메뉴 건너뛰기




Volumn 22, Issue 21, 2003, Pages 5928-5940

Exportin 6: A novel nuclear export receptor that is specific for profilin-actin complexes

Author keywords

Actin; Exportin; Nuclear pore complex; Profilin; RanGTPase

Indexed keywords

ACTIN; CARRIER PROTEIN; CELL NUCLEUS RECEPTOR; EXPORTIN 6; KARYOPHERIN BETA; NUCLEOTIDE; PROFILIN; RNA; UNCLASSIFIED DRUG;

EID: 0242641546     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdg565     Document Type: Article
Times cited : (265)

References (61)
  • 1
    • 0032510462 scopus 로고    scopus 로고
    • Identification of a nuclear export receptor for tRNA
    • Arts, G.J., Fomerod, M. and Mattaj, I.W. (1998) Identification of a nuclear export receptor for tRNA. Curr. Biol., 8, 305-314.
    • (1998) Curr. Biol. , vol.8 , pp. 305-314
    • Arts, G.J.1    Fomerod, M.2    Mattaj, I.W.3
  • 2
    • 0345647103 scopus 로고    scopus 로고
    • RanBP1 is crucial for the release of RanGTP from importin β-related nuclear transport factors
    • Bischoff, F.R. and Görlich, D. (1997) RanBP1 is crucial for the release of RanGTP from importin β-related nuclear transport factors. FEBS Lett., 419, 249-254.
    • (1997) FEBS Lett. , vol.419 , pp. 249-254
    • Bischoff, F.R.1    Görlich, D.2
  • 3
    • 0037112790 scopus 로고    scopus 로고
    • Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm
    • Bohnsack, M.T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E. and Görlich, D. (2002) Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J., 21, 6205-6215.
    • (2002) EMBO J. , vol.21 , pp. 6205-6215
    • Bohnsack, M.T.1    Regener, K.2    Schwappach, B.3    Saffrich, R.4    Paraskeva, E.5    Hartmann, E.6    Görlich, D.7
  • 4
    • 0037112842 scopus 로고    scopus 로고
    • Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
    • Calado, A., Treichel, N., Muller, E.C., Otto, A. and Kutay, U. (2002) Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA. EMBO J., 21, 6216-6224.
    • (2002) EMBO J. , vol.21 , pp. 6216-6224
    • Calado, A.1    Treichel, N.2    Muller, E.C.3    Otto, A.4    Kutay, U.5
  • 6
    • 84886632310 scopus 로고
    • Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells
    • Carlsson, L., Nystrom, L.E., Sundkvist, I., Markey, F. and Lindberg, U. (1977) Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells. J. Mol. Biol., 115, 465-483.
    • (1977) J. Mol. Biol. , vol.115 , pp. 465-483
    • Carlsson, L.1    Nystrom, L.E.2    Sundkvist, I.3    Markey, F.4    Lindberg, U.5
  • 7
    • 0017716157 scopus 로고
    • Diffusible and bound actin nuclei of Xenopus laevis oocytes
    • Clark, T.G. and Merriam, R.W. (1977) Diffusible and bound actin nuclei of Xenopus laevis oocytes. Cell, 12, 883-891.
    • (1977) Cell , vol.12 , pp. 883-891
    • Clark, T.G.1    Merriam, R.W.2
  • 8
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • Conti, E. and Izaurralde, E. (2001) Nucleocytoplasmic transport enters the atomic age. Curr. Opin. Cell Biol., 13, 310-319.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 9
    • 0016698833 scopus 로고
    • Interaction of actin with phalloidin: Polymerization and stabilization of F-actin
    • Dancker, P., Low, I., Hasselbach, W. and Wieland, T. (1975) Interaction of actin with phalloidin: polymerization and stabilization of F-actin. Biochim. Biophys. Acta, 400, 407-414.
    • (1975) Biochim. Biophys. Acta , vol.400 , pp. 407-414
    • Dancker, P.1    Low, I.2    Hasselbach, W.3    Wieland, T.4
  • 10
    • 0030851465 scopus 로고    scopus 로고
    • Disassembly of RanGTP-karyopherin β ?complex, an intermediate in nuclear protein import
    • Floer, M., Blobel, G. and Rexach, M. (1997) Disassembly of RanGTP-karyopherin β ?complex, an intermediate in nuclear protein import. J. Biol. Chem., 272, 19538-19546.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19538-19546
    • Floer, M.1    Blobel, G.2    Rexach, M.3
  • 11
    • 0030924190 scopus 로고    scopus 로고
    • Crm1 is an export receptor for leucine rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M. and Mattaj, I.W. (1997a) Crm1 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
  • 12
    • 0031053791 scopus 로고    scopus 로고
    • The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88
    • Fomerod, 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 CRM1 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
    • Fomerod, 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
  • 14
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich, D. and Kutay, U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell. Dev. Biol., 15, 607-660.
    • (1999) Annu. Rev. Cell. Dev. Biol. , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 15
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Görlich, D., Pante, N., Kutay, U., Aebi, U. and Bischoff, F.R. (1996) Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J., 15, 5584-5594.
    • (1996) EMBO J. , vol.15 , pp. 5584-5594
    • Görlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 16
    • 0037416225 scopus 로고    scopus 로고
    • Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation
    • Görlich, D., Seewald, M.J. and Ribbeck, K. (2003) Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J., 22, 1088-1100.
    • (2003) EMBO J. , vol.22 , pp. 1088-1100
    • Görlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 18
    • 0037062951 scopus 로고    scopus 로고
    • RNA interference
    • Hannon, G.J. (2002) RNA interference. Nature, 418, 244-251.
    • (2002) Nature , vol.418 , pp. 244-251
    • Hannon, G.J.1
  • 19
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt, M.R. and Koffer, A. (2001) Cell motility: proline-rich proteins promote protrusions. Trends Cell. Biol., 11, 38-46.
    • (2001) Trends Cell. Biol. , vol.11 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 20
    • 0034521121 scopus 로고    scopus 로고
    • Diversity in nucleocytoplasmic transport pathways
    • Imamoto, N. (2000) Diversity in nucleocytoplasmic transport pathways. Cell Struct. Funct., 25, 207-216.
    • (2000) Cell Struct. Funct. , vol.25 , pp. 207-216
    • Imamoto, N.1
  • 21
    • 0036370968 scopus 로고    scopus 로고
    • Nuclear export of messenger RNA
    • Izaurralde, E. (2002) Nuclear export of messenger RNA. Results Probl. Cell Differ., 35, 133-150.
    • (2002) Results Probl. Cell Differ. , vol.35 , pp. 133-150
    • Izaurralde, E.1
  • 22
    • 0030856315 scopus 로고    scopus 로고
    • The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus
    • Izaurralde, E., Kutay, U., von Kobbe, C., Mattaj, I.W. and Görlich, D. (1997) The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J., 16, 6535-6547.
    • (1997) EMBO J. , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    Von Kobbe, C.3    Mattaj, I.W.4    Görlich, D.5
  • 24
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • Kalab, P., Weis, K. and Heald, R. (2002) Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science, 295, 2452-2456.
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 25
    • 0342276108 scopus 로고    scopus 로고
    • Export of importin α from the nucleus is mediated by a specific nuclear transport factor
    • Kutay, U., Bischoff, F.R., Kostka, S., Kraft, R. and Görlich, D. (1997) Export of importin α from the nucleus is mediated by a specific nuclear transport factor. Cell, 90, 1061-1071.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Görlich, D.5
  • 27
    • 0033781583 scopus 로고    scopus 로고
    • Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties
    • Lambrechts, A. et al. (2000) Profilin II is alternatively spliced, resulting in profilin isoforms that are differentially expressed and have distinct biochemical properties. Mol. Cell. Biol., 20, 8209-8219.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 8209-8219
    • Lambrechts, A.1
  • 28
    • 0036196670 scopus 로고    scopus 로고
    • Protein and RNA export from the nucleus
    • Lei, E.P. and Silver, P.A. (2002) Protein and RNA export from the nucleus. Dev. Cell, 2, 261-272.
    • (2002) Dev. Cell , vol.2 , pp. 261-272
    • Lei, E.P.1    Silver, P.A.2
  • 29
    • 0026271760 scopus 로고
    • DNA replication in cell-free extracts from Xenopus laevis
    • Leno, G.H. and Laskey, R.A. (1991) DNA replication in cell-free extracts from Xenopus laevis. Methods Cell Biol., 36, 561-579.
    • (1991) Methods Cell Biol. , vol.36 , pp. 561-579
    • Leno, G.H.1    Laskey, R.A.2
  • 31
    • 0035163855 scopus 로고    scopus 로고
    • Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast
    • Lu, J. and Pollard, T.D. (2001) Profilin binding to poly-L-proline and actin monomers along with ability to catalyze actin nucleotide exchange is required for viability of fission yeast. Mol. Biol. Cell, 12, 1161-1175.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1161-1175
    • Lu, J.1    Pollard, T.D.2
  • 32
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I.G. (2001) Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev., 65, 570-594.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 33
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj, I.W. and Englmeier, L. (1998) Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem., 67, 265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 34
    • 0342366294 scopus 로고    scopus 로고
    • Differential colocalization of profilin with microfilaments in PtK2 cells
    • Mayboroda, O., Schluter, K. and Jockusch, B.M. (1997) Differential colocalization of profilin with microfilaments in PtK2 cells. Cell Motil. Cytoskeleton, 37, 166-177.
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 166-177
    • Mayboroda, O.1    Schluter, K.2    Jockusch, B.M.3
  • 35
    • 0035898685 scopus 로고    scopus 로고
    • Importin 13: A novel mediator of nuclear import and export
    • Mingot, J.M., Kostka, S., Kraft, R., Hartmann, E. and Görlich, D. (2001) Importin 13: a novel mediator of nuclear import and export. EMBO J., 20, 3685-3694.
    • (2001) EMBO J. , vol.20 , pp. 3685-3694
    • Mingot, J.M.1    Kostka, S.2    Kraft, R.3    Hartmann, E.4    Görlich, D.5
  • 36
    • 0019194944 scopus 로고
    • Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate
    • Mockrin, S.C. and Korn, E.D. (1980) Acanthamoeba profilin interacts with G-actin to increase the rate of exchange of actin-bound adenosine 5′-triphosphate. Biochemistry, 19, 5359-5362.
    • (1980) Biochemistry , vol.19 , pp. 5359-5362
    • Mockrin, S.C.1    Korn, E.D.2
  • 37
    • 0036308740 scopus 로고    scopus 로고
    • The C-terminal extension of the small GTPase Ran is essential for defining the GDP-bound form
    • Nilsson, J., Weis, K. and Kjems, J. (2002) The C-terminal extension of the small GTPase Ran is essential for defining the GDP-bound form. J. Mol. Biol., 318, 583-593.
    • (2002) J. Mol. Biol. , vol.318 , pp. 583-593
    • Nilsson, J.1    Weis, K.2    Kjems, J.3
  • 38
    • 0019200479 scopus 로고
    • Dimethylsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells
    • Osborn, M. and Weber, K. (1980) Dimethylsulfoxide and the ionophore A23187 affect the arrangement of actin and induce nuclear actin paracrystals in PtK2 cells. Exp. Cell Res., 129, 103-114.
    • (1980) Exp. Cell Res. , vol.129 , pp. 103-114
    • Osborn, M.1    Weber, K.2
  • 39
    • 0024615405 scopus 로고
    • Zygotic lethals with specific maternal effect phenotypes in Drosophila melanogaster. I. Loci on the X chromosome
    • Perrimon, N., Engstrom, L. and Mahowald, A.P. (1989) Zygotic lethals with specific maternal effect phenotypes in Drosophila melanogaster. I. Loci on the X chromosome. Genetics, 121, 333-352.
    • (1989) Genetics , vol.121 , pp. 333-352
    • Perrimon, N.1    Engstrom, L.2    Mahowald, A.P.3
  • 40
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T.D. and Borisy, G.G. (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell, 112, 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 42
    • 0018617361 scopus 로고
    • Acanthamoeba profilin. A protein of low molecular weight from Acanpthamoeba castellanii that inhibits actin nucleation
    • Reichstein, E. and Korn, E.D. (1979) Acanthamoeba profilin. A protein of low molecular weight from Acanpthamoeba castellanii that inhibits actin nucleation. J. Biol. Chem., 254, 6174-6179.
    • (1979) J. Biol. Chem. , vol.254 , pp. 6174-6179
    • Reichstein, E.1    Korn, E.D.2
  • 43
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors and nucleoporins
    • Rexach, M. and Blobel, G. (1995) Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors and nucleoporins. Cell, 83, 683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 44
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck, K. and Görlich, D. (2002) The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J., 21, 2664-2671.
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 46
    • 0019209780 scopus 로고
    • Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide
    • Sanger, J.W., Sanger, J.M., Kreis, T.E. and Jockusch, B.M. (1980) Reversible translocation of cytoplasmic actin into the nucleus caused by dimethyl sulfoxide. Proc. Natl Acad. Sci. USA, 77, 5268-5272.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5268-5272
    • Sanger, J.W.1    Sanger, J.M.2    Kreis, T.E.3    Jockusch, B.M.4
  • 47
    • 0021677114 scopus 로고
    • Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes
    • Scheer, U., Hinssen, H., Franke, W.W. and Jockusch, B.M. (1984) Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes. Cell, 39, 111-122.
    • (1984) Cell , vol.39 , pp. 111-122
    • Scheer, U.1    Hinssen, H.2    Franke, W.W.3    Jockusch, B.M.4
  • 52
    • 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
  • 53
    • 0034913423 scopus 로고    scopus 로고
    • Importin-β-like nuclear transport receptors
    • REVIEWS3008
    • Strom, A.C. and Weis, K. (2001) Importin-β-like nuclear transport receptors. Genome Biol., 2, REVIEWS3008.
    • (2001) Genome Biol. , vol.2
    • Strom, A.C.1    Weis, K.2
  • 54
    • 0022409564 scopus 로고
    • Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin
    • Tanaka, M. and Shibata, H. (1985) Poly(L-proline)-binding proteins from chick embryos are a profilin and a profilactin. Eur. J. Biochem., 151, 291-297.
    • (1985) Eur. J. Biochem. , vol.151 , pp. 291-297
    • Tanaka, M.1    Shibata, H.2
  • 55
    • 0032536820 scopus 로고    scopus 로고
    • Nuclear export of actin: A novel mechanism regulating the subcellular localization of a major cytoskeletal protein
    • Wada, A., Fukuda, M., Mishima, M. and Nishida, E. (1998) Nuclear export of actin: a novel mechanism regulating the subcellular localization of a major cytoskeletal protein. EMBO J., 17, 1635-1641.
    • (1998) EMBO J. , vol.17 , pp. 1635-1641
    • Wada, A.1    Fukuda, M.2    Mishima, M.3    Nishida, E.4
  • 56
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis, K. (2003) Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell, 112, 441-451.
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 57
    • 0031021153 scopus 로고    scopus 로고
    • Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes
    • Welch, M.D., Iwamatsu, A. and Mitchison, T.J. (1997) Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature, 385, 265-269.
    • (1997) Nature , vol.385 , pp. 265-269
    • Welch, M.D.1    Iwamatsu, A.2    Mitchison, T.J.3
  • 58
    • 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
  • 59
  • 61
    • 0019064554 scopus 로고
    • Isolation of polymerization-competent cytoplasmic actin by affinity chromatography on immobilized DNAse I using formamide as eluant
    • Zechel, K. (1980) Isolation of polymerization-competent cytoplasmic actin by affinity chromatography on immobilized DNAse I using formamide as eluant. Eur. J. Biochem., 110, 343-348.
    • (1980) Eur. J. Biochem. , vol.110 , pp. 343-348
    • Zechel, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.