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Volumn 147, Issue 3, 2011, Pages 590-602

Molecular architecture of the transport channel of the nuclear pore complex

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPORIN; PHENYLALANYLGLYCINE; PROTEIN NUCLEOPORIN 54; PROTEIN NUCLEOPORIN 58; PROTEIN NUCLEOPORIN 62; UNCLASSIFIED DRUG;

EID: 80155205513     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2011.09.034     Document Type: Article
Times cited : (91)

References (57)
  • 1
    • 0035967522 scopus 로고    scopus 로고
    • Buried polar residues in coiled-coil interfaces
    • DOI 10.1021/bi002829w
    • D.L. Akey, V.N. Malashkevich, and P.S. Kim Buried polar residues in coiled-coil interfaces Biochemistry 40 2001 6352 6360 (Pubitemid 32472724)
    • (2001) Biochemistry , vol.40 , Issue.21 , pp. 6352-6360
    • Akey, D.L.1    Malashkevich, V.N.2    Kim, P.S.3
  • 3
    • 0035158475 scopus 로고    scopus 로고
    • The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport
    • DOI 10.1128/MCB.21.23.7944-7955.2001
    • S.M. Bailer, C. Balduf, and E. Hurt The Nsp1p carboxy-terminal domain is organized into functionally distinct coiled-coil regions required for assembly of nucleoporin subcomplexes and nucleocytoplasmic transport Mol. Cell. Biol. 21 2001 7944 7955 (Pubitemid 33051787)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.23 , pp. 7944-7955
    • Bailer, S.M.1    Balduf, C.2    Hurt, E.3
  • 5
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking
    • R. Bayliss, T. Littlewood, and M. Stewart Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking Cell 102 2000 99 108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 6
    • 8844226004 scopus 로고    scopus 로고
    • Nuclear pore complex structure and dynamics revealed by cryoelectron tomography
    • DOI 10.1126/science.1104808
    • M. Beck, F. Förster, M. Ecke, J.M. Plitzko, F. Melchior, G. Gerisch, W. Baumeister, and O. Medalia Nuclear pore complex structure and dynamics revealed by cryoelectron tomography Science 306 2004 1387 1390 (Pubitemid 39532518)
    • (2004) Science , vol.306 , Issue.5700 , pp. 1387-1390
    • Beck, M.1    Forster, F.2    Ecke, M.3    Plitzko, J.M.4    Melchior, F.5    Gerisch, G.6    Baumeister, W.7    Medalia, O.8
  • 7
    • 80052406907 scopus 로고    scopus 로고
    • Three-dimensional organization of chromatids by nuclear envelope-associated structures
    • G. Blobel Three-dimensional organization of chromatids by nuclear envelope-associated structures Cold Spring Harb. Symp. Quant. Biol. 75 2010 545 554
    • (2010) Cold Spring Harb. Symp. Quant. Biol. , vol.75 , pp. 545-554
    • Blobel, G.1
  • 8
    • 0028900866 scopus 로고
    • Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: Binding of nucleoporin p54 to the rod domain of p62
    • F. Buss, and M. Stewart Macromolecular interactions in the nucleoporin p62 complex of rat nuclear pores: binding of nucleoporin p54 to the rod domain of p62 J. Cell Biol. 128 1995 251 261
    • (1995) J. Cell Biol. , vol.128 , pp. 251-261
    • Buss, F.1    Stewart, M.2
  • 9
    • 0000920828 scopus 로고
    • The packing of α-helices: Simple coiled-coils
    • F.H.C. Crick The packing of α-helices: simple coiled-coils Acta Crystallogr. 6 1953 689 697
    • (1953) Acta Crystallogr. , vol.6 , pp. 689-697
    • Crick, F.H.C.1
  • 12
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • D. Frenkiel-Krispin, B. Maco, U. Aebi, and O. Medalia Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture J. Mol. Biol. 395 2010 578 586
    • (2010) J. Mol. Biol. , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    MacO, B.2    Aebi, U.3    Medalia, O.4
  • 13
    • 0014059126 scopus 로고
    • Octagonal nuclear pores
    • J.G. Gall Octagonal nuclear pores J. Cell Biol. 32 1967 391 399
    • (1967) J. Cell Biol. , vol.32 , pp. 391-399
    • Gall, J.G.1
  • 14
    • 0028893775 scopus 로고
    • Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p
    • P. Grandi, N. Schlaich, H. Tekotte, and E.C. Hurt Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p EMBO J. 14 1995 76 87
    • (1995) EMBO J. , vol.14 , pp. 76-87
    • Grandi, P.1    Schlaich, N.2    Tekotte, H.3    Hurt, E.C.4
  • 15
    • 0030824317 scopus 로고    scopus 로고
    • Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly
    • P. Grandi, T. Dang, N. Pané, A. Shevchenko, M. Mann, D. Forbes, and E. Hurt Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly Mol. Biol. Cell 8 1997 2017 2038 (Pubitemid 27451118)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.10 , pp. 2017-2038
    • Grandi, P.1    Dang, T.2    Pane, N.3    Shevchenko, A.4    Mann, M.5    Forbes, D.6    Hurt, E.7
  • 16
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • T. Guan, S. Müller, G. Klier, N. Panté, J.M. Blevitt, M. Haner, B. Paschal, U. Aebi, and L. Gerace Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex Mol. Biol. Cell 6 1995 1591 1603
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Müller, S.2    Klier, G.3    Panté, N.4    Blevitt, J.M.5    Haner, M.6    Paschal, B.7    Aebi, U.8    Gerace, L.9
  • 17
    • 37349009269 scopus 로고    scopus 로고
    • Architecture of a Coat for the Nuclear Pore Membrane
    • DOI 10.1016/j.cell.2007.11.038, PII S0092867407015425
    • K.C. Hsia, P. Stavropoulos, G. Blobel, and A. Hoelz Architecture of a coat for the nuclear pore membrane Cell 131 2007 1313 1326 (Pubitemid 350297420)
    • (2007) Cell , vol.131 , Issue.7 , pp. 1313-1326
    • Hsia, K.-C.1    Stavropoulos, P.2    Blobel, G.3    Hoelz, A.4
  • 18
    • 0032561538 scopus 로고    scopus 로고
    • CDNA cloning and analysis of the expression of nucleoporin p45
    • DOI 10.1016/S0378-1119(98)00467-3, PII S0378111998004673
    • T. Hu, and L. Gerace cDNA cloning and analysis of the expression of nucleoporin p45 Gene 221 1998 245 253 (Pubitemid 29023752)
    • (1998) Gene , vol.221 , Issue.2 , pp. 245-253
    • Hu, T.1    Gerace, L.2
  • 19
    • 0029767680 scopus 로고    scopus 로고
    • Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins
    • T. Hu, T. Guan, and L. Gerace Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins J. Cell Biol. 134 1996 589 601 (Pubitemid 26269133)
    • (1996) Journal of Cell Biology , vol.134 , Issue.3 , pp. 589-601
    • Hu, T.1    Guan, T.2    Gerace, L.3
  • 20
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-β
    • DOI 10.1016/j.str.2005.09.007, PII S0969212605003643
    • T.A. Isgro, and K. Schulten Binding dynamics of isolated nucleoporin repeat regions to importin-beta Structure 13 2005 1869 1879 (Pubitemid 41772955)
    • (2005) Structure , vol.13 , Issue.12 , pp. 1869-1879
    • Isgro, T.A.1    Schulten, K.2
  • 21
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • DOI 10.1038/nature05075, PII NATURE05075
    • M.C. King, C.P. Lusk, and G. Blobel Karyopherin-mediated import of integral inner nuclear membrane proteins Nature 442 2006 1003 1007 (Pubitemid 44330251)
    • (2006) Nature , vol.442 , Issue.7106 , pp. 1003-1007
    • King, M.C.1    Lusk, C.P.2    Blobel, G.3
  • 22
    • 0031907210 scopus 로고    scopus 로고
    • Active nuclear pore complexes in Chironomus: Visualization of transporter configurations related to mRNP export
    • E. Kiseleva, M.W. Goldberg, T.D. Allen, and C.W. Akey Active nuclear pore complexes in Chironomus: visualization of transporter configurations related to mRNP export J. Cell Sci. 111 1998 223 236 (Pubitemid 28064147)
    • (1998) Journal of Cell Science , vol.111 , Issue.2 , pp. 223-236
    • Kiseleva, E.1    Goldberg, M.W.2    Allen, T.D.3    Akey, C.W.4
  • 23
    • 0027503111 scopus 로고
    • Purification and characterization of a nuclear pore glycoprotein complex containing p62
    • K. Kita, S. Omata, and T. Horigome Purification and characterization of a nuclear pore glycoprotein complex containing p62 J. Biochem. 113 1993 377 382 (Pubitemid 23100182)
    • (1993) Journal of Biochemistry , vol.113 , Issue.3 , pp. 377-382
    • Kita, K.1    Omata, S.2    Horigome, T.3
  • 24
    • 0021719074 scopus 로고
    • Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils
    • S.Y. Lau, A.K. Taneja, and R.S. Hodges Synthesis of a model protein of defined secondary and quaternary structure. Effect of chain length on the stabilization and formation of two-stranded α-helical coiled-coils J. Biol. Chem. 259 1984 13253 13261 (Pubitemid 15223850)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.21 , pp. 13253-13261
    • Lau, S.Y.M.1    Taneja, A.K.2    Hodges, R.S.3
  • 25
    • 35548946277 scopus 로고    scopus 로고
    • Nanomechanical basis of selective gating by the nuclear pore complex
    • DOI 10.1126/science.1145980
    • R.Y. Lim, B. Fahrenkrog, J. Köser, K. Schwarz-Herion, J. Deng, and U. Aebi Nanomechanical basis of selective gating by the nuclear pore complex Science 318 2007 640 643 (Pubitemid 350014836)
    • (2007) Science , vol.318 , Issue.5850 , pp. 640-643
    • Lim, R.Y.H.1    Fahrenkrog, B.2    Koser, J.3    Schwarz-Herion, K.4    Deng, J.5    Aebi, U.6
  • 26
    • 0029008590 scopus 로고
    • A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil
    • K.J. Lumb, and P.S. Kim A buried polar interaction imparts structural uniqueness in a designed heterodimeric coiled coil Biochemistry 34 1995 8642 8648
    • (1995) Biochemistry , vol.34 , pp. 8642-8648
    • Lumb, K.J.1    Kim, P.S.2
  • 28
    • 34047159864 scopus 로고    scopus 로고
    • Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding
    • DOI 10.1126/science.1135730
    • I. Melčák, A. Hoelz, and G. Blobel Structure of Nup58/45 suggests flexible nuclear pore diameter by intermolecular sliding Science 315 2007 1729 1732 (Pubitemid 46515630)
    • (2007) Science , vol.315 , Issue.5819 , pp. 1729-1732
    • Melcak, I.1    Hoelz, A.2    Blobel, G.3
  • 29
    • 0033790322 scopus 로고    scopus 로고
    • Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay
    • B.R. Miller, M. Powers, M. Park, W. Fischer, and D.J. Forbes Identification of a new vertebrate nucleoporin, Nup188, with the use of a novel organelle trap assay Mol. Biol. Cell 11 2000 3381 3396
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3381-3396
    • Miller, B.R.1    Powers, M.2    Park, M.3    Fischer, W.4    Forbes, D.J.5
  • 30
    • 0022639467 scopus 로고
    • Infantile bilateral striatal necrosis: Clinicopathological classification
    • T. Mito, T. Tanaka, L.E. Becker, S. Takashima, and J. Tanaka Infantile bilateral striatal necrosis. Clinicopathological classification Arch. Neurol. 43 1986 677 680 (Pubitemid 16098018)
    • (1986) Archives of Neurology , vol.43 , Issue.7 , pp. 677-680
    • Mito, T.1    Tanaka, T.2    Becker, L.E.3
  • 31
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of ∼39 nm
    • DOI 10.1091/mbc.01-06-0308
    • N. Panté, and M. Kann Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm Mol. Biol. Cell 13 2002 425 434 (Pubitemid 34165072)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.2 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 32
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex
    • A. Radu, M.S. Moore, and G. Blobel The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex Cell 81 1995 215 222
    • (1995) Cell , vol.81 , pp. 215-222
    • Radu, A.1    Moore, M.S.2    Blobel, G.3
  • 33
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • R. Reichelt, A. Holzenburg, E.L. Buhle Jr., M. Jarnik, A. Engel, and U. Aebi Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components J. Cell Biol. 110 1990 883 894
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle, Jr.E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 34
  • 35
    • 38149118681 scopus 로고    scopus 로고
    • Structural basis of the nic96 subcomplex organization in the nuclear pore channel
    • N. Schrader, P. Stelter, D. Flemming, R. Kunze, E. Hurt, and I.R. Vetter Structural basis of the nic96 subcomplex organization in the nuclear pore channel Mol. Cell 29 2008 46 55
    • (2008) Mol. Cell , vol.29 , pp. 46-55
    • Schrader, N.1    Stelter, P.2    Flemming, D.3    Kunze, R.4    Hurt, E.5    Vetter, I.R.6
  • 36
    • 0020472010 scopus 로고
    • A large particle associated with the perimeter of the nuclear pore complex
    • DOI 10.1083/jcb.93.1.63
    • P.N.T. Unwin, and R.A. Milligan A large particle associated with the perimeter of the nuclear pore complex J. Cell Biol. 93 1982 63 75 (Pubitemid 12117041)
    • (1982) Journal of Cell Biology , vol.93 , Issue.1 , pp. 63-75
    • Unwin, P.N.T.1    Milligan, R.A.2
  • 38
    • 27244439232 scopus 로고    scopus 로고
    • Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages
    • Bär, H., Mücke, N., Kostareva, A., Sjöberg, G., Aebi, U., and Herrmann, H. (2005). Severe muscle disease-causing desmin mutations interfere with in vitro filament assembly at distinct stages. Proc. Natl. Acad. Sci. USA 102, 15099-15104.
    • Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15099-15104
    • Bär, H.1    Mücke, N.2    Kostareva, A.3    Sjöberg, G.4    Aebi, U.5    Herrmann, H.6
  • 41
    • 0028103275 scopus 로고    scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4 (CCP4).
    • Collaborative Computational Project, Number 4 (CCP4). (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 42
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • De La Fortelle, E., and Bricogne, G. (1997). Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494.
    • Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 45
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • García De La Torre, J., Huertas, M.L., and Carrasco, B. (2000). Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730.
    • Biophys. J. , vol.78 , pp. 719-730
    • García De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 47
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., Dalke, A., and Schulten, K. (1996). VMD: visual molecular dynamics. J. Mol. Graph. 14, 33-38, 27-28.
    • J. Mol. Graph. , vol.14 , Issue.33-38 , pp. 27-28
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 48
    • 84889120137 scopus 로고    scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119.
    • Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 49
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: A novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh, K., Misawa, K., Kuma, K., and Miyata, T. (2002). MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 30, 3059-3066.
    • Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 50
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007). Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797.
    • J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 0000243829 scopus 로고    scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.S., and Thornton, J.M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 54
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C., Higgins, D.G., and Heringa, J. (2000). T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 302, 205-217.
    • J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 55
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 56
    • 0035853291 scopus 로고    scopus 로고
    • Socket: A program for identifying and analysing coiled-coil motifs within protein structures
    • Walshaw, J., and Woolfson, D.N. (2001). Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J. Mol. Biol. 307, 1427-1450.
    • J. Mol. Biol. , vol.307 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2


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