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Volumn 8, Issue 3, 2007, Pages 195-208

Molecular mechanism of the nuclear protein import cycle

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR PROTEIN;

EID: 33847176295     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm2114     Document Type: Review
Times cited : (727)

References (99)
  • 1
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Görlich, D. & Kutay, U. Transport between the cell nucleus and the cytoplasm. Ann. Rev. Cell Dev. Biol. 15, 607-660 (1999).
    • (1999) Ann. Rev. Cell Dev. Biol , vol.15 , pp. 607-660
    • Görlich, D.1    Kutay, U.2
  • 2
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • Macara, I. G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65, 570-594 (2001).
    • (2001) Microbiol. Mol. Biol. Rev , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 4
    • 0035370948 scopus 로고    scopus 로고
    • Nuclear transport enters the atomic age
    • Conti, E. & Izaurralde, E. Nuclear transport enters the atomic age. Curr. Opin. Cell Biol. 13, 310-319 (2001).
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 5
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • Fahrenkrog, B. & Aebi, U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nature Rev. Mol. Cell Biol. 4, 757-766 (2003).
    • (2003) Nature Rev. Mol. Cell Biol , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 6
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast, N. & Pemberton, L. F. Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14, 547-556 (2004).
    • (2004) Trends Cell Biol , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 7
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton, L. F. & Paschal, B. M. Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6, 187-198 (2005).
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 8
    • 33645015535 scopus 로고    scopus 로고
    • Nuclear transport is becoming crystal clear
    • Madrid, A. S. & Weis, K. Nuclear transport is becoming crystal clear. Chromosoma 115, 98-109 (2006).
    • (2006) Chromosoma , vol.115 , pp. 98-109
    • Madrid, A.S.1    Weis, K.2
  • 9
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti, E., Müller, C. W. & Stewart, M. Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 16, 237-244 (2006).
    • (2006) Curr. Opin. Struct. Biol , vol.16 , pp. 237-244
    • Conti, E.1    Müller, C.W.2    Stewart, M.3
  • 10
    • 0035827319 scopus 로고    scopus 로고
    • Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
    • Stewart, M. et al. Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. FEBS Lett. 498, 145-149 (2001).
    • (2001) FEBS Lett , vol.498 , pp. 145-149
    • Stewart, M.1
  • 11
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle
    • Weis, K. Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle. Cell 112, 441-451 (2003).
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 12
    • 0035691870 scopus 로고    scopus 로고
    • Regulation of functional nuclear pores size in fibroblasts
    • Feldherr, C. M., Akin, D. & Cohen, R. J. Regulation of functional nuclear pores size in fibroblasts. J. Cell Sci. 114, 4621-4627 (2001).
    • (2001) J. Cell Sci , vol.114 , pp. 4621-4627
    • Feldherr, C.M.1    Akin, D.2    Cohen, R.J.3
  • 13
    • 0027989786 scopus 로고
    • Pores for thought: Nuclear pore complex proteins
    • Rout, M. P. & Wente, S. R. Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4, 357-365 (1994).
    • (1994) Trends Cell Biol , vol.4 , pp. 357-365
    • Rout, M.P.1    Wente, S.R.2
  • 14
    • 0034695924 scopus 로고    scopus 로고
    • Rout, M. P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651 (2000). A landmark paper that established the complete protein composition of yeast NPCs together with the location of each nucleoporin as determined by electron microscopy. The authors also proposed an entropic gating mechanism to prevent entry of inappropriate material into the NPC transport channel.
    • Rout, M. P. et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651 (2000). A landmark paper that established the complete protein composition of yeast NPCs together with the location of each nucleoporin as determined by electron microscopy. The authors also proposed an entropic gating mechanism to prevent entry of inappropriate material into the NPC transport channel.
  • 16
    • 33751222250 scopus 로고    scopus 로고
    • Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo
    • Timney, B. L. et al. Simple kinetic relationships and nonspecific competition govern nuclear import rates in vivo. J. Cell Biol. 175, 579-593 (2006).
    • (2006) J. Cell Biol , vol.175 , pp. 579-593
    • Timney, B.L.1
  • 17
    • 0035897406 scopus 로고    scopus 로고
    • Nuclear import of histone H2A and H2B is mediated by a network of karyopherins
    • Mosammaparast, N. et al. Nuclear import of histone H2A and H2B is mediated by a network of karyopherins. J. Cell Biol. 153, 251-262 (2001).
    • (2001) J. Cell Biol , vol.153 , pp. 251-262
    • Mosammaparast, N.1
  • 18
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherinβ2
    • Lee, B. J. et al. Rules for nuclear localization sequence recognition by karyopherinβ2. Cell 126, 543-558 (2006).
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1
  • 19
    • 0035869022 scopus 로고    scopus 로고
    • Ribbeck, K. & Görlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (2001). Presents a careful analysis of nuclear protein import kinetics and proposes a selective phase model based on the formation of a hydrogel formed by interactions between the hydrophobic cores of FG repeats.
    • Ribbeck, K. & Görlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (2001). Presents a careful analysis of nuclear protein import kinetics and proposes a selective phase model based on the formation of a hydrogel formed by interactions between the hydrophobic cores of FG repeats.
  • 21
    • 0032585533 scopus 로고    scopus 로고
    • Nuclear import of Ran is mediated by the transport factor NTF2
    • Smith, A. E., Brownawell, A. & Macara, I. G. Nuclear import of Ran is mediated by the transport factor NTF2. Curr. Biol. 8, 1403-1406 (1998).
    • (1998) Curr. Biol , vol.8 , pp. 1403-1406
    • Smith, A.E.1    Brownawell, A.2    Macara, I.G.3
  • 22
    • 0032563246 scopus 로고    scopus 로고
    • Conti, E., Uy, M., Leighton, L., Blobel, G. & Kuriyan, J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α. Cell 94, 193-204 (1998). Pioneering determination of the structure of yeast importin-α and the way in which it binds NLSs.
    • Conti, E., Uy, M., Leighton, L., Blobel, G. & Kuriyan, J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin-α. Cell 94, 193-204 (1998). Pioneering determination of the structure of yeast importin-α and the way in which it binds NLSs.
  • 23
    • 0034653375 scopus 로고    scopus 로고
    • Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin-α
    • Conti, E. & Kuriyan, J. Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin-α. Structure Fold. Des. 8, 329-338 (2000).
    • (2000) Structure Fold. Des , vol.8 , pp. 329-338
    • Conti, E.1    Kuriyan, J.2
  • 24
    • 0034646565 scopus 로고    scopus 로고
    • Fontes, M. R., The, T. & Kobe, B. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α. J. Mol. Biol. 297, 1183-1194 (2000).
    • Fontes, M. R., The, T. & Kobe, B. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α. J. Mol. Biol. 297, 1183-1194 (2000).
  • 25
    • 0035847008 scopus 로고    scopus 로고
    • Dissection of a nuclear localization signal
    • Hodel, M. R., Corbett, A. H. & Hodel, A. E. Dissection of a nuclear localization signal. J. Biol. Chem. 276, 1317-1325 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 1317-1325
    • Hodel, M.R.1    Corbett, A.H.2    Hodel, A.E.3
  • 26
    • 0035823482 scopus 로고    scopus 로고
    • Biophysical characterization of interactions involving importin-α during nuclear import
    • Catimel, B. et al. Biophysical characterization of interactions involving importin-α during nuclear import. J. Biol. Chem. 276, 34189-34198 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 34189-34198
    • Catimel, B.1
  • 27
    • 33745674259 scopus 로고    scopus 로고
    • A cytotoxic ribonuclease variant with a discontinuous nuclear localization signal constituted by basic residues scattered over three areas of the molecule
    • Rodriguez, M. et al. A cytotoxic ribonuclease variant with a discontinuous nuclear localization signal constituted by basic residues scattered over three areas of the molecule. J. Mol. Biol. 360, 548-557 (2006).
    • (2006) J. Mol. Biol , vol.360 , pp. 548-557
    • Rodriguez, M.1
  • 28
    • 0345374584 scopus 로고    scopus 로고
    • The structure of importin-β bound to SREBP-2: Nuclear import of a transcription factor
    • Lee, S. J. et al. The structure of importin-β bound to SREBP-2: nuclear import of a transcription factor. Science 302, 1571-1575 (2003).
    • (2003) Science , vol.302 , pp. 1571-1575
    • Lee, S.J.1
  • 29
    • 0036923972 scopus 로고    scopus 로고
    • Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β
    • Cingolani, G., Bednenko, J., Gillespie, M. T. & Gerace, L. Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β. Mol. Cell 10, 1345-1353 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 1345-1353
    • Cingolani, G.1    Bednenko, J.2    Gillespie, M.T.3    Gerace, L.4
  • 30
    • 0029921174 scopus 로고    scopus 로고
    • 41 amino acid motif in importin-α confers binding to importin-β and hence transit into the nucleus
    • Görlich, D., Henklein, P., Laskey, R. A. & Hartmann, E. A 41 amino acid motif in importin-α confers binding to importin-β and hence transit into the nucleus. EMBO J. 15, 1810-1817 (1996).
    • (1996) EMBO J , vol.15 , pp. 1810-1817
    • Görlich, D.1    Henklein, P.2    Laskey, R.A.3    Hartmann, E.A.4
  • 31
    • 0030010107 scopus 로고    scopus 로고
    • The conserved amino-terminal domain of hSRP1 α is essential for nuclear protein import
    • Weis, K., Ryder, U. & Lamond, A. I. The conserved amino-terminal domain of hSRP1 α is essential for nuclear protein import. EMBO J. 15, 1818-1825 (1996).
    • (1996) EMBO J , vol.15 , pp. 1818-1825
    • Weis, K.1    Ryder, U.2    Lamond, A.I.3
  • 32
    • 0032950628 scopus 로고    scopus 로고
    • Kobe, B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α. Nature Struct. Biol. 6, 388-397 (1999). Pioneering structural paper that proposed how the importin-α IBB domain could have an autoinhibitory function that facilitates cargo release in the nucleus.
    • Kobe, B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α. Nature Struct. Biol. 6, 388-397 (1999). Pioneering structural paper that proposed how the importin-α IBB domain could have an autoinhibitory function that facilitates cargo release in the nucleus.
  • 33
    • 11144257756 scopus 로고    scopus 로고
    • Matsuura, Y. & Stewart, M. Structural basis for the assembly of a nuclear export complex. Nature 432, 872-877 (2004). Describes the structure of the yeast CAS:RanGTP: importin-α complex, showing the central role of the IBB domain in preventing futile cycles in which cargo is returned to the cytoplasm. Also proposes a spring-loaded model to account for how karyopherin flexibility can mediate the release of importin-α following GTP hydrolysis on Ran.
    • Matsuura, Y. & Stewart, M. Structural basis for the assembly of a nuclear export complex. Nature 432, 872-877 (2004). Describes the structure of the yeast CAS:RanGTP: importin-α complex, showing the central role of the IBB domain in preventing futile cycles in which cargo is returned to the cytoplasm. Also proposes a spring-loaded model to account for how karyopherin flexibility can mediate the release of importin-α following GTP hydrolysis on Ran.
  • 34
    • 0142073738 scopus 로고    scopus 로고
    • Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import
    • Matsuura, Y., Lange, A., Harreman, M. T., Corbett, A. H. & Stewart, M. Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J. 22, 5358-5369 (2003).
    • (2003) EMBO J , vol.22 , pp. 5358-5369
    • Matsuura, Y.1    Lange, A.2    Harreman, M.T.3    Corbett, A.H.4    Stewart, M.5
  • 35
    • 27744577638 scopus 로고    scopus 로고
    • Matsuura, Y. & Stewart, M. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 24, 3681-3689 (2005). Demonstration of active displacement of cargo from importin-α by NUP50 and how this can generate a molecular ratchet to prevent futile cycles.
    • Matsuura, Y. & Stewart, M. Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 24, 3681-3689 (2005). Demonstration of active displacement of cargo from importin-α by NUP50 and how this can generate a molecular ratchet to prevent futile cycles.
  • 37
    • 33747697156 scopus 로고    scopus 로고
    • Nuclear localization signal-receptor affinity correlates with in vivo localization in S. cerevisiae
    • Hodel, H. E. et al. Nuclear localization signal-receptor affinity correlates with in vivo localization in S. cerevisiae. J. Biol. Chem. 281, 23545-23556 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 23545-23556
    • Hodel, H.E.1
  • 38
    • 4444284306 scopus 로고    scopus 로고
    • Yang, W., Gelles, J. & Musser, S. M. Imaging of single-molecule translocation through nuclear pore complexes. Proc. Natl Acad. Sci. USA 101, 12887-12892 (2004). Direct demonstration of the random-walk diffusion of import complexes in the central transport channel of NPCs.
    • Yang, W., Gelles, J. & Musser, S. M. Imaging of single-molecule translocation through nuclear pore complexes. Proc. Natl Acad. Sci. USA 101, 12887-12892 (2004). Direct demonstration of the random-walk diffusion of import complexes in the central transport channel of NPCs.
  • 39
    • 13844264432 scopus 로고    scopus 로고
    • Nuclear transport of single molecules: Dwell times at the nuclear pore complex
    • Kubitscheck, U. et al. Nuclear transport of single molecules: dwell times at the nuclear pore complex. J. Cell Biol. 168, 233-243 (2005).
    • (2005) J. Cell Biol , vol.168 , pp. 233-243
    • Kubitscheck, U.1
  • 40
    • 33749023069 scopus 로고    scopus 로고
    • Nuclear import time and transport efficiency depend on importin β concentration
    • Wang, W. & Musser, S. M. Nuclear import time and transport efficiency depend on importin β concentration. J. Cell Biol. 174, 951-961 (2006).
    • (2006) J. Cell Biol , vol.174 , pp. 951-961
    • Wang, W.1    Musser, S.M.2
  • 41
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTF2 and xFxFG nucleoporins is required for the nuclear import of RanGDP
    • Bayliss, R. et al. Interaction between NTF2 and xFxFG nucleoporins is required for the nuclear import of RanGDP. J. Mol. Biol. 293, 579-593 (1999).
    • (1999) J. Mol. Biol , vol.293 , pp. 579-593
    • Bayliss, R.1
  • 42
    • 0034616910 scopus 로고    scopus 로고
    • Bayliss, R., Littlewood, T. & Stewart, M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102, 99-108 (2000). Describes the structural basis for the interaction between importin-β and FG-nucleoporin cores.
    • Bayliss, R., Littlewood, T. & Stewart, M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102, 99-108 (2000). Describes the structural basis for the interaction between importin-β and FG-nucleoporin cores.
  • 43
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-β
    • Bayliss, R., Littlewood, T., Strawn, L. A., Wente, S. R. & Stewart, M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-β. J. Biol. Chem. 277, 50597-50606 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 50597-50606
    • Bayliss, R.1    Littlewood, T.2    Strawn, L.A.3    Wente, S.R.4    Stewart, M.5
  • 44
    • 0037124352 scopus 로고    scopus 로고
    • Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats
    • Bayliss, R. et al. Structural basis for the interaction between NTF2 and nucleoporin FxFG repeats. EMBO J. 21, 2843-2853 (2002).
    • (2002) EMBO J , vol.21 , pp. 2843-2853
    • Bayliss, R.1
  • 45
    • 0034800318 scopus 로고    scopus 로고
    • Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor
    • Fribourg, S. Braun, I. C., Izaurralde, E. & Conti, E. Structural basis for the recognition of a nucleoporin FG repeat by the NTF2-like domain of the TAP/p15 mRNA nuclear export factor. Mol. Cell 8, 645-656 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 645-656
    • Fribourg, S.1    Braun, I.C.2    Izaurralde, E.3    Conti, E.4
  • 46
    • 0037459067 scopus 로고    scopus 로고
    • Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1Å resolution
    • Grant, R. P., Neuhaus, D. N. & Stewart, M. Structural basis for the interaction between the Tap/NXF1 UBA domain and FG nucleoporins at 1Å resolution. J. Mol. Biol. 326, 849-858 (2003).
    • (2003) J. Mol. Biol , vol.326 , pp. 849-858
    • Grant, R.P.1    Neuhaus, D.N.2    Stewart, M.3
  • 47
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach, M. & Blobel, G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83, 683-692 (1995).
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 48
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck, K. & Görlich, D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 21, 2664-2671 (2002).
    • (2002) EMBO J , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Görlich, D.2
  • 49
    • 0035794237 scopus 로고    scopus 로고
    • The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex
    • Strawn, L. A., Shen, T. & Wente, S. R. The GLFG regions of Nup116p and Nup100p serve as binding sites for both Kap95p and Mex67p at the nuclear pore complex. J. Biol. Chem. 276, 6445-6452 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 6445-6452
    • Strawn, L.A.1    Shen, T.2    Wente, S.R.3
  • 50
    • 1542609480 scopus 로고    scopus 로고
    • Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S. & Wente, S. R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nature Cell Biol. 6, 197-206 (2004). Exploration of the importance of the FG-repeat regions of nucleoporins using an innovative method for deleting these regions in S. cerevisiae. Whereas up to half the mass of FG repeats can be deleted using particular groups of nucleoporins, deletion from several selected nucleoporins has a marked effect.
    • Strawn, L. A., Shen, T., Shulga, N., Goldfarb, D. S. & Wente, S. R. Minimal nuclear pore complexes define FG repeat domains essential for transport. Nature Cell Biol. 6, 197-206 (2004). Exploration of the importance of the FG-repeat regions of nucleoporins using an innovative method for deleting these regions in S. cerevisiae. Whereas up to half the mass of FG repeats can be deleted using particular groups of nucleoporins, deletion from several selected nucleoporins has a marked effect.
  • 51
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic nuclear pore complexes: Life on the edge
    • Tran, E. J. & Wente, S. R. Dynamic nuclear pore complexes: life on the edge. Cell 125, 1041-1053 (2006).
    • (2006) Cell , vol.125 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 52
    • 0029118089 scopus 로고
    • Mapping of nucleoporins to the centre of the nuclear pore complex by post-embedding immunogold electron microscopy
    • Grote, M., Kubitscheck, U., Reichelt, R. & Peters, R. Mapping of nucleoporins to the centre of the nuclear pore complex by post-embedding immunogold electron microscopy. J. Cell Sci. 108, 2963-2972 (1995).
    • (1995) J. Cell Sci , vol.108 , pp. 2963-2972
    • Grote, M.1    Kubitscheck, U.2    Reichelt, R.3    Peters, R.4
  • 53
    • 0037031842 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein
    • Denning, D. P., Uversky, V., Patel, S. S., Fink, A. L. & Rexach, M. The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein. J. Biol. Chem. 277, 33447-33455 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 33447-33455
    • Denning, D.P.1    Uversky, V.2    Patel, S.S.3    Fink, A.L.4    Rexach, M.5
  • 54
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L. & Rexach, M. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded. Proc. Natl Acad. Sci. USA 100, 2450-2455 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 55
    • 23444435454 scopus 로고    scopus 로고
    • Nucleoporin domain topology is linked to transport status of the nuclear pore complex
    • Paulillo, S. M. et al. Nucleoporin domain topology is linked to transport status of the nuclear pore complex. J. Mol. Biol. 351, 784-798 (2005).
    • (2005) J. Mol. Biol , vol.351 , pp. 784-798
    • Paulillo, S.M.1
  • 56
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • Liu, S. M. & Stewart, M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J. Mol. Biol. 349, 515-525 (2005).
    • (2005) J. Mol. Biol , vol.349 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 57
    • 0041731883 scopus 로고    scopus 로고
    • Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • Bednenko, J., Cingolani, G. & Gerace, L. Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport. J. Cell Biol. 162, 391-401 (2003).
    • (2003) J. Cell Biol , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 58
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin-β for nucleoporins along the pathway of nuclear import
    • Ben-Efraim, I. & Gerace, L. Gradient of increasing affinity of importin-β for nucleoporins along the pathway of nuclear import. J. Cell Biol. 152, 411-418 (2001).
    • (2001) J. Cell Biol , vol.152 , pp. 411-418
    • Ben-Efraim, I.1    Gerace, L.2
  • 59
    • 0142180053 scopus 로고    scopus 로고
    • A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex
    • Pyhtila, B. & Rexach, M. A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex. J. Biol. Chem. 278, 42699-42709 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 60
    • 9444254054 scopus 로고    scopus 로고
    • The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo
    • Zeitler, B. & Weis, K. The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo. J. Cell Biol. 167, 583-590 (2004).
    • (2004) J. Cell Biol , vol.167 , pp. 583-590
    • Zeitler, B.1    Weis, K.2
  • 61
    • 0033578298 scopus 로고    scopus 로고
    • Nachury, M. V. & Weis, K. The direction of transport through the nuclear pore can be inverted. Proc. Natl Acad. Sci. USA 96, 9622-9627 (1999). Direct demonstration that the directionality of nuclear transport can be reversed by reversing the RanGTP gradient. This work shows conclusively that directionality of transport is driven by the Ran nucleotide state and not by a nucleoporin-affinity gradient for importin-β.
    • Nachury, M. V. & Weis, K. The direction of transport through the nuclear pore can be inverted. Proc. Natl Acad. Sci. USA 96, 9622-9627 (1999). Direct demonstration that the directionality of nuclear transport can be reversed by reversing the RanGTP gradient. This work shows conclusively that directionality of transport is driven by the Ran nucleotide state and not by a nucleoporin-affinity gradient for importin-β.
  • 62
    • 33745451968 scopus 로고    scopus 로고
    • Lim, R. Y. et al. Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA 103, 9512-9517 (2006). This paper uses atomic force microscopy to show that FG-repeats can form molecular brushes when bound to gold particles in vitro.
    • Lim, R. Y. et al. Flexible phenylalanine-glycine nucleoporins as entropic barriers to nucleocytoplasmic transport. Proc. Natl Acad. Sci. USA 103, 9512-9517 (2006). This paper uses atomic force microscopy to show that FG-repeats can form molecular brushes when bound to gold particles in vitro.
  • 65
    • 0343510028 scopus 로고
    • Conformations of polymers attached to an interface
    • de Gennes, P. G. Conformations of polymers attached to an interface. Macromolecules 13, 1069-1075 (1980).
    • (1980) Macromolecules , vol.13 , pp. 1069-1075
    • de Gennes, P.G.1
  • 66
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey, S., Richter, R. P. & Görlich, D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314, 815-817 (2006).
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Görlich, D.3
  • 68
    • 0037124045 scopus 로고    scopus 로고
    • Accelerating the rate of disassembly of karyopherin-cargo complexes
    • Gilchrist, D., Mykytka, B. & Rexach, M. Accelerating the rate of disassembly of karyopherin-cargo complexes. J. Biol. Chem. 277, 18161-18172 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 18161-18172
    • Gilchrist, D.1    Mykytka, B.2    Rexach, M.3
  • 69
    • 0016326866 scopus 로고
    • Structure, biochemistry and functions of the nuclear envelope
    • Franke, W. W. Structure, biochemistry and functions of the nuclear envelope. Internat. Rev. Cytol. (Suppl. 4), 71-236 (1974).
    • (1974) Internat. Rev. Cytol , Issue.SUPPL. 4 , pp. 71-236
    • Franke, W.W.1
  • 70
    • 0023852444 scopus 로고
    • Nuclear protein migration involves two steps: Rapid binding at the nuclear envelope followed by slower translocation through nuclear pores
    • 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 52, 655-664 (1988).
    • (1988) Cell , vol.52 , pp. 655-664
    • Richardson, W.D.1    Mills, A.D.2    Dilworth, S.M.3    Laskey, R.A.4    Dingwall, C.5
  • 71
    • 0037043339 scopus 로고    scopus 로고
    • The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import
    • Walther, T. C. et al. The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import. J. Cell Biol. 158, 63-77 (2002).
    • (2002) J. Cell Biol , vol.158 , pp. 63-77
    • Walther, T.C.1
  • 72
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors and nucleoporins
    • Rexach, M. & Blobel, G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors and nucleoporins. Cell 83, 683-692 (1995).
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 73
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2. 3 Å resolution
    • Vetter, I. R., Arndt, A., Kutay, U., Görlich, D. & Wittinghofer, A. Structural view of the Ran-importin β interaction at 2. 3 Å resolution. Cell 97, 635-646 (1999).
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Görlich, D.4    Wittinghofer, A.5
  • 74
    • 20444468112 scopus 로고    scopus 로고
    • Lee, S. J., Matsuura, Y., Liu, S. M. & Stewart, M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 435, 693-696 (2005). The structure of full-length yeast importin-β bound to RanGTP shows how Ran binding alters the pitch of the importin-β helicoid and facilitates release of the importin-α IBB domain.
    • Lee, S. J., Matsuura, Y., Liu, S. M. & Stewart, M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 435, 693-696 (2005). The structure of full-length yeast importin-β bound to RanGTP shows how Ran binding alters the pitch of the importin-β helicoid and facilitates release of the importin-α IBB domain.
  • 75
    • 0033587167 scopus 로고    scopus 로고
    • Cingolani, G., Petosa, C., Weis, K. & Müller C. W. Structure of importin-β bound to the IBB domain of importin-α. Nature 399, 221-229 (1999). Structure of the IBB:importin-β complex showing how the 19 HEAT repeats of importin-β are arranged to form a helicoidal molecule that coils around the α-helical IBB domain. Comparison between different crystal forms indicated that importin-β might be flexible.
    • Cingolani, G., Petosa, C., Weis, K. & Müller C. W. Structure of importin-β bound to the IBB domain of importin-α. Nature 399, 221-229 (1999). Structure of the IBB:importin-β complex showing how the 19 HEAT repeats of importin-β are arranged to form a helicoidal molecule that coils around the α-helical IBB domain. Comparison between different crystal forms indicated that importin-β might be flexible.
  • 76
    • 1842300384 scopus 로고    scopus 로고
    • A novel class of RanGTP binding proteins
    • Görlich, D. et al. A novel class of RanGTP binding proteins. J. Cell Biol. 138, 65-80 (1997).
    • (1997) J. Cell Biol , vol.138 , pp. 65-80
    • Görlich, D.1
  • 77
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp
    • Chook, Y. M. & Blobel, G. Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp. Nature 399, 230-237 (1999).
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 78
    • 0345647103 scopus 로고    scopus 로고
    • RanBP1 is crucial for the release of RanGTP from importin-β-related nuclear transport factors
    • Bischoff, F. R. & Görlich, D. RanBP1 is crucial for the release of RanGTP from importin-β-related nuclear transport factors. FEBS Lett. 419, 249-254 (1997).
    • (1997) FEBS Lett , vol.419 , pp. 249-254
    • Bischoff, F.R.1    Görlich, D.2
  • 79
    • 20844458749 scopus 로고    scopus 로고
    • Cook, A. et al. The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol. Cell 18, 355-367 (2005). Direct demonstration of the dramatic conform ational change in the yeast homologue of CAS, Cse1. In the absence of RanGTP and importin-α, the Cse1 helicoid adopts a closed conformation in which the N terminus becomes bound to a region near the centre of the molecule.
    • Cook, A. et al. The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol. Cell 18, 355-367 (2005). Direct demonstration of the dramatic conform ational change in the yeast homologue of CAS, Cse1. In the absence of RanGTP and importin-α, the Cse1 helicoid adopts a closed conformation in which the N terminus becomes bound to a region near the centre of the molecule.
  • 80
    • 0346457106 scopus 로고    scopus 로고
    • Fukuhara, N., Fernandez, E., Ebert, J., Conti, E. & Svergun, D. Conformational variability of nucleocytoplasmic transport factors. J. Biol. Chem. 279, 2176-2181 (2004). Low-angle X-ray scattering is used to show that several β-karyopherins can adopt different structures in solution, leading to the concept of these molecules having flexible structures.
    • Fukuhara, N., Fernandez, E., Ebert, J., Conti, E. & Svergun, D. Conformational variability of nucleocytoplasmic transport factors. J. Biol. Chem. 279, 2176-2181 (2004). Low-angle X-ray scattering is used to show that several β-karyopherins can adopt different structures in solution, leading to the concept of these molecules having flexible structures.
  • 81
    • 0344827223 scopus 로고    scopus 로고
    • Molecular recognition in nuclear trafficking
    • Stewart, M. Molecular recognition in nuclear trafficking. Science 302, 1513-1514 (2003).
    • (2003) Science , vol.302 , pp. 1513-1514
    • Stewart, M.1
  • 82
    • 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. & Ribbeck, K. Characterization of Ran-driven cargo transport and the RanGTPase system by kinetic measurements and computer simulation. EMBO J. 22, 1088-1100 (2003).
    • (2003) EMBO J , vol.22 , pp. 1088-1100
    • Görlich, D.1    Seewald, M.J.2    Ribbeck, K.3
  • 83
    • 16844374515 scopus 로고    scopus 로고
    • Riddick, G. & Macara, I. G. A systems analysis of importin-α:β mediated nuclear protein import. J. Cell Biol. 168, 1027-1038 (2005). A comprehensive simulation of the classic nuclear protein import cycle that gives several novel and unanticipated functional insights.
    • Riddick, G. & Macara, I. G. A systems analysis of importin-α:β mediated nuclear protein import. J. Cell Biol. 168, 1027-1038 (2005). A comprehensive simulation of the classic nuclear protein import cycle that gives several novel and unanticipated functional insights.
  • 85
    • 12344323514 scopus 로고    scopus 로고
    • Quantitative models of nuclear transport
    • Becskei, A. & Mattaj, I. W. Quantitative models of nuclear transport. Curr. Opin. Cell Biol. 17, 27-34 (2005).
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 27-34
    • Becskei, A.1    Mattaj, I.W.2
  • 86
    • 0029021928 scopus 로고
    • Structural plasticity of the nuclear pore complex
    • Akey, C. W. Structural plasticity of the nuclear pore complex. J. Mol. Biol. 248, 273-293 (1995).
    • (1995) J. Mol. Biol , vol.248 , pp. 273-293
    • Akey, C.W.1
  • 87
    • 0027287349 scopus 로고
    • Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy
    • Akey, C. W. & Radermacher, M. Architecture of the Xenopus nuclear pore complex revealed by three-dimensional cryo-electron microscopy. J. Cell Biol. 122, 1-19 (1993).
    • (1993) J. Cell Biol , vol.122 , pp. 1-19
    • Akey, C.W.1    Radermacher, M.2
  • 88
    • 0037453221 scopus 로고    scopus 로고
    • Stoffler, D. et al. Cryo-electron microscopy provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328, 119-130 (2003). Comprehensive analysis of NPC morphology using cryo-EM and tomography.
    • Stoffler, D. et al. Cryo-electron microscopy provides novel insights into nuclear pore architecture: implications for nucleocytoplasmic transport. J. Mol. Biol. 328, 119-130 (2003). Comprehensive analysis of NPC morphology using cryo-EM and tomography.
  • 89
  • 90
    • 31344455700 scopus 로고    scopus 로고
    • From the trap to the basket: Getting to the bottom of the nuclear pore complex
    • Lim, R. Y., Aebi U. & Stoffler D. From the trap to the basket: getting to the bottom of the nuclear pore complex. Chromosoma 115, 15-26 (2006).
    • (2006) Chromosoma , vol.115 , pp. 15-26
    • Lim, R.Y.1    Aebi, U.2    Stoffler, D.3
  • 91
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • Beck, M. et al. Nuclear pore complex structure and dynamics revealed by cryoelectron tomography. Science 306, 1387-1390 (2004).
    • (2004) Science , vol.306 , pp. 1387-1390
    • Beck, M.1
  • 92
    • 0036968863 scopus 로고    scopus 로고
    • Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex
    • Fahrenkrog, B. et al. Domain-specific antibodies reveal multiple-site topology of Nup153 within the nuclear pore complex. J. Struct. Biol. 140, 254-267 (2002).
    • (2002) J. Struct. Biol , vol.140 , pp. 254-267
    • Fahrenkrog, B.1
  • 93
    • 9444273167 scopus 로고    scopus 로고
    • Components of coated vesicles and nuclear pore complexes share a common molecular architecture
    • Devos, D. et al. Components of coated vesicles and nuclear pore complexes share a common molecular architecture. PloS Biol. 2, e380 (2004).
    • (2004) PloS Biol , vol.2
    • Devos, D.1
  • 94
    • 0033522118 scopus 로고    scopus 로고
    • Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: Implications for nuclear transport
    • Vetter, I. R., Nowak, C., Nishimoto, T., Kuhlmann, J. & Wittinghofer, A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature 398, 39-46 (1999).
    • (1999) Nature , vol.398 , pp. 39-46
    • Vetter, I.R.1    Nowak, C.2    Nishimoto, T.3    Kuhlmann, J.4    Wittinghofer, A.5
  • 95
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase, Ran
    • Stewart, M., Kent, H. M. & McCoy, A. J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase, Ran. J. Mol. Biol. 277, 635-646 (1998).
    • (1998) J. Mol. Biol , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 96
    • 0030593377 scopus 로고    scopus 로고
    • The 1.6 Å resolution crystal structure of nuclear transport factor 2 (NTF2)
    • Bullock, T. L., Clarkson, W. D., Kent, H. M. & Stewart, M. The 1.6 Å resolution crystal structure of nuclear transport factor 2 (NTF2). J. Mol. Biol. 260, 422-431 (1996).
    • (1996) J. Mol. Biol , vol.260 , pp. 422-431
    • Bullock, T.L.1    Clarkson, W.D.2    Kent, H.M.3    Stewart, M.4
  • 97
    • 0035917523 scopus 로고    scopus 로고
    • Structural basis for guanine nucleotide exchange on ran by the regulator of chromosome condensation (RCC1)
    • Renault, L., Kuhlmann, J., Henkel, A. & Wittinghofer, A. Structural basis for guanine nucleotide exchange on ran by the regulator of chromosome condensation (RCC1). Cell 105, 245-255 (2001).
    • (2001) Cell , vol.105 , pp. 245-255
    • Renault, L.1    Kuhlmann, J.2    Henkel, A.3    Wittinghofer, A.4
  • 98
    • 0033152163 scopus 로고    scopus 로고
    • The crystal structure of rna1p: A new fold for a GTPase activating protein
    • Hillig, R. C. et al. The crystal structure of rna1p: a new fold for a GTPase activating protein. Mol. Cell 3, 781-791 (1999).
    • (1999) Mol. Cell , vol.3 , pp. 781-791
    • Hillig, R.C.1
  • 99
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • Seewald, M. J., Korner, C., Wittinghofer, A. & Vetter, I. R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 415, 662-666 (2002).
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Korner, C.2    Wittinghofer, A.3    Vetter, I.R.4


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