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Volumn 8, Issue 3, 2000, Pages 329-338

Crystallographic analysis of the specific yet versatile recognition of distinct nuclear localization signals by karyopherin α

Author keywords

Bipartite; Crystal structure; Karyopherin ; Nuclear import; Nuclear localization signal

Indexed keywords

KARYOPHERIN; NUCLEOPLASMIN;

EID: 0034653375     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00107-6     Document Type: Article
Times cited : (264)

References (47)
  • 1
    • 0033598989 scopus 로고    scopus 로고
    • Transport of proteins and RNAs in and out of the nucleus
    • Nakielny S., Dreyfuss G. Transport of proteins and RNAs in and out of the nucleus. Cell. 99:1999;677-690.
    • (1999) Cell , vol.99 , pp. 677-690
    • Nakielny, S.1    Dreyfuss, G.2
  • 2
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj I.W., Englmeier L. Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67:1998;265-306.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 4
    • 0028217405 scopus 로고
    • Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope
    • Adam E.J., Adam S.A. Identification of cytosolic factors required for nuclear-location sequence-mediated binding to the nuclear envelope. J. Cell. Biol. 125:1994;547-555.
    • (1994) J. Cell. Biol. , vol.125 , pp. 547-555
    • Adam, E.J.1    Adam, S.A.2
  • 5
    • 0028970112 scopus 로고
    • A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding
    • Imamoto N., Tachibana Y., Matsubae M., Yoneda Y. A karyophilic protein forms a stable complex with cytoplasmic components prior to nuclear pore binding. J. Biol. Chem. 270:1995;8559-8565.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8559-8565
    • Imamoto, N.1    Tachibana, Y.2    Matsubae, M.3    Yoneda, Y.4
  • 6
    • 0029025345 scopus 로고
    • Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes
    • Enenkel C., Blobel G., Rexach M. Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270:1995;16499-16502.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16499-16502
    • Enenkel, C.1    Blobel, G.2    Rexach, M.3
  • 7
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Görlich D., Prehn S.et al. Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr. Biol. 5:1995;383-392.
    • (1995) Curr. Biol. , vol.5 , pp. 383-392
    • Görlich, D.1    Prehn, S.2
  • 8
    • 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., Radu A. 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. 92:1995;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
  • 9
    • 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., Hartmann E. Isolation of a protein that is essential for the first step of nuclear protein import. Cell. 79:1994;767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Görlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 10
    • 0028988731 scopus 로고
    • Identification of hSRP1α as a functional receptor for nuclear localization sequences
    • Weis K., Mattaj I.W., Lamond A.I. Identification of hSRP1α as a functional receptor for nuclear localization sequences. Science. 268:1995;1049-1053.
    • (1995) Science , vol.268 , pp. 1049-1053
    • Weis, K.1    Mattaj, I.W.2    Lamond, A.I.3
  • 11
    • 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., Radu A. 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. 92:1995;2008-2011.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 12
    • 0028834428 scopus 로고
    • Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • Rexach M., Blobel G. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 83:1995;683-692.
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 13
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Görlich D., Pante N., Kutay U., Aebi U., Bischoff F.R. Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J. 15:1996;5584-5594.
    • (1996) EMBO J. , vol.15 , pp. 5584-5594
    • Görlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 14
    • 0342276108 scopus 로고    scopus 로고
    • Export of importin α from the nucleus is mediated by a specific nuclear transport factor
    • Kutay U., Bischoff F.R., Kostka S., Kraft R., Görlich D. Export of importin α from the nucleus is mediated by a specific nuclear transport factor. Cell. 90:1997;1061-1071.
    • (1997) Cell , vol.90 , pp. 1061-1071
    • Kutay, U.1    Bischoff, F.R.2    Kostka, S.3    Kraft, R.4    Görlich, D.5
  • 15
    • 0020188311 scopus 로고
    • A polypeptide domain that specifies migration into the nucleus
    • Dingwall C., Sharnick S.V., Laskey R.A. A polypeptide domain that specifies migration into the nucleus. Cell. 30:1982;449-458.
    • (1982) Cell , vol.30 , pp. 449-458
    • Dingwall, C.1    Sharnick, S.V.2    Laskey, R.A.3
  • 16
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus?
    • Dingwall C., Laskey R.A. Nuclear targeting sequences - a consensus? Trends. Biol. Sci. 16:1991;178-181.
    • (1991) Trends. Biol. Sci. , vol.16 , pp. 178-181
    • Dingwall, C.1    Laskey, R.A.2
  • 17
    • 0021716406 scopus 로고
    • A short amino acid sequence able to specify nuclear location
    • Kalderon D., Roberts B.L., Richardson W.D., Smith A.E. A short amino acid sequence able to specify nuclear location. Cell. 39:1984;499-509.
    • (1984) Cell , vol.39 , pp. 499-509
    • Kalderon, D.1    Roberts, B.L.2    Richardson, W.D.3    Smith, A.E.4
  • 18
    • 0021670868 scopus 로고
    • Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen
    • Lanford R.E., Butel J.S. Construction and characterization of an SV40 mutant defective in nuclear transport of T antigen. Cell. 37:1984;801-813.
    • (1984) Cell , vol.37 , pp. 801-813
    • Lanford, R.E.1    Butel, J.S.2
  • 19
    • 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., Smith A.E. Extensive mutagenesis of the nuclear location signal of simian virus 40 large-T antigen. Mol. Cell Biol. 6:1986;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
  • 20
    • 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., Richardson W.D. The nucleoplasmin nuclear location sequence is larger and more complex than that of SV40 large T antigen. J. Cell Biol. 107:1988;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
  • 21
    • 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., Dingwall C. Two interdependent basic domains in nucleoplasmin targeting sequence: identification of a class of bipartite nuclear targeting sequence. Cell. 64:1991;615-623.
    • (1991) Cell , vol.64 , pp. 615-623
    • Robbins, J.1    Dilworth, S.M.2    Laskey, R.A.3    Dingwall, C.4
  • 22
    • 0023731952 scopus 로고
    • Identification of the human c-myc protein nuclear translocation signal
    • Dang C.V., Lee W.M.F. Identification of the human c-myc protein nuclear translocation signal. Mol. Cell Biol. 8:1988;4048-4054.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 4048-4054
    • Dang, C.V.1    Lee, W.M.F.2
  • 23
    • 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., Laskey R.A. Comparative mutagenesis of nuclear localization signals reveals the importance of neutral and acidic amino acids. Curr. Biol. 6:1996;025-1027.
    • (1996) Curr. Biol. , vol.6 , pp. 025-1027
    • Makkerh, J.P.S.1    Dingwall, C.2    Laskey, R.A.3
  • 24
    • 0032563246 scopus 로고    scopus 로고
    • Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α
    • Conti E., Uy M., Leighton L., Blobel G., Kuriyan J. Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α Cell. 94:1998;193-204.
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 25
    • 0029921174 scopus 로고    scopus 로고
    • A 41 amino acid motif in importin-α confers binding to importin-β And hence transit into the nucleus
    • Görlich D., Henklein P., Laskey R.A., Hartmann E. A 41 amino acid motif in importin-α confers binding to importin-β and hence transit into the nucleus. EMBO J. 15:1996;1810-1817.
    • (1996) EMBO J. , vol.15 , pp. 1810-1817
    • Görlich, D.1    Henklein, P.2    Laskey, R.A.3    Hartmann, E.4
  • 26
    • 0032950628 scopus 로고    scopus 로고
    • Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α
    • Kobe B. Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α Nat. Struct. Biol. 6:1999;388-397.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 388-397
    • Kobe, B.1
  • 27
    • 0032585625 scopus 로고    scopus 로고
    • Nuclear import: A tale of two sites
    • Dingwall C., Laskey R.A. Nuclear import: a tale of two sites. Curr. Biol. 8:1998;R922-R924.
    • (1998) Curr. Biol. , vol.8
    • Dingwall, C.1    Laskey, R.A.2
  • 28
    • 0026662651 scopus 로고
    • The human poly (ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity
    • Schreiber V., Molinete M., Boeuf H., de Murcia G., Menissier-de Murcia J. The human poly (ADP-ribose) polymerase nuclear localization signal is a bipartite element functionally separate from DNA binding and catalytic activity. EMBO J. 11:1992;3263-3269.
    • (1992) EMBO J. , vol.11 , pp. 3263-3269
    • Schreiber, V.1    Molinete, M.2    Boeuf, H.3    De Murcia, G.4    Menissier-De Murcia, J.5
  • 29
    • 0025764782 scopus 로고
    • The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5
    • Moll T., Tebb G., Surana U., Robitsch H., Nasmyth K. The role of phosphorylation and the CDC28 protein kinase in cell cycle-regulated nuclear import of the S. cerevisiae transcription factor SWI5. Cell. 66:1991;743-758.
    • (1991) Cell , vol.66 , pp. 743-758
    • Moll, T.1    Tebb, G.2    Surana, U.3    Robitsch, H.4    Nasmyth, K.5
  • 30
    • 0024411243 scopus 로고
    • Sequence requirements for synthetic peptide-mediated trasnslocation to the nucleus
    • Chelsky D., Ralph R., Jonak G. Sequence requirements for synthetic peptide-mediated trasnslocation to the nucleus. Mol. Cell Biol. 9:1989;2487-2492.
    • (1989) Mol. Cell Biol. , vol.9 , pp. 2487-2492
    • Chelsky, D.1    Ralph, R.2    Jonak, G.3
  • 31
    • 0039612732 scopus 로고    scopus 로고
    • Evidence for distinct substrate specificities of importin a family members in nuclear protein import
    • Köhler M., Hartmann E.et al. Evidence for distinct substrate specificities of importin a family members in nuclear protein import. Mol. Cell Biol. 19:1999;7782-7791.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 7782-7791
    • Köhler, M.1    Hartmann, E.2
  • 32
    • 0032547742 scopus 로고    scopus 로고
    • Determination of the functional domain organization of the importin α nuclear import factor
    • Herold A., Truant R., Wiegand H., Cullen B.R. Determination of the functional domain organization of the importin α nuclear import factor. J. Cell Biol. 143:1998;309-318.
    • (1998) J. Cell Biol. , vol.143 , pp. 309-318
    • Herold, A.1    Truant, R.2    Wiegand, H.3    Cullen, B.R.4
  • 33
    • 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., Yoneda Y. Extracellular signal-dependent nuclear import of Stat1 is mediated by nuclear pore-targeting complex formation with NPI-1, but not Rch1. EMBO J. 16:1997;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
  • 34
    • 0031058042 scopus 로고    scopus 로고
    • The NPI-1/NPI-3 (karyopherin α) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal
    • Wang P., Palese P., O'Neill R.E. The NPI-1/NPI-3 (karyopherin α) binding site on the influenza a virus nucleoprotein NP is a nonconventional nuclear localization signal. J. Virol. 71:1997;1850-1856.
    • (1997) J. Virol. , vol.71 , pp. 1850-1856
    • Wang, P.1    Palese, P.2    O'Neill, R.E.3
  • 35
    • 0030576521 scopus 로고    scopus 로고
    • Peptide-surface association: The case of PDZ and PTB domains
    • Harrison S.C. Peptide-surface association: the case of PDZ and PTB domains. Cell. 86:1996;341-343.
    • (1996) Cell , vol.86 , pp. 341-343
    • Harrison, S.C.1
  • 37
    • 0032217264 scopus 로고    scopus 로고
    • Structure of an IκBα/NF-κB complex
    • Jacobs M.D., Harrison S.C. Structure of an IκBα/NF-κB complex. Cell. 95:1998;749-758.
    • (1998) Cell , vol.95 , pp. 749-758
    • Jacobs, M.D.1    Harrison, S.C.2
  • 38
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • Cingolani G., Petosa C., Weis K., Müller C.W. Structure of importin-β bound to the IBB domain of importin-α Nature. 399:1999;221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Müller, C.W.4
  • 39
    • 0025223160 scopus 로고
    • Solution structure of the DNA-binding domain of the oestrogen receptor
    • Schwabe J.W., Neuhaus D., Rhodes D. Solution structure of the DNA-binding domain of the oestrogen receptor. Nature. 348:1990;458-461.
    • (1990) Nature , vol.348 , pp. 458-461
    • Schwabe, J.W.1    Neuhaus, D.2    Rhodes, D.3
  • 40
    • 0027049805 scopus 로고
    • The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: Crystal structure of the DNA complex
    • Ellenberger T.E., Brandl C.J., Struhl K., Harrison S.C. The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted α helices: crystal structure of the DNA complex. Cell. 71:1992;1223-1237.
    • (1992) Cell , vol.71 , pp. 1223-1237
    • Ellenberger, T.E.1    Brandl, C.J.2    Struhl, K.3    Harrison, S.C.4
  • 41
    • 0028073893 scopus 로고
    • Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor
    • Staley J.P., Kim P.S. Formation of a native-like subdomain in a partially folded intermediate of bovine pancreatic trypsin inhibitor. Protein Sci. 3:1994;1822-1832.
    • (1994) Protein Sci. , vol.3 , pp. 1822-1832
    • Staley, J.P.1    Kim, P.S.2
  • 42
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 44
    • 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., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 45
    • 3543012707 scopus 로고    scopus 로고
    • Crystallographic and NMR system: A new software system for macromolecular structure determination
    • Brünger A.T., Warren G.L.et al. Crystallographic and NMR system: a new software system for macromolecular structure determination. Acta Crystallogr. D. 54:1998;905-921.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brünger, A.T.1    Warren, G.L.2
  • 46
  • 47
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


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