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Volumn 90, Issue 9, 2011, Pages 751-758

Lighting up the nuclear pore complex

Author keywords

FG repeats; Nuclear pore complex; Nuclear transport; Nuclear transport receptor; Super resolution microscopy; Transport model

Indexed keywords

CELL NUCLEUS RECEPTOR; GLYCINE; PHENYLALANINE;

EID: 79960557348     PISSN: 01719335     EISSN: 16181298     Source Type: Journal    
DOI: 10.1016/j.ejcb.2011.04.004     Document Type: Short Survey
Times cited : (14)

References (71)
  • 2
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • Bayliss R., Littlewood T., Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell 2000, 102:99-108.
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 3
    • 0032589798 scopus 로고    scopus 로고
    • Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP
    • Bayliss R., Ribbeck K., Akin D., Kent H.M., Feldherr C.M., Gorlich D., Stewart M. Interaction between NTF2 and xFxFG-containing nucleoporins is required to mediate nuclear import of RanGDP. J. Mol. Biol. 1999, 293:579-593.
    • (1999) J. Mol. Biol. , vol.293 , pp. 579-593
    • Bayliss, R.1    Ribbeck, K.2    Akin, D.3    Kent, H.M.4    Feldherr, C.M.5    Gorlich, D.6    Stewart, M.7
  • 5
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • Beck M., Lucic V., Forster F., Baumeister W., Medalia O. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature 2007, 449:611-615.
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucic, V.2    Forster, F.3    Baumeister, W.4    Medalia, O.5
  • 6
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import
    • Ben-Efraim I., Gerace L. Gradient of increasing affinity of importin beta for nucleoporins along the pathway of nuclear import. J. Cell Biol. 2001, 152:411-417.
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 8
    • 0026419320 scopus 로고
    • Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
    • Bischoff F.R., Ponstingl H. Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature 1991, 354:80-82.
    • (1991) Nature , vol.354 , pp. 80-82
    • Bischoff, F.R.1    Ponstingl, H.2
  • 11
    • 0030910804 scopus 로고    scopus 로고
    • Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore
    • Chi N.C., Adam S.A. Functional domains in nuclear import factor p97 for binding the nuclear localization sequence receptor and the nuclear pore. Mol. Biol. Cell 1997, 8:945-956.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 945-956
    • Chi, N.C.1    Adam, S.A.2
  • 13
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study
    • Dange T., Grunwald D., Grunwald A., Peters R., Kubitscheck U. Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study. J. Cell Biol. 2008, 183:77-86.
    • (2008) J. Cell Biol. , vol.183 , pp. 77-86
    • Dange, T.1    Grunwald, D.2    Grunwald, A.3    Peters, R.4    Kubitscheck, U.5
  • 14
    • 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. U. S. A. 2003, 100:2450-2455.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 2450-2455
    • Denning, D.P.1    Patel, S.S.2    Uversky, V.3    Fink, A.L.4    Rexach, M.5
  • 17
    • 0029027191 scopus 로고
    • Genetic approaches to nuclear pore structure and function
    • Doye V., Hurt E.C. Genetic approaches to nuclear pore structure and function. Trends Genet. 1995, 11:235-241.
    • (1995) Trends Genet. , vol.11 , pp. 235-241
    • Doye, V.1    Hurt, E.C.2
  • 18
    • 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. Nat. Rev. Mol. Cell Biol. 2003, 4:757-766.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 19
    • 84856314430 scopus 로고    scopus 로고
    • Structural and functional analysis of the nuclear pore complex in Saccharomyces cerevisiae. PhD thesis, University Münster.
    • Farr, J.C., 2009. Structural and functional analysis of the nuclear pore complex in Saccharomyces cerevisiae. PhD thesis, University Münster.
    • (2009)
    • Farr, J.C.1
  • 20
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink A.L. Natively unfolded proteins. Curr. Opin. Struct. Biol. 2005, 15:35-41.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 21
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey S., Gorlich D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 2007, 130:512-523.
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Gorlich, D.2
  • 22
    • 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., Gorlich D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 2006, 314:815-817.
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 23
    • 77957370148 scopus 로고    scopus 로고
    • In vivo imaging of labelled endogenous beta-actin mRNA during nucleocytoplasmic transport
    • Grunwald D., Singer R.H. In vivo imaging of labelled endogenous beta-actin mRNA during nucleocytoplasmic transport. Nature 2010, 467:604-607.
    • (2010) Nature , vol.467 , pp. 604-607
    • Grunwald, D.1    Singer, R.H.2
  • 24
    • 24944539530 scopus 로고    scopus 로고
    • Nonlinear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution
    • Gustafsson M.G. Nonlinear structured-illumination microscopy: wide-field fluorescence imaging with theoretically unlimited resolution. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:13081-13086.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 13081-13086
    • Gustafsson, M.G.1
  • 25
    • 55049135085 scopus 로고    scopus 로고
    • Stimulated emission depletion (STED) nanoscopy of a fluorescent protein-labeled organelle inside a living cell
    • Hein B., Willig K.I., Hell S.W. Stimulated emission depletion (STED) nanoscopy of a fluorescent protein-labeled organelle inside a living cell. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:14271-14276.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14271-14276
    • Hein, B.1    Willig, K.I.2    Hell, S.W.3
  • 26
    • 0026931496 scopus 로고
    • Fundamental improvement of resolution with a 4Pi-confocal fluorescence microscope using 2-photon excitation
    • Hell S.W., Stelzer E.H.K. Fundamental improvement of resolution with a 4Pi-confocal fluorescence microscope using 2-photon excitation. Opt. Commun. 1992, 93:277-282.
    • (1992) Opt. Commun. , vol.93 , pp. 277-282
    • Hell, S.W.1    Stelzer, E.H.K.2
  • 27
    • 70350765083 scopus 로고    scopus 로고
    • Ultrahigh resolution imaging of biomolecules by fluorescence photoactivation localization microscopy
    • Hess S.T., Gould T.J., Gunewardene M., Bewersdorf J., Mason M.D. Ultrahigh resolution imaging of biomolecules by fluorescence photoactivation localization microscopy. Methods Mol. Biol. 2009, 544:483-522.
    • (2009) Methods Mol. Biol. , vol.544 , pp. 483-522
    • Hess, S.T.1    Gould, T.J.2    Gunewardene, M.3    Bewersdorf, J.4    Mason, M.D.5
  • 28
    • 17844364215 scopus 로고    scopus 로고
    • High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions
    • Hoppener C., Siebrasse J.P., Peters R., Kubitscheck U., Naber A. High-resolution near-field optical imaging of single nuclear pore complexes under physiological conditions. Biophys. J. 2005, 88:3681-3688.
    • (2005) Biophys. J. , vol.88 , pp. 3681-3688
    • Hoppener, C.1    Siebrasse, J.P.2    Peters, R.3    Kubitscheck, U.4    Naber, A.5
  • 30
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-beta
    • Isgro T.A., Schulten K. Binding dynamics of isolated nucleoporin repeat regions to importin-beta. Structure 2005, 13:1869-1879.
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 31
    • 33846270287 scopus 로고    scopus 로고
    • Association of nuclear pore FG-repeat domains to NTF2 import and export complexes
    • Isgro T.A., Schulten K. Association of nuclear pore FG-repeat domains to NTF2 import and export complexes. J. Mol. Biol. 2007, 366:330-345.
    • (2007) J. Mol. Biol. , vol.366 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 32
    • 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 K.C., Mattaj I.W., Gorlich D. The asymmetric distribution of the constituents of the Ran system is essential for transport into and out of the nucleus. EMBO J. 1997, 16:6535-6547.
    • (1997) EMBO J. , vol.16 , pp. 6535-6547
    • Izaurralde, E.1    Kutay, U.2    von, K.C.3    Mattaj, I.W.4    Gorlich, D.5
  • 34
    • 68549083700 scopus 로고    scopus 로고
    • Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes
    • Kahms M., Lehrich P., Huve J., Sanetra N., Peters R. Binding site distribution of nuclear transport receptors and transport complexes in single nuclear pore complexes. Traffic 2009, 10:1228-1242.
    • (2009) Traffic , vol.10 , pp. 1228-1242
    • Kahms, M.1    Lehrich, P.2    Huve, J.3    Sanetra, N.4    Peters, R.5
  • 35
    • 0032974756 scopus 로고    scopus 로고
    • Permeability of single nuclear pores
    • Keminer O., Peters R. Permeability of single nuclear pores. Biophys. J. 1999, 77:217-228.
    • (1999) Biophys. J. , vol.77 , pp. 217-228
    • Keminer, O.1    Peters, R.2
  • 36
    • 0141754083 scopus 로고    scopus 로고
    • Optical microwell assay of membrane transport kinetics
    • Kiskin N.I., Siebrasse J.P., Peters R. Optical microwell assay of membrane transport kinetics. Biophys. J. 2003, 85:2311-2322.
    • (2003) Biophys. J. , vol.85 , pp. 2311-2322
    • Kiskin, N.I.1    Siebrasse, J.P.2    Peters, R.3
  • 37
    • 0029930929 scopus 로고    scopus 로고
    • Single nuclear pores visualized by confocal microscopy and image processing
    • Kubitscheck U., Wedekind P., Zeidler O., Grote M., Peters R. Single nuclear pores visualized by confocal microscopy and image processing. Biophys. J. 1996, 70:2067-2077.
    • (1996) Biophys. J. , vol.70 , pp. 2067-2077
    • Kubitscheck, U.1    Wedekind, P.2    Zeidler, O.3    Grote, M.4    Peters, R.5
  • 39
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • Lee S.J., Matsuura Y., Liu S.M., Stewart M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 2005, 435:693-696.
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 42
    • 77957343471 scopus 로고    scopus 로고
    • Selectivity mechanism of the nuclear pore complex characterized by single cargo tracking
    • Lowe A.R., Siegel J.J., Kalab P., Siu M., Weis K., Liphardt J.T. Selectivity mechanism of the nuclear pore complex characterized by single cargo tracking. Nature 2010, 467:600-603.
    • (2010) Nature , vol.467 , pp. 600-603
    • Lowe, A.R.1    Siegel, J.J.2    Kalab, P.3    Siu, M.4    Weis, K.5    Liphardt, J.T.6
  • 43
    • 77952212806 scopus 로고    scopus 로고
    • Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots
    • Ma J., Yang W. Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:7305-7310.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 7305-7310
    • Ma, J.1    Yang, W.2
  • 44
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 1997, 88:97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 45
    • 66449129815 scopus 로고    scopus 로고
    • Experimental characterization of 3D localization techniques for particle-tracking and super-resolution microscopy
    • Mlodzianoski M.J., Juette M.F., Beane G.L., Bewersdorf J. Experimental characterization of 3D localization techniques for particle-tracking and super-resolution microscopy. Opt. Express 2009, 17:8264-8277.
    • (2009) Opt. Express , vol.17 , pp. 8264-8277
    • Mlodzianoski, M.J.1    Juette, M.F.2    Beane, G.L.3    Bewersdorf, J.4
  • 46
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39nm
    • Pante N., Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39nm. Mol. Biol. Cell 2002, 13:425-434.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 47
    • 33751407500 scopus 로고    scopus 로고
    • Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy
    • Paradise A., Levin M.K., Korza G., Carson J.H. Significant proportions of nuclear transport proteins with reduced intracellular mobilities resolved by fluorescence correlation spectroscopy. J. Mol. Biol. 2007, 365:50-65.
    • (2007) J. Mol. Biol. , vol.365 , pp. 50-65
    • Paradise, A.1    Levin, M.K.2    Korza, G.3    Carson, J.H.4
  • 48
    • 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 2005, 6:187-198.
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 49
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality
    • Peters R. Translocation through the nuclear pore complex: selectivity and speed by reduction-of-dimensionality. Traffic 2005, 6:421-427.
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 50
    • 33745508014 scopus 로고    scopus 로고
    • Introduction to nucleocytoplasmic transport: molecules and mechanisms
    • Peters R. Introduction to nucleocytoplasmic transport: molecules and mechanisms. Methods Mol. Biol. 2006, 322:235-258.
    • (2006) Methods Mol. Biol. , vol.322 , pp. 235-258
    • Peters, R.1
  • 51
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters R. Translocation through the nuclear pore: Kaps pave the way. Bioessays 2009, 31:466-477.
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 52
    • 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. 2003, 278:42699-42709.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 53
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut G., Doye V., Ellenberg J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat. Cell Biol. 2004, 6:1114-1121.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 55
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck K., Gorlich D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 2001, 20:1320-1330.
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 56
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • Ribbeck K., Gorlich D. The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J. 2002, 21:2664-2671.
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 61
    • 0036748289 scopus 로고    scopus 로고
    • Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes
    • Siebrasse J.P., Peters R. Rapid translocation of NTF2 through the nuclear pore of isolated nuclei and nuclear envelopes. EMBO Rep. 2002, 3:887-892.
    • (2002) EMBO Rep. , vol.3 , pp. 887-892
    • Siebrasse, J.P.1    Peters, R.2
  • 62
    • 0033151769 scopus 로고    scopus 로고
    • The nuclear pore complex: from molecular architecture to functional dynamics
    • Stoffler D., Fahrenkrog B., Aebi U. The nuclear pore complex: from molecular architecture to functional dynamics. Curr. Opin. Cell Biol. 1999, 11:391-401.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 391-401
    • Stoffler, D.1    Fahrenkrog, B.2    Aebi, U.3
  • 63
  • 64
    • 0036231415 scopus 로고    scopus 로고
    • Precise nanometer localization analysis for individual fluorescent probes
    • Thompson R.E., Larson D.R., Webb W.W. Precise nanometer localization analysis for individual fluorescent probes. Biophys. J. 2002, 82:2775-2783.
    • (2002) Biophys. J. , vol.82 , pp. 2775-2783
    • Thompson, R.E.1    Larson, D.R.2    Webb, W.W.3
  • 66
    • 38749118235 scopus 로고    scopus 로고
    • Highly inclined thin illumination enables clear single-molecule imaging in cells
    • Tokunaga M., Imamoto N., Sakata-Sogawa K. Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat. Methods 2008, 5:159-161.
    • (2008) Nat. Methods , vol.5 , pp. 159-161
    • Tokunaga, M.1    Imamoto, N.2    Sakata-Sogawa, K.3
  • 68
    • 77954043950 scopus 로고    scopus 로고
    • Nuclear transport and the mitotic apparatus: an evolving relationship
    • Wozniak R., Burke B., Doye V. Nuclear transport and the mitotic apparatus: an evolving relationship. Cell. Mol. Life Sci. 2010, 67:2215-2230.
    • (2010) Cell. Mol. Life Sci. , vol.67 , pp. 2215-2230
    • Wozniak, R.1    Burke, B.2    Doye, V.3
  • 70
    • 4444284306 scopus 로고    scopus 로고
    • Imaging of single-molecule translocation through nuclear pore complexes
    • Yang W., Gelles J., Musser S.M. Imaging of single-molecule translocation through nuclear pore complexes. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:12887-12892.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12887-12892
    • Yang, W.1    Gelles, J.2    Musser, S.M.3
  • 71
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization
    • Yildiz A., Forkey J.N., McKinney S.A., Ha T., Goldman Y.E., Selvin P.R. Myosin V walks hand-over-hand: single fluorophore imaging with 1.5-nm localization. Science 2003, 300:2061-2065.
    • (2003) Science , vol.300 , pp. 2061-2065
    • Yildiz, A.1    Forkey, J.N.2    McKinney, S.A.3    Ha, T.4    Goldman, Y.E.5    Selvin, P.R.6


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