메뉴 건너뛰기




Volumn 23, Issue 3, 2016, Pages 239-247

Super-resolution 3D tomography of interactions and competition in the nuclear pore complex

Author keywords

[No Author keywords available]

Indexed keywords

CHLORMETHINE; EXPORTIN 1; FLUORESCENT DYE; IMPORTIN BETA1; KARYOPHERIN; NUCLEOPORIN; PHE GLY; RECEPTOR; TRANSPORT RECEPTOR; UNCLASSIFIED DRUG; NUCLEOCYTOPLASMIC TRANSPORT PROTEIN;

EID: 84959529287     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.3174     Document Type: Article
Times cited : (52)

References (37)
  • 1
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition architecture, and transport mechanism
    • Rout, M.P., et al. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148, 635-651 (2000
    • (2000) J. Cell Biol , vol.148 , pp. 635-651
    • Rout, M.P.1
  • 2
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam, M., & Wente, S.R. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 4, 775-789 (2003
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 3
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried, H., & Kutay, U. Nucleocytoplasmic transport: taking an inventory. Cell. Mol. Life Sci. 60, 1659-1688 (2003
    • (2003) Cell. Mol. Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 4
    • 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. 4, 757-766 (2003
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2
  • 5
    • 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
  • 6
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart, M. Molecular mechanism of the nuclear protein import cycle. Nat. Rev. Mol. Cell Biol. 8, 195-208 (2007
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 7
    • 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.H. 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 (1999
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1218-1225
    • Palmeri, D.1    Malim, M.H.2
  • 8
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • Hoelz, A., Debler, E.W., & Blobel, G. The structure of the nuclear pore complex. Annu. Rev. Biochem. 80, 613-643 (2011
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 9
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout, M.P., & Blobel, G. Isolation of the yeast nuclear pore complex. J. Cell Biol. 123, 771-783 (1993
    • (1993) J. Cell Biol , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 10
    • 73349134975 scopus 로고    scopus 로고
    • Flexible gates: Dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport
    • Terry, L.J., & Wente, S.R. Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport. Eukaryot. Cell 8, 1814-1827 (2009
    • (2009) Eukaryot. Cell , vol.8 , pp. 1814-1827
    • Terry, L.J.1    Wente, S.R.2
  • 11
    • 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
  • 12
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout, M.P., & Aitchison, J.D. The nuclear pore complex as a transport machine. J. Biol. Chem. 276, 16593-16596 (2001
    • (2001) J. Biol. Chem , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 13
    • 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 6, 421-427 (2005
    • (2005) Traffic , vol.6 , pp. 421-427
    • Peters, R.1
  • 14
    • 35548946277 scopus 로고    scopus 로고
    • Nanomechanical basis of selective gating by the nuclear pore complex
    • Lim R.Y., et al. Nanomechanical basis of selective gating by the nuclear pore complex. Science 318, 640-643 (2007
    • (2007) Science , vol.318 , pp. 640-643
    • Lim, R.Y.1
  • 16
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck, K., & Görlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (2001
    • (2001) EMBO J. , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Görlich, D.2
  • 17
    • 34547679515 scopus 로고    scopus 로고
    • A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes
    • Frey, S & Görlich, D. A saturated FG-repeat hydrogel can reproduce the permeability properties of nuclear pore complexes. Cell 130 512-523 2007
    • (2007) Cell , vol.130 , pp. 512-523
    • Frey, S.1    Görlich, D.2
  • 18
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • Mohr, D., Frey, S., Fischer, T., Güttler, T., & Görlich, D. Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 28, 2541-2553 (2009
    • (2009) EMBO J. , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Güttler, T.4    Görlich, D.5
  • 19
    • 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
  • 20
    • 8444247065 scopus 로고    scopus 로고
    • Analysis and prediction of leucine-rich nuclear export signals
    • la Cour T., et al. Analysis and prediction of leucine-rich nuclear export signals. Protein Eng. Des. Sel. 17, 527-536 (2004
    • (2004) Protein Eng. Des. Sel , vol.17 , pp. 527-536
    • La Cour, T.1
  • 21
    • 77954615134 scopus 로고    scopus 로고
    • A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins
    • Yamada J., et al. A bimodal distribution of two distinct categories of intrinsically disordered structures with separate functions in FG nucleoporins. Mol. Cell. Proteomics 9, 2205-2224 (2010
    • (2010) Mol Cell. Proteomics , vol.9 , pp. 2205-2224
    • Yamada, J.1
  • 22
    • 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. USA 107, 7305-7310 (2010
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7305-7310
    • Ma, J.1    Yang, W.2
  • 23
    • 84860822266 scopus 로고    scopus 로고
    • Self-regulated viscous channel in the nuclear pore complex
    • Ma, J., Goryaynov, A., Sarma, A., & Yang, W. Self-regulated viscous channel in the nuclear pore complex. Proc. Natl. Acad. Sci. USA 109, 7326-7331 (2012
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 7326-7331
    • Ma, J.1    Goryaynov, A.2    Sarma, A.3    Yang, W.4
  • 24
    • 84884164838 scopus 로고    scopus 로고
    • High-resolution three-dimensional mapping of mRNA export through the nuclear pore
    • 2414
    • Ma J., et al. High-resolution three-dimensional mapping of mRNA export through the nuclear pore. Nat. Commun. 4, 2414 (2013
    • (2013) Nat. Commun , vol.4
    • Ma, J.1
  • 25
    • 0030960586 scopus 로고    scopus 로고
    • Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex
    • Kutay, U., Izaurralde, E., Bischoff, F.R., Mattaj, I.W., & Görlich, D. Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. EMBO J. 16, 1153-1163 (1997
    • (1997) EMBO J. , vol.16 , pp. 1153-1163
    • Kutay, U.1    Izaurralde, E.2    Bischoff, F.R.3    Mattaj, I.W.4    Görlich, D.5
  • 26
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta
    • Bayliss, R., Littlewood, T., Strawn, L.A., Wente, S.R., & Stewart, M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta. 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
  • 27
    • 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. Natively unfolded nucleoporins gate protein diffusion across the nuclear pore complex. Cell 129, 83-96 (2007
    • (2007) Cell , vol.129 , pp. 83-96
    • Patel, S.S.1    Belmont, B.J.2    Sante, J.M.3    Rexach, M.F.4
  • 28
    • 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 31, 466-477 (2009
    • (2009) BioEssays , vol.31 , pp. 466-477
    • Peters, R.1
  • 29
    • 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. 152, 411-417 (2001
    • (2001) J. Cell Biol , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 30
    • 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. 366, 330-345 (2007
    • (2007) J. Mol. Biol , vol.366 , pp. 330-345
    • Isgro, T.A.1    Schulten, K.2
  • 31
    • 77954161165 scopus 로고    scopus 로고
    • Nucleoporin Nup98: A gatekeeper in the eukaryotic kingdoms
    • Iwamoto, M., Asakawa, H., Hiraoka, Y., & Haraguchi, T. Nucleoporin Nup98: a gatekeeper in the eukaryotic kingdoms. Genes Cells 15, 661-669 (2010
    • (2010) Genes Cells , vol.15 , pp. 661-669
    • Iwamoto, M.1    Asakawa, H.2    Hiraoka, Y.3    Haraguchi, T.4
  • 32
    • 0037088591 scopus 로고    scopus 로고
    • Complex formation between Tap and p15 affects binding to FG-repeat nucleoporins and nucleocytoplasmic shuttling
    • Katahira, J., Straesser, K., Saiwaki, T., Yoneda, Y., & Hurt, E. Complex formation between Tap and p15 affects binding to FG-repeat nucleoporins and nucleocytoplasmic shuttling. J. Biol. Chem. 277, 9242-9246 (2002
    • (2002) J. Biol. Chem , vol.277 , pp. 9242-9246
    • Katahira, J.1    Straesser, K.2    Saiwaki, T.3    Yoneda, Y.4    Hurt, E.5
  • 33
    • 84909987435 scopus 로고    scopus 로고
    • Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations
    • Ghavami, A., Veenhoff, L.M., van der Giessen, E., & Onck, P.R. Probing the disordered domain of the nuclear pore complex through coarse-grained molecular dynamics simulations. Biophys. J. 107, 1393-1402 (2014
    • (2014) Biophys. J. , vol.107 , pp. 1393-1402
    • Ghavami, A.1    Veenhoff, L.M.2    Van Der Giessen, E.3    Onck, P.R.4
  • 34
    • 53749102019 scopus 로고    scopus 로고
    • Autonomy and robustness of translocation through the nuclear pore complex: A single-molecule study
    • Dange, T., Grünwald, D., Grünwald, A., Peters, R., & Kubitscheck, U. Autonomy and robustness of translocation through the nuclear pore complex: a single-molecule study. J. Cell Biol. 183, 77-86 (2008
    • (2008) J. Cell Biol , vol.183 , pp. 77-86
    • Dange, T.1    Grünwald, D.2    Grünwald, A.3    Peters, R.4    Kubitscheck, U.5
  • 35
    • 84923313995 scopus 로고    scopus 로고
    • Promiscuous binding of Karyopherinβ1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics
    • Wagner, R.S., Kapinos, L.E., Marshall, N.J., Stewart, M., & Lim, R.Y. Promiscuous binding of Karyopherinβ1 modulates FG nucleoporin barrier function and expedites NTF2 transport kinetics. Biophys. J. 108, 918-927 (2015
    • (2015) Biophys. J. , vol.108 , pp. 918-927
    • Wagner, R.S.1    Kapinos, L.E.2    Marshall, N.J.3    Stewart, M.4    Lim, R.Y.5
  • 36
    • 84861127061 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: A role for nonspecific competition in karyopherin-nucleoporin interactions
    • Tetenbaum-Novatt, J., Hough, L.E., Mironska, R., McKenney, A.S., & Rout, M.P. Nucleocytoplasmic transport: a role for nonspecific competition in karyopherin-nucleoporin interactions. Mol. Cell. Proteomics 11, 31-46 (2012
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 31-46
    • Tetenbaum-Novatt, J.1    Hough, L.E.2    Mironska, R.3    McKenney, A.S.4    Rout, M.P.5
  • 37
    • 84861363181 scopus 로고    scopus 로고
    • FG repeats facilitate integral protein trafficking to the inner nuclear membrane
    • Kerr, A.R., & Schirmer, E.C. FG repeats facilitate integral protein trafficking to the inner nuclear membrane. Commun. Integr. Biol. 4, 557-559 (2011
    • (2011) Commun. Integr. Biol , vol.4 , pp. 557-559
    • Kerr, A.R.1    Schirmer, E.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.