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Volumn 107, Issue 16, 2010, Pages 7305-7310

Three-dimensional distribution of transient interactions in the nuclear pore complex obtained from single-molecule snapshots

Author keywords

Deconvolution; Imaging and tracking; Nucleocytoplasmic transport; Single molecule fluorescence

Indexed keywords

CHAPERONE; GLYCINE; KARYOPHERIN BETA; NUCLEOPORIN; PHENYLALANINE;

EID: 77952212806     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0908269107     Document Type: Article
Times cited : (104)

References (41)
  • 1
    • 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
  • 2
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried H, Kutay U (2003) Nucleocytoplasmic transport: Taking an inventory. Cell Mol Life Sci 60:1659-1688.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 3
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: Nucleocytoplasmic transport and beyond
    • Fahrenkrog B, Aebi U (2003) The nuclear pore complex: Nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 4:757-766. (Pubitemid 37229372)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.10 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 5
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout M-P, Blobel G (1993) Isolation of the yeast nuclear pore complex. J Cell Biol 123:771-783.
    • (1993) J Cell Biol , vol.123 , pp. 771-783
    • Rout, M.-P.1    Blobel, G.2
  • 7
    • 0037418190 scopus 로고    scopus 로고
    • Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded
    • Denning D-P, et al. (2003) Disorder in the nuclear pore complex: The FG repeat regions of nucleoporins are natively unfolded. Proc Natl Acad Sci USA 100:2450-2455.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 2450-2455
    • Denning, D.-P.1
  • 8
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • DOI 10.1038/nrm2114, PII NRM2114
    • Stewart M (2007) Molecular mechanism of the nuclear import cycle. Nat Rev Mol Cell Biol 8:195-208. (Pubitemid 46310545)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.3 , pp. 195-208
    • Stewart, M.1
  • 9
    • 0032961356 scopus 로고    scopus 로고
    • Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha
    • Palmeri D, Malim M (1999) Importin beta can mediate the nuclear import of an Arginine-Rich nuclear localization signal in the absence of Importin alpha. Mol Cell Biol 19:1218-1225. (Pubitemid 29046864)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1218-1225
    • Palmeri, D.1    Malim, M.H.2
  • 10
    • 68549085409 scopus 로고    scopus 로고
    • Importins and beyond: Non-conventional nuclear transport mechanisms
    • Wagstaff K, Jans D (2009) Importins and beyond: Non-conventional nuclear transport mechanisms. Traffic 10:1188-1198.
    • (2009) Traffic , vol.10 , pp. 1188-1198
    • Wagstaff, K.1    Jans, D.2
  • 11
    • 28844445505 scopus 로고    scopus 로고
    • Binding dynamics of isolated nucleoporin repeat regions to importin-β
    • Isgro T-A, Schulten K (2005) Binding dynamics of isolated nucleoporin repeat regions to importin-β. Structure 13:1869-1879.
    • (2005) Structure , vol.13 , pp. 1869-1879
    • Isgro, T.-A.1    Schulten, K.2
  • 12
    • 0041731883 scopus 로고    scopus 로고
    • Importin beta contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • DOI 10.1083/jcb.200303085
    • Bednenko J, Cingolani G, Gerace L (2003) Importin ß contains a COOH-terminal nucleoporin binding region important for nuclear transport. J Cell Biol 162:391-401. (Pubitemid 36988549)
    • (2003) Journal of Cell Biology , vol.162 , Issue.3 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 14
    • 33748449331 scopus 로고    scopus 로고
    • Visualizing single molecules interacting with nuclear pore complexes by narrow-field epifluorescence microscopy
    • DOI 10.1016/j.ymeth.2006.06.002, PII S1046202306000934
    • Yang W, Musser S-M (2006) Visualizing single molecules interacting with nuclear pore complexes by narrow-field epifluorescence microscopy. Methods 39:316-328. (Pubitemid 44354201)
    • (2006) Methods , vol.39 , Issue.4 , pp. 316-328
    • Yang, W.1    Musser, S.M.2
  • 15
    • 33749023069 scopus 로고    scopus 로고
    • Nuclear import time and transport efficiency depend on importin beta concentration
    • DOI 10.1083/jcb.200605053
    • Yang W, Musser S-M (2006) Nuclear import time and transport efficiency depend on importin beta concentration. J Cell Biol 174:951-961. (Pubitemid 44455184)
    • (2006) Journal of Cell Biology , vol.174 , Issue.7 , pp. 951-961
    • Yang, W.1    Musser, S.M.2
  • 17
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: A single-molecule study
    • Dange T, et al. (2008) Autonomy and robustness of translocation through the nuclear pore complex: A single-molecule study. J Cell Biol 183:77-86.
    • (2008) J Cell Biol , vol.183 , pp. 77-86
    • Dange, T.1
  • 18
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg E, Wozniak R-W, Blobel G (1993) An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J Cell Biol 122(3):513-521. (Pubitemid 23226669)
    • (1993) Journal of Cell Biology , vol.122 , Issue.3 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 19
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • DOI 10.1038/ncb1184
    • Rabut G, Doye V, Ellenberg J (2004) Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nat Cell Biol 6:1114-1121. (Pubitemid 39468013)
    • (2004) Nature Cell Biology , vol.6 , Issue.11 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 20
    • 34948818777 scopus 로고    scopus 로고
    • Two distinct human POM121 genes: Requirement for the formation of nuclear pore complexes
    • DOI 10.1016/j.febslet.2007.09.021, PII S0014579307010034
    • Funakoshi T, et al. (2007) Two distinct human POM121 genes: Requirement for the formation of nuclear pore complexes. FEBS Lett 581:4910-4916. (Pubitemid 47531761)
    • (2007) FEBS Letters , vol.581 , Issue.25 , pp. 4910-4916
    • Funakoshi, T.1    Maeshima, K.2    Yahata, K.3    Sugano, S.4    Imamoto, F.5    Imamoto, N.6
  • 22
    • 0021717131 scopus 로고
    • Movement of a karyophilic protein through the nuclear pores of oocytes
    • DOI 10.1083/jcb.99.6.2216
    • Feldherr C-M, Kallenbach E, Schultz N (1984) Movement of a karyophilic protein through the nuclear pores of oocytes. J Cell Biol 99:2216-2222. (Pubitemid 15181886)
    • (1984) Journal of Cell Biology , vol.99 , Issue.6 , pp. 2216-2222
    • Feldherr, C.M.1    Kallenbach, E.2    Schultz, N.3
  • 24
    • 0037832404 scopus 로고    scopus 로고
    • Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization
    • DOI 10.1126/science.1084398
    • Yildiz A, et al. (2003) Myosin V walks hand-over-hand: Single fluorophore imaging with 1.5-nm localization. Science 300:2061-2065. (Pubitemid 36760126)
    • (2003) Science , vol.300 , Issue.5628 , 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
  • 27
    • 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 (2000) Structural basis for the interaction between FxFG nucleoporin repeats and importin-beta in nuclear trafficking. Cell 102:99-108.
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 28
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti E, Müller C-W, Stewart M (2006) Karyopherin flexibility in nucleocytoplasmic transport. Curr Opin Struct Biol 16(2):237-244.
    • (2006) Curr Opin Struct Biol , vol.16 , Issue.2 , pp. 237-244
    • Conti, E.1    Müller, C.-W.2    Stewart, M.3
  • 29
    • 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 (2005) 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) J Mol Biol , vol.349 , pp. 515-525
    • Liu, S.-M.1    Stewart, M.2
  • 31
    • 55849144420 scopus 로고    scopus 로고
    • Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP
    • Otsuka S, et al. (2008) Individual binding pockets of importin-beta for FG-nucleoporins have different binding properties and different sensitivities to RanGTP. Proc Natl Acad Sci USA 105:16101-16106.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 16101-16106
    • Otsuka, S.1
  • 32
    • 33947727395 scopus 로고    scopus 로고
    • Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex
    • Patel S-S, Belmont B-J, Sante J-M, Rexach M-F (2007) Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129:83-96.
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.-S.1    Belmont, B.-J.2    Sante, J.-M.3    Rexach, M.-F.4
  • 33
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout M-P (2000) The yeast nuclear pore complex: Composition, architecture, and transport mechanism. J Cell Biol 148:635-651.
    • (2000) J Cell Biol , vol.148 , pp. 635-651
    • Rout, M.-P.1
  • 34
    • 17444427382 scopus 로고    scopus 로고
    • Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality
    • DOI 10.1111/j.1600-0854.2005.00287.x
    • Peters R (2005) Translocation through the nuclear pore complex: Selectivity and speed by reduction-of-dimensionality. Traffic 6:421-427. (Pubitemid 40542768)
    • (2005) Traffic , vol.6 , Issue.5 , pp. 421-427
    • Peters, R.1
  • 35
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • DOI 10.1093/emboj/20.6.1320
    • Ribbeck K, Gorlich D (2001) Kinetic analysis of translocation through nuclear pore complexes. EMBO J 20:1320-1330. (Pubitemid 32233972)
    • (2001) EMBO Journal , vol.20 , Issue.6 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 36
    • 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
  • 38
    • 35548946277 scopus 로고    scopus 로고
    • Nanomechanical basis of selective gating by the nuclear pore complex
    • Lim R-Y, et al. (2007) Nanomechanical basis of selective gating by the nuclear pore complex. Science 318:640-643.
    • (2007) Science , vol.318 , pp. 640-643
    • Lim, R.-Y.1
  • 39
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • DOI 10.1038/nature03578
    • Lee S-J, Matsuura Y, Liu S-M, Stewart M (2005) Structural basis for nuclear import complex dissociation by RanGTP. Nature 435:693-696. (Pubitemid 40825515)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 40
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • DOI 10.1126/science.1068798
    • Kalab P, Weis K, Heald R (2002) Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts. Science 295(5564):2452-2456. (Pubitemid 34270259)
    • (2002) Science , vol.295 , Issue.5564 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 41
    • 34547679515 scopus 로고    scopus 로고
    • A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes
    • DOI 10.1016/j.cell.2007.06.024, PII S009286740700791X
    • Frey S, Gorlich D (2007) A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130:512-523. (Pubitemid 47208521)
    • (2007) Cell , vol.130 , Issue.3 , pp. 512-523
    • Frey, S.1    Gorlich, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.