzymol. , vol.101 , pp. 370-386
    • Gurdon, J.P.1    Wickens, M.P.2
  • 40
    • 0029019877 scopus 로고
    • Detection of a sub-set of polysomal mRNAs associated with modulation of hypusine formation at the G1-S boundary: Proposal of a role for eIF-5A in onset of DNA replication
    • Hanauske-Abel, H. M., Slowinska, B., Zagulska, S., Wilson, R. C., Staiano-Coico, L., Hanauske, A.-R., McCaffrey, T. and Szabo, P. (1995). Detection of a sub-set of polysomal mRNAs associated with modulation of hypusine formation at the G1-S boundary: Proposal of a role for eIF-5A in onset of DNA replication. FEBS Lett. 366, 92-98.
    • (1995) FEBS Lett. , vol.366 , pp. 92-98
    • Hanauske-Abel, H.M.1    Slowinska, B.2    Zagulska, S.3    Wilson, R.C.4    Staiano-Coico, L.5    Hanauske, A.-R.6    McCaffrey, T.7    Szabo, P.8
  • 41
    • 0023225084 scopus 로고
    • Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine
    • Holt, G. D., Snow, C. M., Senior, A., Haltiwanger, R. S., Gerace, L. and Hart, G. W. (1987). Nuclear pore complex glycoproteins contain cytoplasmically disposed O-linked N-acetylglucosamine. J. Cell Biol. 104, 1157-1164.
    • (1987) J. Cell Biol. , vol.104 , pp. 1157-1164
    • Holt, G.D.1    Snow, C.M.2    Senior, A.3    Haltiwanger, R.S.4    Gerace, L.5    Hart, G.W.6
  • 42
    • 0026323478 scopus 로고
    • Toward a more complete 3-D structure of the nuclear pore complex
    • Jarnik, M. and Aebi, U. (1991). Toward a more complete 3-D structure of the nuclear pore complex. J. Struct. Biol. 107, 291-308.
    • (1991) J. Struct. Biol. , vol.107 , pp. 291-308
    • Jarnik, M.1    Aebi, U.2
  • 43
    • 0030764692 scopus 로고    scopus 로고
    • Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively
    • Johnson, A. W. (1997). Rat1p and Xrn1p are functionally interchangeable exoribonucleases that are restricted to and required in the nucleus and cytoplasm, respectively. Mol. Cell Biol. 17, 6122-6130.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6122-6130
    • Johnson, A.W.1
  • 44
    • 0029857203 scopus 로고    scopus 로고
    • Intracellular expression of cellular eIF-5A mutants inhibits HIV-1 replication in human T cells: A feasibility study
    • Junker, U., Bevec, D., Barske, C., Kalfoglou, C., Escaich, S., Dobrovnik, M., Hauber, J. and Böhnlein, E. (1996). Intracellular expression of cellular eIF-5A mutants inhibits HIV-1 replication in human T cells: a feasibility study. Hum. Gene Ther. 7, 1861-1869.
    • (1996) Hum. Gene Ther. , vol.7 , pp. 1861-1869
    • Junker, U.1    Bevec, D.2    Barske, C.3    Kalfoglou, C.4    Escaich, S.5    Dobrovnik, M.6    Hauber, J.7    Böhnlein, E.8
  • 45
    • 0009632793 scopus 로고
    • Effect of initiation factor eIF-5A depletion on cell proliferation and protein synthesis
    • ed. A. J. P. Brown, M. F. Tuite and J. E. G. McCarthy. Berlin, Germany: Springer Verlag
    • Kang, H. A., Schwelberger, H. G. and Hershey, J. W. B. (1993). Effect of initiation factor eIF-5A depletion on cell proliferation and protein synthesis. In Protein Synthesis and Targeting in Yeast. NATO Series H: Cell Biol. (ed. A. J. P. Brown, M. F. Tuite and J. E. G. McCarthy), p. 123. Berlin, Germany: Springer Verlag.
    • (1993) Protein Synthesis and Targeting in Yeast. NATO Series H: Cell Biol. , pp. 123
    • Kang, H.A.1    Schwelberger, H.G.2    Hershey, J.W.B.3
  • 46
    • 0028145708 scopus 로고
    • Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae
    • Kang, H. A. and Hershey, J. W. B. (1994). Effect of initiation factor eIF-5A depletion on protein synthesis and proliferation of Saccharomyces cerevisiae. J. Biol. Chem. 269, 3934-3940.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3934-3940
    • Kang, H.A.1    Hershey, J.W.B.2
  • 47
    • 0028922123 scopus 로고
    • Effects of translation initiation factor eIF-5A on the functioning of human T-cell leukemia virus type I Rex and human immunodeficiency virus Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding
    • Katahira, J., Ishizaki, T., Sakai, H., Adachi, A., Yamamoto, K. and Shida, H. (1995). Effects of translation initiation factor eIF-5A on the functioning of human T-cell leukemia virus type I Rex and human immunodeficiency virus Rev inhibited trans dominantly by a Rex mutant deficient in RNA binding. J. Virol. 69, 3125-3133.
    • (1995) J. Virol. , vol.69 , pp. 3125-3133
    • Katahira, J.1    Ishizaki, T.2    Sakai, H.3    Adachi, A.4    Yamamoto, K.5    Shida, H.6
  • 48
    • 0031239961 scopus 로고    scopus 로고
    • Rapid targeting of nuclear proteins to the cytoplasm
    • Klemm, J. D., Beals, C. R. and Crabtree, G. R. (1997). Rapid targeting of nuclear proteins to the cytoplasm. Curr. Biol. 7, 638-644.
    • (1997) Curr. Biol. , vol.7 , pp. 638-644
    • Klemm, J.D.1    Beals, C.R.2    Crabtree, G.R.3
  • 49
    • 0028852113 scopus 로고
    • Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF-5A from HeLa cells
    • Klier, H., Csonga, R., JoÄo, H. C., Eckerskorn, C., Auer, M., Lottspeich, F. and Eder, J. (1995). Isolation and structural characterization of different isoforms of the hypusine-containing protein eIF-5A from HeLa cells. Biochemistry 34, 14693-14702.
    • (1995) Biochemistry , vol.34 , pp. 14693-14702
    • Klier, H.1    Csonga, R.2    JoÄo, H.C.3    Eckerskorn, C.4    Auer, M.5    Lottspeich, F.6    Eder, J.7
  • 50
    • 0027979480 scopus 로고
    • The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc
    • Kraemer, D., Wozniak, R. W., Blobel, G. and Radu, A. (1994). The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc. Nat. Acad. Sci. USA 91, 1519-1523.
    • (1994) Nat. Acad. Sci. USA , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 51
    • 0022721628 scopus 로고
    • Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface
    • Kreis, T. E. (1986). Microinjected antibodies against the cytoplasmic domain of vesicular stomatitis virus glycoprotein block its transport to the cell surface. EMBO J. 5, 931-941.
    • (1986) EMBO J. , vol.5 , pp. 931-941
    • Kreis, T.E.1
  • 52
    • 0021005632 scopus 로고
    • Proteins of pore complex-lamina structures from nuclei and nuclear membranes
    • Krohne, G. and Franke, W. W. (1983). Proteins of pore complex-lamina structures from nuclei and nuclear membranes. Meth. Enzymol. 96, 597-608.
    • (1983) Meth. Enzymol. , vol.96 , pp. 597-608
    • Krohne, G.1    Franke, W.W.2
  • 53
    • 0030701840 scopus 로고    scopus 로고
    • Molecular cloning and cell cycle dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins
    • Kudo, N., Khochbin, S., Nishi, K., Kitano, K., Yanagida, M., Yoshida, M. and Horinouchi, S. (1997). Molecular cloning and cell cycle dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J. Biol. Chem. 272, 29742-29751.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29742-29751
    • Kudo, N.1    Khochbin, S.2    Nishi, K.3    Kitano, K.4    Yanagida, M.5    Yoshida, M.6    Horinouchi, S.7
  • 55
    • 0028206481 scopus 로고
    • A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation
    • Lounsbury, K. M., Beddow, A. L. and Macara, I. G. (1994). A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation. J. Biol. Chem. 269, 11285-11290.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11285-11290
    • Lounsbury, K.M.1    Beddow, A.L.2    Macara, I.G.3
  • 56
    • 0032080831 scopus 로고    scopus 로고
    • Two-way trafficking with Ran
    • Melchior, F. and Gerace, L. (1998). Two-way trafficking with Ran. Trends Cell Biol 8, 175-179.
    • (1998) Trends Cell Biol , vol.8 , pp. 175-179
    • Melchior, F.1    Gerace, L.2
  • 57
    • 0030935858 scopus 로고    scopus 로고
    • The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited
    • Middeler, G., Zerf, K., Jenovai, S., Thulig, A., Tschodrich Rotter, M., Kubitscheck, U. and Peters, R. (1997). The tumor suppressor p53 is subject to both nuclear import and export, and both are fast, energy-dependent and lectin-inhibited. Oncogene 14, 1407-1417.
    • (1997) Oncogene , vol.14 , pp. 1407-1417
    • Middeler, G.1    Zerf, K.2    Jenovai, S.3    Thulig, A.4    Tschodrich Rotter, M.5    Kubitscheck, U.6    Peters, R.7
  • 58
    • 0028170744 scopus 로고
    • Purification of a Ran-interacting protein that is required for protein import into the nucleus
    • Moore, M. S. and Blobel, G. (1994). Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc. Nat. Acad. Sci. USA 91, 10212-10216.
    • (1994) Proc. Nat. Acad. Sci. USA , vol.91 , pp. 10212-10216
    • Moore, M.S.1    Blobel, G.2
  • 59
    • 0029745374 scopus 로고    scopus 로고
    • An RNA-export mediator with an essential nuclear export signal
    • Murphy, R. and Wente, S. R. (1996). An RNA-export mediator with an essential nuclear export signal. Nature 383, 357-360.
    • (1996) Nature , vol.383 , pp. 357-360
    • Murphy, R.1    Wente, S.R.2
  • 60
    • 0030570091 scopus 로고    scopus 로고
    • Role of the nuclear transport factor plO in nuclear import
    • Nehrbass, U. and Blobel, G. (1996). Role of the nuclear transport factor plO in nuclear import. Science 272, 120-122.
    • (1996) Science , vol.272 , pp. 120-122
    • Nehrbass, U.1    Blobel, G.2
  • 61
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg, E. A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386, 779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 62
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno, M., Fornerod, M. and Mattaj, I. W. (1998). Nucleocytoplasmic transport: the last 200 nanometers. Cell 92, 327-336.
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 63
    • 0030748907 scopus 로고    scopus 로고
    • Evidence for a role of CRM1 in signal-mediated nuclear protein export
    • Ossareh-Nazari, B., Bachelerie, F. and Dargemont, C. (1997). Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science 278, 141-144.
    • (1997) Science , vol.278 , pp. 141-144
    • Ossareh-Nazari, B.1    Bachelerie, F.2    Dargemont, C.3
  • 64
    • 0029922169 scopus 로고    scopus 로고
    • Molecular dissection of the nuclear pore complex
    • Pante, N. and Aebi, U. (1996). Molecular dissection of the nuclear pore complex. Crit. Rev. Biochem. Mol. Biol. 31, 153-199.
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 153-199
    • Pante, N.1    Aebi, U.2
  • 65
    • 0024418120 scopus 로고
    • The essential role of hypusine in eukaryotic translation initiation factor 4D (eIF-4D)
    • Park, M. H. (1989). The essential role of hypusine in eukaryotic translation initiation factor 4D (eIF-4D). J. Biol. Chem. 264, 18531-18535.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18531-18535
    • Park, M.H.1
  • 66
    • 0027197906 scopus 로고
    • Hypusine: Its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation
    • Park, M. H., Wolff, E. C. and Folk, J. E. (1993a). Hypusine: its post-translational formation in eukaryotic initiation factor 5A and its potential role in cellular regulation. BioFactors 4, 95-104.
    • (1993) BioFactors , vol.4 , pp. 95-104
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 67
    • 0027370986 scopus 로고
    • Is hypusine essential for eukaryotic cell proliferation?
    • Park, M. H., Wolff, E. C. and Folk, J. E. (1993b). Is hypusine essential for eukaryotic cell proliferation? Trends Biochem. Sci. 18, 475-479.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 475-479
    • Park, M.H.1    Wolff, E.C.2    Folk, J.E.3
  • 68
    • 0029027836 scopus 로고
    • Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62
    • Paschal, B. M. 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.
    • (1995) J. Cell Biol. , vol.129 , pp. 925-937
    • Paschal, B.M.1    Gerace, L.2
  • 69
    • 0030764959 scopus 로고    scopus 로고
    • High levels of the GTPase Ran/TC4 relieve the requirement for nuclear protein transport factor 2
    • Paschal, B. M., Fritze, C., Guan, T. and Gerace, L. (1997). High levels of the GTPase Ran/TC4 relieve the requirement for nuclear protein transport factor 2. J. Biol. Chem. 272, 21534-21539.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21534-21539
    • Paschal, B.M.1    Fritze, C.2    Guan, T.3    Gerace, L.4
  • 71
    • 0002272634 scopus 로고
    • The three-dimensional structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy
    • Ris, H. (1991). The three-dimensional structure of the nuclear pore complex as seen by high voltage electron microscopy and high resolution low voltage scanning electron microscopy. EMSA Bulletin 21, 54-56.
    • (1991) EMSA Bulletin , vol.21 , pp. 54-56
    • Ris, H.1
  • 72
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth, J., Dobbelstein, M., Freedman, D. A., Shenk, T. and Levine, A. J. (1998). Nucleo-cytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J. 17, 554-564.
    • (1998) EMBO J. , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 75
    • 0024509495 scopus 로고
    • Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein
    • Smit-McBride, Z., Dever, T. E., Hershey, J. W. B. and Merrick, W. C. (1989a). Sequence determination and cDNA cloning of eukaryotic initiation factor 4D, the hypusine-containing protein. J. Biol. Chem. 264, 1578-1583.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1578-1583
    • Smit-McBride, Z.1    Dever, T.E.2    Hershey, J.W.B.3    Merrick, W.C.4
  • 77
    • 0023257987 scopus 로고
    • Monoclonal antibodies identify a group of nuclear pore complex glycoproteins
    • Snow, C. M., Senior, A. and Gerace, L. (1987). Monoclonal antibodies identify a group of nuclear pore complex glycoproteins. J. Cell Biol. 104, 1143-1156.
    • (1987) J. Cell Biol. , vol.104 , pp. 1143-1156
    • Snow, C.M.1    Senior, A.2    Gerace, L.3
  • 78
    • 0030985459 scopus 로고    scopus 로고
    • Exportin 1 (Crm1p) is an essential nuclear export factor
    • Stade, K., Ford, C. S., Guthrie, C. and Weis, K. (1997). Exportin 1 (Crm1p) is an essential nuclear export factor. Cell 90, 1041-1050.
    • (1997) Cell , vol.90 , pp. 1041-1050
    • Stade, K.1    Ford, C.S.2    Guthrie, C.3    Weis, K.4
  • 79
    • 0029923982 scopus 로고    scopus 로고
    • A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus
    • Stutz, F., Izaurralde, E., Mattaj, I. W. and Rosbash, M. (1996). 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. 16, 7144-7150.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 7144-7150
    • Stutz, F.1    Izaurralde, E.2    Mattaj, I.W.3    Rosbash, M.4
  • 80
    • 0004875492 scopus 로고
    • An octamer of histones in chromatin and free in solution
    • Thomas, J. O. and Kornberg, R. D. (1975). An octamer of histones in chromatin and free in solution. Proc. Nat. Acad. Sci. USA 72, 2626-2630.
    • (1975) Proc. Nat. Acad. Sci. USA , vol.72 , pp. 2626-2630
    • Thomas, J.O.1    Kornberg, R.D.2
  • 81
    • 0026560593 scopus 로고
    • The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dekcan mRNA
    • von Lindern, M., Fornerod, M., van Baal, S., Jaegle, M., de Wit, T., Buijs, A. and Grosveld, G. (1992). The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dekcan mRNA. Mol. Cell Biol. 12, 1687-1697.
    • (1992) Mol. Cell Biol. , vol.12 , pp. 1687-1697
    • Von Lindern, M.1    Fornerod, M.2    Van Baal, S.3    Jaegle, M.4    De Wit, T.5    Buijs, A.6    Grosveld, G.7
  • 82
    • 0029130168 scopus 로고
    • Identification of a signal for rapid export of proteins from the nucleus
    • Wen, W., Meinkoth, J. L., Tsien, R. Y. and Taylor, S. S. (1995). Identification of a signal for rapid export of proteins from the nucleus. Cell 82, 463-473.
    • (1995) Cell , vol.82 , pp. 463-473
    • Wen, W.1    Meinkoth, J.L.2    Tsien, R.Y.3    Taylor, S.S.4
  • 83
    • 0028802811 scopus 로고
    • Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex
    • Wilken, N., Senecal, J. L., Scheer, U. and Dabauvalle, M. C. (1995). Localization of the Ran-GTP binding protein RanBP2 at the cytoplasmic side of the nuclear pore complex. Eur. J Cell Biol. 68, 211-219.
    • (1995) Eur. J Cell Biol. , vol.68 , pp. 211-219
    • Wilken, N.1    Senecal, J.L.2    Scheer, U.3    Dabauvalle, M.C.4
  • 84
    • 0031079648 scopus 로고    scopus 로고
    • 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
    • Wolff, B., Sanglier, J. J. and Wang, Y. (1997). 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. 4, 139-147.
    • (1997) Chem. Biol. , vol.4 , pp. 139-147
    • Wolff, B.1    Sanglier, J.J.2    Wang, Y.3
  • 85
    • 0032528001 scopus 로고    scopus 로고
    • Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1
    • Yang, J., Bardes, E. S. G., Moore, J. D., Brennan, J., Powers, M. A. and Kornbluth, S. (1998). Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev. 12, 2131-2143.
    • (1998) Genes Dev. , vol.12 , pp. 2131-2143
    • Yang, J.1    Bardes, E.S.G.2    Moore, J.D.3    Brennan, J.4    Powers, M.A.5    Kornbluth, S.6
  • 86
    • 0032525327 scopus 로고    scopus 로고
    • A single amino acid substitution in yeast e1F-5A results in mRNA stabilization
    • Zuk, D. and Jacobson, A. (1998). A single amino acid substitution in yeast e1F-5A results in mRNA stabilization. EMBO J. 17, 2914-2925.
    • (1998) EMBO J. , vol.17 , pp. 2914-2925
    • Zuk, D.1    Jacobson, A.2


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