메뉴 건너뛰기




Volumn 94, Issue 2, 1998, Pages 193-204

Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN;

EID: 0032563246     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81419-1     Document Type: Article
Times cited : (684)

References (50)
  • 1
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope
    • Adam, E.J., and Adam, S.A. (1994). Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555.
    • (1994) J. Cell Biol. , vol.125 , pp. 547-555
    • Adam, E.J.1    Adam, S.A.2
  • 2
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade, M.A., and Bork, P. (1995). HEAT repeats in the Huntington's disease protein. Nature Genet. 11, 115-116.
    • (1995) Nature Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 3
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel, G. (1980). Intracellular protein topogenesis. Proc. Natl. Acad. Sci. USA 77, 1496-1500.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 5
    • 0024260626 scopus 로고
    • Weakly polar interactions in proteins
    • Burley, S.K., and Petsko, G.A. (1988). Weakly polar interactions in proteins. Adv. Protein Chem. 39, 125-189.
    • (1988) Adv. Protein Chem. , vol.39 , pp. 125-189
    • Burley, S.K.1    Petsko, G.A.2
  • 6
    • 0026240806 scopus 로고
    • Ribbons 2.0
    • Carson, M. (1991). Ribbons 2.0. Acta Crystallogr. 24, 958-961.
    • (1991) Acta Crystallogr. , vol.24 , pp. 958-961
    • Carson, M.1
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (1994). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. , vol.D50 , pp. 760-763
  • 8
    • 0026551292 scopus 로고
    • Nuclear translocation of viral Jun but not cellular Jun is cell cycle dependent
    • Chida, K., and Vogt, P.K. (1992). Nuclear translocation of viral Jun but not cellular Jun is cell cycle dependent. Proc. Natl. Acad. Sci. USA 89, 4290-4294.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4290-4294
    • Chida, K.1    Vogt, P.K.2
  • 9
    • 0022814978 scopus 로고
    • Extensive mutagenesis of the nuclear location signal of simian virus 40 large-T antigen
    • Colledge, W.H., Richardson, W.D., Edge, M.D., and Smith, A.E. (1986). Extensive mutagenesis of the nuclear location signal of simian virus 40 large-T antigen. Mol. Cell. Biol. 6, 4136-4139.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4136-4139
    • Colledge, W.H.1    Richardson, W.D.2    Edge, M.D.3    Smith, A.E.4
  • 10
    • 0027994484 scopus 로고
    • RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1
    • Cortes, P., Ye, Z.-S., and Baltimore, D. (1994). RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1. Proc. Natl. Acad. Sci. USA 91, 7633-7637.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7633-7637
    • Cortes, P.1    Ye, Z.-S.2    Baltimore, D.3
  • 11
    • 0023731952 scopus 로고
    • Identification of the human c-myc protein nuclear translocation signal
    • Dang, C.V., and Lee, W.M.F. (1988). Identification of the human c-myc protein nuclear translocation signal. Mol. Cell. Biol. 8, 4048-4054.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4048-4054
    • Dang, C.V.1    Lee, W.M.F.2
  • 12
    • 0025949412 scopus 로고
    • Nuclear targeting sequences: A consensus?
    • Dingwall, C., and Laskey, R.A. (1991). Nuclear targeting sequences: a consensus? Trends Biol. Sci. 16, 178-181.
    • (1991) Trends Biol. Sci. , vol.16 , pp. 178-181
    • Dingwall, C.1    Laskey, R.A.2
  • 13
    • 0024077328 scopus 로고
    • The nucleoplasmin nuclear location sequence is larger and more complex than that of SV40 large T antigen
    • Dingwall, C., Robbins, J., Dilworth, S.M., Roberts, B., and Richardson, W.D. (1988). The nucleoplasmin nuclear location sequence is larger and more complex than that of SV40 large T antigen. J. Cell Biol. 107, 841-849.
    • (1988) J. Cell Biol. , vol.107 , pp. 841-849
    • Dingwall, C.1    Robbins, J.2    Dilworth, S.M.3    Roberts, B.4    Richardson, W.D.5
  • 14
    • 0030875858 scopus 로고    scopus 로고
    • Kinetic characterization of the human retinoblastoma protein bipartite nuclear localization sequence (NLS) in vivo and in vitro: A comparison with the SV40 large Tantigen NLS
    • Efthymiadis, A., Shao, H., Hubner, S., and Jans, D.A. (1997). Kinetic characterization of the human retinoblastoma protein bipartite nuclear localization sequence (NLS) in vivo and in vitro: a comparison with the SV40 large Tantigen NLS. J. Biol. Chem. 272, 22134-22139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22134-22139
    • Efthymiadis, A.1    Shao, H.2    Hubner, S.3    Jans, D.A.4
  • 15
    • 0029025345 scopus 로고
    • Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes
    • Enenkel, C., Blobel, G., and Rexach, M. (1995). Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270, 16499-16502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16499-16502
    • Enenkel, C.1    Blobel, G.2    Rexach, M.3
  • 16
    • 0029984570 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport
    • Görlich, D., and Mattaj, I.W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
    • (1996) Science , vol.271 , pp. 1513-1518
    • Görlich, D.1    Mattaj, I.W.2
  • 17
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Görlich, D., Prehn, S., Laskey, R.A., and Hartmann, E. (1994). Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Görlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 18
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Görlich, D., Kostka, S., Krarft, R., Dingwall, C., Laskey, R.A., Hartmann, E., and Prehn, S. (1995). Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr. Biol. 5, 383-392.
    • (1995) Curr. Biol. , vol.5 , pp. 383-392
    • Görlich, D.1    Kostka, S.2    Krarft, R.3    Dingwall, C.4    Laskey, R.A.5    Hartmann, E.6    Prehn, S.7
  • 19
    • 0029921174 scopus 로고    scopus 로고
    • A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus
    • Görlich, D., Henklein, P., Laskey, R.A., and Hartmann, E. (1996). A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus. EMBO J. 15, 1810-1817.
    • (1996) EMBO J. , vol.15 , pp. 1810-1817
    • Görlich, D.1    Henklein, P.2    Laskey, R.A.3    Hartmann, E.4
  • 20
    • 0028204490 scopus 로고
    • Do salt bridges stabilize proteins?: A continuum electrostatic analysis
    • Hendsch, Z.S., and Tidor, B. (1994). Do salt bridges stabilize proteins?: a continuum electrostatic analysis. Protein Sci. 3, 211-226.
    • (1994) Protein Sci. , vol.3 , pp. 211-226
    • Hendsch, Z.S.1    Tidor, B.2
  • 21
    • 0030800831 scopus 로고    scopus 로고
    • Three-dimensional structure of the armadillo repeat region of β-catenin
    • Huber, A.H., Nelson, W.J., and Weis, W.I. (1997). Three-dimensional structure of the armadillo repeat region of β-catenin. Cell 90, 871-882.
    • (1997) Cell , vol.90 , pp. 871-882
    • Huber, A.H.1    Nelson, W.J.2    Weis, W.I.3
  • 22
    • 0028970112 scopus 로고
    • A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding
    • Imamoto, N., Tachibana, Y., Matsubae, M., and Yoneda, Y. (1995). A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding. J. Biol. Chem. 270, 8559-8565.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8559-8565
    • Imamoto, N.1    Tachibana, Y.2    Matsubae, M.3    Yoneda, Y.4
  • 23
    • 84889120137 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. A47, 110-119.
    • (1991) Acta Crystallogr. , vol.A47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon, D., Roberts, B.L., Richardson, W.D., and Smith, A.E. (1984). A short amino acid sequence able to specify nuclear location. Cell 39, 499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 25
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe, B., and Deisenhofer, J. (1994). The leucine-rich repeat: a versatile binding motif. Trends Biochem. Sci. 19, 415-421.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 26
    • 0021670868 scopus 로고
    • Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen
    • Lanford, R.E., and Butel, J.S. (1984). Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell 37, 801-813.
    • (1984) Cell , vol.37 , pp. 801-813
    • Lanford, R.E.1    Butel, J.S.2
  • 28
    • 0030221192 scopus 로고    scopus 로고
    • Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids
    • Makkerh, J.P.S., Dingwall, C., and Laskey, R.A. (1996). Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol. 6, 1025-1027.
    • (1996) Curr. Biol. , vol.6 , pp. 1025-1027
    • Makkerh, J.P.S.1    Dingwall, C.2    Laskey, R.A.3
  • 29
    • 0031470630 scopus 로고    scopus 로고
    • Evolutionary specialization of the nuclear targeting apparatus
    • Malik, H.S., Eickbush, T.H., and Goldfarb, D.S. (1997). Evolutionary specialization of the nuclear targeting apparatus. Proc. Natl. Acad. Sci. USA 94, 13738-13742.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13738-13742
    • Malik, H.S.1    Eickbush, T.H.2    Goldfarb, D.S.3
  • 30
  • 31
    • 0028962511 scopus 로고
    • Previously identified protein of uncertain function is karyopherin α and together with karyopherin β docks import substrate at nuclear pore complexes
    • Moroianu, J., Blobel, G., and Radu, A. (1995a). Previously identified protein of uncertain function is karyopherin α and together with karyopherin β docks import substrate at nuclear pore complexes. Proc. Natl. Acad. Sci. USA 92, 2008-2011.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 32
    • 0028983494 scopus 로고
    • Mammalian karyopherin α1β and α2β heterodimers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins
    • Moroianu, J., Hijikata, M., Blobel, G., and Radu, A. (1995b). Mammalian karyopherin α1β and α2β heterodimers: α1 or α2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins. Proc. Natl. Acad. Sci. USA 92, 6532-6536.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6532-6536
    • Moroianu, J.1    Hijikata, M.2    Blobel, G.3    Radu, A.4
  • 33
    • 0029987590 scopus 로고    scopus 로고
    • The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence
    • Moroianu, J., Blobel, G., and Radu, A. (1996). The binding site of karyopherin alpha for karyopherin beta overlaps with a nuclear localization sequence. Proc. Natl. Acad. Sci. USA 93, 6572-6576.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6572-6576
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 35
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11, 281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 36
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Signals, mechanisms and regulation
    • Nigg, E.A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386, 779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 37
    • 0032489013 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The last 200 nanometers
    • Ohno, M., Fornerod, M., and Mattaj, I.W. (1998). Nucleocytoplasmic transport: the last 200 nanometers. Cell 92, 327-336.
    • (1998) Cell , vol.92 , pp. 327-336
    • Ohno, M.1    Fornerod, M.2    Mattaj, I.W.3
  • 38
    • 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.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 39
    • 0028266975 scopus 로고
    • A repeating amino acid motif shared by proteins with diverse cellular roles
    • Peifer, M., Berg, S., and Reynolds, A.B. (1994). A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 76, 789-791.
    • (1994) Cell , vol.76 , pp. 789-791
    • Peifer, M.1    Berg, S.2    Reynolds, A.B.3
  • 41
    • 0029021567 scopus 로고
    • The peptide repeat domain of nucleoporin 98 functions as a docking site in transport across the nuclear pore complex
    • Radu, A., Moore, M.S., and Blobel, G. (1995). The peptide repeat domain of nucleoporin 98 functions as a docking site in transport across the nuclear pore complex. Cell 81, 215-222.
    • (1995) Cell , vol.81 , pp. 215-222
    • Radu, A.1    Moore, M.S.2    Blobel, G.3
  • 42
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach, M., and Blobel, G. (1995). Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83, 683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 43
    • 0026078249 scopus 로고
    • Two interdependent basic domains in nucleoplasmin targeting sequence: Identification of a class of bipartite nuclear targeting sequence
    • Robbins, J., Dilworth, S.M., Laskey, R.A., and Dingwall, C. (1991). Two interdependent basic domains in nucleoplasmin targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell 64, 615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 44
    • 0030670639 scopus 로고    scopus 로고
    • Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1
    • Sekimoto, T., Imamoto, N., Nakajima, K., Hirano, T., and Yoneda, Y. (1997). Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 16, 7067-7077.
    • (1997) EMBO J. , vol.16 , pp. 7067-7077
    • Sekimoto, T.1    Imamoto, N.2    Nakajima, K.3    Hirano, T.4    Yoneda, Y.5
  • 45
    • 0028348369 scopus 로고
    • Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide
    • Stern, L.J., Brown, J.H., Jardetzky, T.S., Gorga, J.C., Urban, R.G., Strominger, J.L., and Wiley, D.C. (1994). Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 360, 215-221.
    • (1994) Nature , vol.360 , pp. 215-221
    • Stern, L.J.1    Brown, J.H.2    Jardetzky, T.S.3    Gorga, J.C.4    Urban, R.G.5    Strominger, J.L.6    Wiley, D.C.7
  • 46
    • 0028988731 scopus 로고
    • Identification of hSRP1α as a functional receptor for nuclear localization sequences
    • Weis, K., Mattaj, I.W., and Lamond, A.I. (1995). Identification of hSRP1α as a functional receptor for nuclear localization sequences. Science 268, 1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 47
    • 0030454052 scopus 로고    scopus 로고
    • The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import
    • Weis, K., Ryder, U., and Lamond, A.I. (1996). The conserved amino-terminal domain of hSRP1 alpha is essential for nuclear protein import. EMBO J. 15, 7120-7128.
    • (1996) EMBO J. , vol.15 , pp. 7120-7128
    • Weis, K.1    Ryder, U.2    Lamond, A.I.3
  • 49
    • 0031604505 scopus 로고    scopus 로고
    • Three dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang, Q., Rout, M.P., and Akey, C.W. (1998). Three dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1, 223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 50
    • 0026490039 scopus 로고
    • Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations in Saccharomyces cerevisiae
    • Yano, R.M., Oakes, M., Yamaghishi, M.M., Dodd, J.A., and Nomura, M. (1992). Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 5640-5651.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5640-5651
    • Yano, R.M.1    Oakes, M.2    Yamaghishi, M.M.3    Dodd, J.A.4    Nomura, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.