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Volumn 468, Issue 3, 2015, Pages 353-362

Nuclear localization signals for four distinct Karyopherin-β nuclear import systems

Author keywords

Importin; Karyopherin; Nuclear import; Nuclear localization signal (NLS); Nuclear pore; Nucleocytoplasmic transport

Indexed keywords

KAP121 PROTEIN; KARYOPHERIN BETA; KARYOPHERIN BETA2; LYSINE; PROTEIN; UNCLASSIFIED DRUG; ISOPROTEIN; NUCLEAR EXPORT SIGNAL; NUCLEAR LOCALIZATION SIGNAL; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 84934920273     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20150368     Document Type: Review
Times cited : (137)

References (147)
  • 1
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich, D. and Kutay, U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15, 607-660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 3
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • Conti, E. and Izaurralde, E. (2001) Nucleocytoplasmic transport enters the atomic age. Curr. Opin. Cell Biol. 13, 310-319
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 4
    • 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
  • 5
    • 35348903268 scopus 로고    scopus 로고
    • SnapShot: Nuclear transport
    • Tran, E. J., Bolger, T. A. and Wente, S. R. (2007) SnapShot: nuclear transport. Cell 131, 420
    • (2007) Cell , vol.131 , pp. 420
    • Tran, E.J.1    Bolger, T.A.2    Wente, S.R.3
  • 6
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • Cook, A., Bono, F., Jinek, M. and Conti, E. (2007) Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76, 647-671
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 7
    • 78649650714 scopus 로고    scopus 로고
    • Recognition of nuclear targeting signals by Karyopherin-β proteins
    • Xu, D., Farmer, A. and Chook, Y. M. (2010) Recognition of nuclear targeting signals by Karyopherin-β proteins. Curr. Opin. Struct. Biol. 20, 782-790
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 782-790
    • Xu, D.1    Farmer, A.2    Chook, Y.M.3
  • 8
    • 79960912049 scopus 로고    scopus 로고
    • Nuclear import by karyopherin-βs: Recognition and inhibition
    • Chook, Y. M. and Suel, K. E. (2011) Nuclear import by karyopherin-βs: recognition and inhibition. Biochim. Biophys. Acta 1813, 1593-1606
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1593-1606
    • Chook, Y.M.1    Suel, K.E.2
  • 9
    • 84904465312 scopus 로고    scopus 로고
    • Atomic basis of CRM1-cargo recognition, release and inhibition
    • Fung, H. Y. and Chook, Y. M. (2014) Atomic basis of CRM1-cargo recognition, release and inhibition. Semin. Cancer Biol. 27, 52-61
    • (2014) Semin. Cancer Biol. , vol.27 , pp. 52-61
    • Fung, H.Y.1    Chook, Y.M.2
  • 10
    • 79959865166 scopus 로고    scopus 로고
    • TDP-43 and FUS: A nuclear affair
    • Dormann, D. and Haass, C. (2011) TDP-43 and FUS: a nuclear affair. Trends Neurosci. 34, 339-348
    • (2011) Trends Neurosci. , vol.34 , pp. 339-348
    • Dormann, D.1    Haass, C.2
  • 11
    • 79551472601 scopus 로고    scopus 로고
    • Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS
    • Ito, D., Seki, M., Tsunoda, Y., Uchiyama, H. and Suzuki, N. (2011) Nuclear transport impairment of amyotrophic lateral sclerosis-linked mutations in FUS/TLS. Ann. Neurol. 69, 152-162
    • (2011) Ann. Neurol. , vol.69 , pp. 152-162
    • Ito, D.1    Seki, M.2    Tsunoda, Y.3    Uchiyama, H.4    Suzuki, N.5
  • 13
    • 84892502706 scopus 로고    scopus 로고
    • Viral subversion of nucleocytoplasmic trafficking
    • Yarbrough, M. L., Mata, M. A., Sakthivel, R. and Fontoura, B. M. (2014) Viral subversion of nucleocytoplasmic trafficking. Traffic 15, 127-140
    • (2014) Traffic , vol.15 , pp. 127-140
    • Yarbrough, M.L.1    Mata, M.A.2    Sakthivel, R.3    Fontoura, B.M.4
  • 14
    • 79955679956 scopus 로고    scopus 로고
    • Evolution of the karyopherin-β family of nucleocytoplasmic transport factors; ancient origins and continued specialization
    • O'Reilly, A. J., Dacks, J. B. and Field, M. C. (2011) Evolution of the karyopherin-β family of nucleocytoplasmic transport factors; ancient origins and continued specialization. PLoS ONE 6, e19308
    • (2011) PLoS ONE , vol.6 , pp. e19308
    • O'Reilly, A.J.1    Dacks, J.B.2    Field, M.C.3
  • 15
    • 47849096203 scopus 로고    scopus 로고
    • Evolutionary and transcriptional analysis of karyopherin β superfamily proteins
    • Quan, Y., Ji, Z. L., Wang, X., Tartakoff, A. M. and Tao, T. (2008) Evolutionary and transcriptional analysis of karyopherin β superfamily proteins. Mol. Cell. Proteomics 7, 1254-1269
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 1254-1269
    • Quan, Y.1    Ji, Z.L.2    Wang, X.3    Tartakoff, A.M.4    Tao, T.5
  • 16
    • 33748449145 scopus 로고    scopus 로고
    • Atomic resolution structures in nuclear transport
    • Suel, K. E., Cansizoglu, A. E. and Chook, Y. M. (2006) Atomic resolution structures in nuclear transport. Methods 39, 342-355
    • (2006) Methods , vol.39 , pp. 342-355
    • Suel, K.E.1    Cansizoglu, A.E.2    Chook, Y.M.3
  • 17
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • Lee, S. J., Matsuura, Y., Liu, S. M. and Stewart, M. (2005) Structural basis for nuclear import complex dissociation by RanGTP. Nature 435, 693-696
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 18
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • Mosammaparast, N. and Pemberton, L. F. (2004) Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol. 14, 547-556
    • (2004) Trends Cell Biol. , vol.14 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 19
    • 33646482468 scopus 로고    scopus 로고
    • Karyopherin flexibility in nucleocytoplasmic transport
    • Conti, E., Muller, C. W. and Stewart, M. (2006) Karyopherin flexibility in nucleocytoplasmic transport. Curr. Opin. Struct. Biol. 16, 237-244
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 237-244
    • Conti, E.1    Muller, C.W.2    Stewart, M.3
  • 20
    • 0039115156 scopus 로고    scopus 로고
    • Transport into and out of the cell nucleus
    • Gorlich, D. (1998) Transport into and out of the cell nucleus. EMBO J. 17, 2721-2727
    • (1998) EMBO J. , vol.17 , pp. 2721-2727
    • Gorlich, D.1
  • 21
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • Pemberton, L. F. and Paschal, B. M. (2005) Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6, 187-198
    • (2005) Traffic , vol.6 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 22
    • 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. (1995) 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. U. S. A. 92, 2008-2011
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 2008-2011
    • Moroianu, J.1    Blobel, G.2    Radu, A.3
  • 23
    • 0029028762 scopus 로고
    • The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate
    • Kraemer, D. M., Strambio-de-Castillia, C., Blobel, G. and Rout, M. P. (1995) The essential yeast nucleoporin NUP159 is located on the cytoplasmic side of the nuclear pore complex and serves in karyopherin-mediated binding of transport substrate. J. Biol. Chem. 270, 19017-19021
    • (1995) J. Biol. Chem. , vol.270 , pp. 19017-19021
    • Kraemer, D.M.1    Strambio-De-Castillia, C.2    Blobel, G.3    Rout, M.P.4
  • 24
    • 0020188311 scopus 로고
    • A polypeptide domain that specifies migration of nucleoplasmin into the nucleus
    • Dingwall, C., Sharnick, S. V. and Laskey, R. A. (1982) A polypeptide domain that specifies migration of nucleoplasmin into the nucleus. Cell 30, 449-458
    • (1982) Cell , vol.30 , pp. 449-458
    • Dingwall, C.1    Sharnick, S.V.2    Laskey, R.A.3
  • 25
    • 0021269089 scopus 로고
    • Sequence requirements for nuclear location of simian virus 40 large-T antigen
    • Kalderon, D., Richardson, W. D., Markham, A. F. and Smith, A. E. (1984) Sequence requirements for nuclear location of simian virus 40 large-T antigen. Nature 311, 33-38
    • (1984) Nature , vol.311 , pp. 33-38
    • Kalderon, D.1    Richardson, W.D.2    Markham, A.F.3    Smith, A.E.4
  • 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
  • 27
    • 34247135913 scopus 로고    scopus 로고
    • Classical nuclear localization signals: Definition, function, and interaction with importin α
    • Lange, A., Mills, R. E., Lange, C. J., Stewart, M., Devine, S. E. and Corbett, A. H. (2007) Classical nuclear localization signals: definition, function, and interaction with importin α. J. Biol. Chem. 282, 5101-5105
    • (2007) J. Biol. Chem. , vol.282 , pp. 5101-5105
    • Lange, A.1    Mills, R.E.2    Lange, C.J.3    Stewart, M.4    Devine, S.E.5    Corbett, A.H.6
  • 28
    • 67650136746 scopus 로고    scopus 로고
    • Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus
    • Suel, K. E. and Chook, Y. M. (2009) Kap104p imports the PY-NLS-containing transcription factor Tfg2p into the nucleus. J. Biol. Chem. 284, 15416-15424
    • (2009) J. Biol. Chem. , vol.284 , pp. 15416-15424
    • Suel, K.E.1    Chook, Y.M.2
  • 29
    • 33746776838 scopus 로고    scopus 로고
    • Rules for nuclear localization sequence recognition by karyopherin β2
    • Lee, B. J., Cansizoglu, A. E., Suel, K. E., Louis, T. H., Zhang, Z. and Chook, Y. M. (2006) Rules for nuclear localization sequence recognition by karyopherin β2. Cell 126, 543-558
    • (2006) Cell , vol.126 , pp. 543-558
    • Lee, B.J.1    Cansizoglu, A.E.2    Suel, K.E.3    Louis, T.H.4    Zhang, Z.5    Chook, Y.M.6
  • 30
    • 84864366184 scopus 로고    scopus 로고
    • Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS)
    • Zhang, Z. C. and Chook, Y. M. (2012) Structural and energetic basis of ALS-causing mutations in the atypical proline-tyrosine nuclear localization signal of the Fused in Sarcoma protein (FUS). Proc. Natl. Acad. Sci. U. S. A. 109, 12017-12021
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 12017-12021
    • Zhang, Z.C.1    Chook, Y.M.2
  • 31
    • 67349140506 scopus 로고    scopus 로고
    • Structural basis for leucine-rich nuclear export signal recognition by CRM1
    • Dong, X., Biswas, A., Suel, K. E., Jackson, L. K., Martinez, R., Gu, H. and Chook, Y. M. (2009) Structural basis for leucine-rich nuclear export signal recognition by CRM1. Nature 458, 1136-1141
    • (2009) Nature , vol.458 , pp. 1136-1141
    • Dong, X.1    Biswas, A.2    Suel, K.E.3    Jackson, L.K.4    Martinez, R.5    Gu, H.6    Chook, Y.M.7
  • 33
    • 0036923972 scopus 로고    scopus 로고
    • Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β
    • Cingolani, G., Bednenko, J., Gillespie, M. T. and Gerace, L. (2002) Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β. Mol. Cell 10, 1345-1353
    • (2002) Mol. Cell , vol.10 , pp. 1345-1353
    • Cingolani, G.1    Bednenko, J.2    Gillespie, M.T.3    Gerace, L.4
  • 34
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • Cingolani, G., Petosa, C., Weis, K. and Muller, C. W. (1999) Structure of importin-β bound to the IBB domain of importin-α. Nature 399, 221-229
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 36
    • 84922326889 scopus 로고    scopus 로고
    • Diversification of importin-α isoforms in cellular trafficking and disease states
    • Pumroy, R. A. and Cingolani, G. (2015) Diversification of importin-α isoforms in cellular trafficking and disease states. Biochem. J. 466, 13-28
    • (2015) Biochem. J. , vol.466 , pp. 13-28
    • Pumroy, R.A.1    Cingolani, G.2
  • 37
    • 84900439244 scopus 로고    scopus 로고
    • Transportin-1 and Transportin-2: Protein nuclear import and beyond
    • Twyffels, L., Gueydan, C. and Kruys, V. (2014) Transportin-1 and Transportin-2: protein nuclear import and beyond. FEBS Lett. 588, 1857-1868
    • (2014) FEBS Lett. , vol.588 , pp. 1857-1868
    • Twyffels, L.1    Gueydan, C.2    Kruys, V.3
  • 38
    • 84904505245 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated DJ-1 monomerization modulates intracellular trafficking involving karyopherin β2
    • Bjorkblom, B., Maple-Grodem, J., Puno, M. R., Odell, M., Larsen, J. P. and Moller, S. G. (2014) Reactive oxygen species-mediated DJ-1 monomerization modulates intracellular trafficking involving karyopherin β2. Mol. Cell. Biol. 34, 3024-3040
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 3024-3040
    • Bjorkblom, B.1    Maple-Grodem, J.2    Puno, M.R.3    Odell, M.4    Larsen, J.P.5    Moller, S.G.6
  • 39
    • 84870317115 scopus 로고    scopus 로고
    • The nuclear localization of glycogen synthase kinase 3β is required its putative PY-nuclear localization sequences
    • Shin, S. H., Lee, E. J., Chun, J., Hyun, S., Kim, Y. I. and Kang, S. S. (2012) The nuclear localization of glycogen synthase kinase 3β is required its putative PY-nuclear localization sequences. Mol. Cells 34, 375-382
    • (2012) Mol. Cells , vol.34 , pp. 375-382
    • Shin, S.H.1    Lee, E.J.2    Chun, J.3    Hyun, S.4    Kim, Y.I.5    Kang, S.S.6
  • 40
    • 84896861295 scopus 로고    scopus 로고
    • Suppressor of fused impedes Ci/Gli nuclear import by opposing Trn/Kapβ2 in Hedgehog signaling
    • Shi, Q., Han, Y. and Jiang, J. (2014) Suppressor of fused impedes Ci/Gli nuclear import by opposing Trn/Kapβ2 in Hedgehog signaling. J. Cell Sci. 127, 1092-1103
    • (2014) J. Cell Sci. , vol.127 , pp. 1092-1103
    • Shi, Q.1    Han, Y.2    Jiang, J.3
  • 41
    • 84864337336 scopus 로고    scopus 로고
    • A PY-nuclear localization signal is required for nuclear accumulation of HCMV UL79 protein
    • Wang, L., Li, M., Cai, M., Xing, J., Wang, S. and Zheng, C. (2012) A PY-nuclear localization signal is required for nuclear accumulation of HCMV UL79 protein. Med. Microbiol. Immunol. 201, 381-387
    • (2012) Med. Microbiol. Immunol. , vol.201 , pp. 381-387
    • Wang, L.1    Li, M.2    Cai, M.3    Xing, J.4    Wang, S.5    Zheng, C.6
  • 42
    • 84873947122 scopus 로고    scopus 로고
    • Identification of a karyopherin β1/β2 proline-tyrosine nuclear localization signal in huntingtin protein
    • Desmond, C. R., Atwal, R. S., Xia, J. and Truant, R. (2012) Identification of a karyopherin β1/β2 proline-tyrosine nuclear localization signal in huntingtin protein. J. Biol. Chem. 287, 39626-39633
    • (2012) J. Biol. Chem. , vol.287 , pp. 39626-39633
    • Desmond, C.R.1    Atwal, R.S.2    Xia, J.3    Truant, R.4
  • 43
    • 84873424140 scopus 로고    scopus 로고
    • A proline-tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1
    • Mallet, P. L. and Bachand, F. (2013) A proline-tyrosine nuclear localization signal (PY-NLS) is required for the nuclear import of fission yeast PAB2, but not of human PABPN1. Traffic 14, 282-294
    • (2013) Traffic , vol.14 , pp. 282-294
    • Mallet, P.L.1    Bachand, F.2
  • 44
    • 80052959701 scopus 로고    scopus 로고
    • FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations
    • Neumann, M., Bentmann, E., Dormann, D., Jawaid, A., DeJesus-Hernandez, M., Ansorge, O., Roeber, S., Kretzschmar, H. A., Munoz, D. G., Kusaka, H. et al. (2011) FET proteins TAF15 and EWS are selective markers that distinguish FTLD with FUS pathology from amyotrophic lateral sclerosis with FUS mutations. Brain 134, 2595-2609
    • (2011) Brain , vol.134 , pp. 2595-2609
    • Neumann, M.1    Bentmann, E.2    Dormann, D.3    Jawaid, A.4    De Jesus-Hernandez, M.5    Ansorge, O.6    Roeber, S.7    Kretzschmar, H.A.8    Munoz, D.G.9    Kusaka, H.10
  • 46
    • 84881261748 scopus 로고    scopus 로고
    • A masked PY-NLS in Drosophila TIS11 and its mammalian homolog tristetraprolin
    • Twyffels, L., Wauquier, C., Soin, R., Decaestecker, C., Gueydan, C. and Kruys, V. (2013) A masked PY-NLS in Drosophila TIS11 and its mammalian homolog tristetraprolin. PLoS ONE 8, e71686
    • (2013) PLoS ONE , vol.8 , pp. e71686
    • Twyffels, L.1    Wauquier, C.2    Soin, R.3    Decaestecker, C.4    Gueydan, C.5    Kruys, V.6
  • 48
    • 84898756024 scopus 로고    scopus 로고
    • Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration
    • Bernis, C., Swift-Taylor, B., Nord, M., Carmona, S., Chook, Y. M. and Forbes, D. J. (2014) Transportin acts to regulate mitotic assembly events by target binding rather than Ran sequestration. Mol. Biol. Cell 25, 992-1009
    • (2014) Mol. Biol. Cell , vol.25 , pp. 992-1009
    • Bernis, C.1    Swift-Taylor, B.2    Nord, M.3    Carmona, S.4    Chook, Y.M.5    Forbes, D.J.6
  • 50
    • 79952798372 scopus 로고    scopus 로고
    • Localization of retinitis pigmentosa 2 to cilia is regulated by Importin β2
    • Hurd, T. W., Fan, S. and Margolis, B. L. (2011) Localization of retinitis pigmentosa 2 to cilia is regulated by Importin β2. J. Cell Sci. 124, 718-726
    • (2011) J. Cell Sci. , vol.124 , pp. 718-726
    • Hurd, T.W.1    Fan, S.2    Margolis, B.L.3
  • 52
    • 84867290759 scopus 로고    scopus 로고
    • FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS
    • Niu, C., Zhang, J., Gao, F., Yang, L., Jia, M., Zhu, H. and Gong, W. (2012) FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS. PLoS ONE 7, e47056
    • (2012) PLoS ONE , vol.7 , pp. e47056
    • Niu, C.1    Zhang, J.2    Gao, F.3    Yang, L.4    Jia, M.5    Zhu, H.6    Gong, W.7
  • 53
    • 43149121353 scopus 로고    scopus 로고
    • Molecular basis for the recognition of snurportin 1 by importin β
    • Mitrousis, G., Olia, A. S., Walker-Kopp, N. and Cingolani, G. (2008) Molecular basis for the recognition of snurportin 1 by importin β. J. Biol. Chem. 283, 7877-7884
    • (2008) J. Biol. Chem. , vol.283 , pp. 7877-7884
    • Mitrousis, G.1    Olia, A.S.2    Walker-Kopp, N.3    Cingolani, G.4
  • 54
    • 0033548434 scopus 로고    scopus 로고
    • Importin β recognizes parathyroid hormone-related protein with high affinity and mediates its nuclear import in the absence of importin α
    • Lam, M. H., Briggs, L. J., Hu, W., Martin, T. J., Gillespie, M. T. and Jans, D. A. (1999) Importin β recognizes parathyroid hormone-related protein with high affinity and mediates its nuclear import in the absence of importin α. J. Biol. Chem. 274, 7391-7398
    • (1999) J. Biol. Chem. , vol.274 , pp. 7391-7398
    • Lam, M.H.1    Briggs, L.J.2    Hu, W.3    Martin, T.J.4    Gillespie, M.T.5    Jans, D.A.6
  • 58
    • 0035898685 scopus 로고    scopus 로고
    • Importin 13: A novel mediator of nuclear import and export
    • Mingot, J. M., Kostka, S., Kraft, R., Hartmann, E. and Gorlich, D. (2001) Importin 13: a novel mediator of nuclear import and export. EMBO J. 20, 3685-3694
    • (2001) EMBO J. , vol.20 , pp. 3685-3694
    • Mingot, J.M.1    Kostka, S.2    Kraft, R.3    Hartmann, E.4    Gorlich, D.5
  • 59
    • 2442642835 scopus 로고    scopus 로고
    • Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13
    • Ploski, J. E., Shamsher, M. K. and Radu, A. (2004) Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13. Mol. Cell. Biol. 24, 4824-4834
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4824-4834
    • Ploski, J.E.1    Shamsher, M.K.2    Radu, A.3
  • 60
    • 66449105245 scopus 로고    scopus 로고
    • Importin 13 mediates nuclear import of histone fold-containing chromatin accessibility complex heterodimers
    • Walker, P., Doenecke, D. and Kahle, J. (2009) Importin 13 mediates nuclear import of histone fold-containing chromatin accessibility complex heterodimers. J. Biol. Chem. 284, 11652-11662
    • (2009) J. Biol. Chem. , vol.284 , pp. 11652-11662
    • Walker, P.1    Doenecke, D.2    Kahle, J.3
  • 61
    • 20744448038 scopus 로고    scopus 로고
    • Subunits of the heterotrimeric transcription factor NF-Y are imported into the nucleus by distinct pathways involving importin β and importin 13
    • Kahle, J., Baake, M., Doenecke, D. and Albig, W. (2005) Subunits of the heterotrimeric transcription factor NF-Y are imported into the nucleus by distinct pathways involving importin β and importin 13. Mol. Cell. Biol. 25, 5339-5354
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5339-5354
    • Kahle, J.1    Baake, M.2    Doenecke, D.3    Albig, W.4
  • 63
    • 74749084019 scopus 로고    scopus 로고
    • Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13
    • Bono, F., Cook, A. G., Grunwald, M., Ebert, J. and Conti, E. (2010) Nuclear import mechanism of the EJC component Mago-Y14 revealed by structural studies of importin 13. Mol. Cell 37, 211-222
    • (2010) Mol. Cell , vol.37 , pp. 211-222
    • Bono, F.1    Cook, A.G.2    Grunwald, M.3    Ebert, J.4    Conti, E.5
  • 64
    • 84877694405 scopus 로고    scopus 로고
    • Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p
    • Kobayashi, J. and Matsuura, Y. (2013) Structural basis for cell-cycle-dependent nuclear import mediated by the karyopherin Kap121p. J. Mol. Biol. 425, 1852-1868
    • (2013) J. Mol. Biol. , vol.425 , pp. 1852-1868
    • Kobayashi, J.1    Matsuura, Y.2
  • 66
    • 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
  • 67
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Gorlich, 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
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 68
    • 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
  • 69
    • 0028950991 scopus 로고
    • Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins
    • Radu, A., Blobel, G. and Moore, M. S. (1995) Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. U. S. A. 92, 1769-1773
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 1769-1773
    • Radu, A.1    Blobel, G.2    Moore, M.S.3
  • 70
    • 79960915158 scopus 로고    scopus 로고
    • The importin β binding domain as a master regulator of nucleocytoplasmic transport
    • Lott, K. and Cingolani, G. (2011) The importin β binding domain as a master regulator of nucleocytoplasmic transport. Biochim. Biophys. Acta 1813, 1578-1592
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1578-1592
    • Lott, K.1    Cingolani, G.2
  • 71
    • 84858294567 scopus 로고    scopus 로고
    • Structural basis of high-affinity nuclear localization signal interactions with importin-α
    • Marfori, M., Lonhienne, T. G., Forwood, J. K. and Kobe, B. (2012) Structural basis of high-affinity nuclear localization signal interactions with importin-α. Traffic 13, 532-548
    • (2012) Traffic , vol.13 , pp. 532-548
    • Marfori, M.1    Lonhienne, T.G.2    Forwood, J.K.3    Kobe, B.4
  • 72
    • 84883141388 scopus 로고    scopus 로고
    • Identification of cargo proteins specific for importin-β with importin-α applying a stable isotope labeling by amino acids in cell culture (SILAC)-based in vitro transport system
    • Kimura, M., Okumura, N., Kose, S., Takao, T. and Imamoto, N. (2013) Identification of cargo proteins specific for importin-β with importin-α applying a stable isotope labeling by amino acids in cell culture (SILAC)-based in vitro transport system. J. Biol. Chem. 288, 24540-24549
    • (2013) J. Biol. Chem. , vol.288 , pp. 24540-24549
    • Kimura, M.1    Okumura, N.2    Kose, S.3    Takao, T.4    Imamoto, N.5
  • 74
    • 77953750360 scopus 로고    scopus 로고
    • Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-α using oriented peptide library screening
    • Yang, S. N., Takeda, A. A., Fontes, M. R., Harris, J. M., Jans, D. A. and Kobe, B. (2010) Probing the specificity of binding to the major nuclear localization sequence-binding site of importin-α using oriented peptide library screening. J. Biol. Chem. 285, 19935-19946
    • (2010) J. Biol. Chem. , vol.285 , pp. 19935-19946
    • Yang, S.N.1    Takeda, A.A.2    Fontes, M.R.3    Harris, J.M.4    Jans, D.A.5    Kobe, B.6
  • 75
    • 33645659409 scopus 로고    scopus 로고
    • A functional proteomics approach for the detection of nuclear proteins based on derepressed importin α
    • Blazek, E. and Meisterernst, M. (2006) A functional proteomics approach for the detection of nuclear proteins based on derepressed importin α. Proteomics 6, 2070-2078
    • (2006) Proteomics , vol.6 , pp. 2070-2078
    • Blazek, E.1    Meisterernst, M.2
  • 77
    • 79953838272 scopus 로고    scopus 로고
    • Proteomic analysis of importin α-interacting proteins in adult mouse brain
    • Fukumoto, M., Sekimoto, T. and Yoneda, Y. (2011) Proteomic analysis of importin α-interacting proteins in adult mouse brain. Cell Struct. Funct. 36, 57-67
    • (2011) Cell Struct. Funct. , vol.36 , pp. 57-67
    • Fukumoto, M.1    Sekimoto, T.2    Yoneda, Y.3
  • 79
    • 84871885622 scopus 로고    scopus 로고
    • Identification of karyopherin α1 and α7 interacting proteins in porcine tissue
    • Park, K. E., Inerowicz, H. D., Wang, X., Li, Y., Koser, S. and Cabot, R. A. (2012) Identification of karyopherin α1 and α7 interacting proteins in porcine tissue. PLoS ONE 7, e38990
    • (2012) PLoS ONE , vol.7 , pp. e38990
    • Park, K.E.1    Inerowicz, H.D.2    Wang, X.3    Li, Y.4    Koser, S.5    Cabot, R.A.6
  • 80
    • 0032950628 scopus 로고    scopus 로고
    • Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α
    • Kobe, B. (1999) Autoinhibition by an internal nuclear localization signal revealed by the crystal structure of mammalian importin α. Nat. Struct. Biol. 6, 388-397
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 388-397
    • Kobe, B.1
  • 81
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α
    • Fontes, M. R., Teh, T. and Kobe, B. (2000) Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α. J. Mol. Biol. 297, 1183-1194
    • (2000) J. Mol. Biol. , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 83
    • 0041845285 scopus 로고    scopus 로고
    • Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-α
    • Fontes, M. R., Teh, T., Jans, D., Brinkworth, R. I. and Kobe, B. (2003) Structural basis for the specificity of bipartite nuclear localization sequence binding by importin-α. J. Biol. Chem. 278, 27981-27987
    • (2003) J. Biol. Chem. , vol.278 , pp. 27981-27987
    • Fontes, M.R.1    Teh, T.2    Jans, D.3    Brinkworth, R.I.4    Kobe, B.5
  • 84
    • 0142231575 scopus 로고    scopus 로고
    • Role of flanking sequences and phosphorylation in the recognition of the simian-virus-40 large T-antigen nuclear localization sequences by importin-α
    • Fontes, M. R., Teh, T., Toth, G., John, A., Pavo, I., Jans, D. A. and Kobe, B. (2003) Role of flanking sequences and phosphorylation in the recognition of the simian-virus-40 large T-antigen nuclear localization sequences by importin-α. Biochem. J. 375, 339-349
    • (2003) Biochem. J. , vol.375 , pp. 339-349
    • Fontes, M.R.1    Teh, T.2    Toth, G.3    John, A.4    Pavo, I.5    Jans, D.A.6    Kobe, B.7
  • 85
    • 15444368332 scopus 로고    scopus 로고
    • Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin α
    • Chen, M. H., Ben-Efraim, I., Mitrousis, G., Walker-Kopp, N., Sims, P. J. and Cingolani, G. (2005) Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin α. J. Biol. Chem. 280, 10599-10606
    • (2005) J. Biol. Chem. , vol.280 , pp. 10599-10606
    • Chen, M.H.1    Ben-Efraim, I.2    Mitrousis, G.3    Walker-Kopp, N.4    Sims, P.J.5    Cingolani, G.6
  • 86
    • 27744577638 scopus 로고    scopus 로고
    • Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling
    • Matsuura, Y. and Stewart, M. (2005) Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling. EMBO J. 24, 3681-3689
    • (2005) EMBO J. , vol.24 , pp. 3681-3689
    • Matsuura, Y.1    Stewart, M.2
  • 87
    • 43149125406 scopus 로고    scopus 로고
    • Structural basis for the nuclear import of the human androgen receptor
    • Cutress, M. L., Whitaker, H. C., Mills, I. G., Stewart, M. and Neal, D. E. (2008) Structural basis for the nuclear import of the human androgen receptor. J. Cell Sci. 121, 957-968
    • (2008) J. Cell Sci. , vol.121 , pp. 957-968
    • Cutress, M.L.1    Whitaker, H.C.2    Mills, I.G.3    Stewart, M.4    Neal, D.E.5
  • 88
    • 69949149572 scopus 로고    scopus 로고
    • The molecular basis for the regulation of the cap-binding complex by the importins
    • Dias, S. M., Wilson, K. F., Rojas, K. S., Ambrosio, A. L. and Cerione, R. A. (2009) The molecular basis for the regulation of the cap-binding complex by the importins. Nat. Struct. Mol. Biol. 16, 930-937
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 930-937
    • Dias, S.M.1    Wilson, K.F.2    Rojas, K.S.3    Ambrosio, A.L.4    Cerione, R.A.5
  • 89
    • 77952909627 scopus 로고    scopus 로고
    • Novel binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-α
    • Giesecke, A. and Stewart, M. (2010) Novel binding of the mitotic regulator TPX2 (target protein for Xenopus kinesin-like protein 2) to importin-α. J. Biol. Chem. 285, 17628-17635
    • (2010) J. Biol. Chem. , vol.285 , pp. 17628-17635
    • Giesecke, A.1    Stewart, M.2
  • 90
    • 80051541300 scopus 로고    scopus 로고
    • A minimal nuclear localization signal (NLS) in human phospholipid scramblase 4 that binds only the minor NLS-binding site of importin α1
    • Lott, K., Bhardwaj, A., Sims, P. J. and Cingolani, G. (2011) A minimal nuclear localization signal (NLS) in human phospholipid scramblase 4 that binds only the minor NLS-binding site of importin α1. J. Biol. Chem. 286, 28160-28169
    • (2011) J. Biol. Chem. , vol.286 , pp. 28160-28169
    • Lott, K.1    Bhardwaj, A.2    Sims, P.J.3    Cingolani, G.4
  • 91
    • 79955616324 scopus 로고    scopus 로고
    • Crystal structure of importin-α bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4
    • Mynott, A. V., Harrop, S. J., Brown, L. J., Breit, S. N., Kobe, B. and Curmi, P. M. (2011) Crystal structure of importin-α bound to a peptide bearing the nuclear localisation signal from chloride intracellular channel protein 4. FEBS J. 278, 1662-1675
    • (2011) FEBS J. , vol.278 , pp. 1662-1675
    • Mynott, A.V.1    Harrop, S.J.2    Brown, L.J.3    Breit, S.N.4    Kobe, B.5    Curmi, P.M.6
  • 92
    • 80052038304 scopus 로고    scopus 로고
    • Structural basis of importin-α-mediated nuclear transport for Ku70 and Ku80
    • Takeda, A. A., De Barros, A. C., Chang, C. W., Kobe, B. and Fontes, M. R. (2011) Structural basis of importin-α-mediated nuclear transport for Ku70 and Ku80. J. Mol. Biol. 412, 226-234
    • (2011) J. Mol. Biol. , vol.412 , pp. 226-234
    • Takeda, A.A.1    De Barros, A.C.2    Chang, C.W.3    Kobe, B.4    Fontes, M.R.5
  • 93
    • 80054842900 scopus 로고    scopus 로고
    • Sensing actin dynamics: Structural basis for G-actin-sensitive nuclear import of MAL
    • Hirano, H. and Matsuura, Y. (2011) Sensing actin dynamics: structural basis for G-actin-sensitive nuclear import of MAL. Biochem. Biophys. Res. Commun. 414, 373-378
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 373-378
    • Hirano, H.1    Matsuura, Y.2
  • 95
    • 84873047215 scopus 로고    scopus 로고
    • Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals
    • Chang, C. W., Counago, R. L., Williams, S. J., Boden, M. and Kobe, B. (2012) Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals. Plant Cell 24, 5074-5088
    • (2012) Plant Cell , vol.24 , pp. 5074-5088
    • Chang, C.W.1    Counago, R.L.2    Williams, S.J.3    Boden, M.4    Kobe, B.5
  • 96
    • 84885371123 scopus 로고    scopus 로고
    • Distinctive conformation of minor site-specific nuclear localization signals bound to importin-α
    • Chang, C. W., Counago, R. M., Williams, S. J., Boden, M. and Kobe, B. (2013) Distinctive conformation of minor site-specific nuclear localization signals bound to importin-α. Traffic 14, 1144-1154 PubMed
    • (2013) Traffic , vol.14 , pp. 1144-1154
    • Chang, C.W.1    Counago, R.M.2    Williams, S.J.3    Boden, M.4    Kobe, B.5
  • 98
    • 84892408508 scopus 로고    scopus 로고
    • Structural characterisation of the nuclear import receptor importin α in complex with the bipartite NLS of Prp20
    • Roman, N., Christie, M., Swarbrick, C. M., Kobe, B. and Forwood, J. K. (2013) Structural characterisation of the nuclear import receptor importin α in complex with the bipartite NLS of Prp20. PLoS ONE 8, e82038
    • (2013) PLoS ONE , vol.8 , pp. e82038
    • Roman, N.1    Christie, M.2    Swarbrick, C.M.3    Kobe, B.4    Forwood, J.K.5
  • 100
    • 84930190367 scopus 로고    scopus 로고
    • Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7
    • Pumroy, R. A., Ke, S., Hart, D. J., Zachariae, U. and Cingolani, G. (2015) Molecular determinants for nuclear import of influenza A PB2 by importin α isoforms 3 and 7. Structure 23, 374-384
    • (2015) Structure , vol.23 , pp. 374-384
    • Pumroy, R.A.1    Ke, S.2    Hart, D.J.3    Zachariae, U.4    Cingolani, G.5
  • 101
    • 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. and Kuriyan, J. (1998) Crystallographic analysis of the recognition of a nuclear localization signal by the nuclear import factor karyopherin α. Cell 94, 193-204
    • (1998) Cell , vol.94 , pp. 193-204
    • Conti, E.1    Uy, M.2    Leighton, L.3    Blobel, G.4    Kuriyan, J.5
  • 102
    • 0142073738 scopus 로고    scopus 로고
    • Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import
    • Matsuura, Y., Lange, A., Harreman, M. T., Corbett, A. H. and Stewart, M. (2003) Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import. EMBO J. 22, 5358-5369
    • (2003) EMBO J. , vol.22 , pp. 5358-5369
    • Matsuura, Y.1    Lange, A.2    Harreman, M.T.3    Corbett, A.H.4    Stewart, M.5
  • 103
    • 45849096845 scopus 로고    scopus 로고
    • Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals
    • Suel, K. E., Gu, H. and Chook, Y. M. (2008) Modular organization and combinatorial energetics of proline-tyrosine nuclear localization signals. PLoS Biol. 6, e137
    • (2008) PLoS Biol. , vol.6 , pp. e137
    • Suel, K.E.1    Gu, H.2    Chook, Y.M.3
  • 104
    • 82655189968 scopus 로고    scopus 로고
    • Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1
    • Zhang, Z. C., Satterly, N., Fontoura, B. M. and Chook, Y. M. (2011) Evolutionary development of redundant nuclear localization signals in the mRNA export factor NXF1. Mol. Biol. Cell 22, 4657-4668
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4657-4668
    • Zhang, Z.C.1    Satterly, N.2    Fontoura, B.M.3    Chook, Y.M.4
  • 105
    • 35748960826 scopus 로고    scopus 로고
    • Conformational heterogeneity of karyopherin β2 is segmental
    • Cansizoglu, A. E. and Chook, Y. M. (2007) Conformational heterogeneity of karyopherin β2 is segmental. Structure 15, 1431-1441
    • (2007) Structure , vol.15 , pp. 1431-1441
    • Cansizoglu, A.E.1    Chook, Y.M.2
  • 108
    • 62849103689 scopus 로고    scopus 로고
    • RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1
    • Fritz, J., Strehblow, A., Taschner, A., Schopoff, S., Pasierbek, P. and Jantsch, M. F. (2009) RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1. Mol. Cell. Biol. 29, 1487-1497
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1487-1497
    • Fritz, J.1    Strehblow, A.2    Taschner, A.3    Schopoff, S.4    Pasierbek, P.5    Jantsch, M.F.6
  • 109
    • 84899893118 scopus 로고    scopus 로고
    • A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1
    • Barraud, P., Banerjee, S., Mohamed, W. I., Jantsch, M. F. and Allain, F. H. (2014) A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1. Proc. Natl. Acad. Sci. U. S. A. 111, E1852-E1861
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. E1852-E1861
    • Barraud, P.1    Banerjee, S.2    Mohamed, W.I.3    Jantsch, M.F.4    Allain, F.H.5
  • 112
    • 84885084354 scopus 로고    scopus 로고
    • Identification and functional implication of nuclear localization signals in the N-terminal domain of JMJD5
    • Huang, X., Zhang, L., Qi, H., Shao, J. and Shen, J. (2013) Identification and functional implication of nuclear localization signals in the N-terminal domain of JMJD5. Biochimie 95, 2114-2122
    • (2013) Biochimie , vol.95 , pp. 2114-2122
    • Huang, X.1    Zhang, L.2    Qi, H.3    Shao, J.4    Shen, J.5
  • 113
    • 69949085720 scopus 로고    scopus 로고
    • Identification of a nuclear localization signal in the polo box domain of Plk1
    • Lee, M. S., Huang, Y. H., Huang, S. P., Lin, R. I., Wu, S. F. and Li, C. (2009) Identification of a nuclear localization signal in the polo box domain of Plk1. Biochim. Biophys. Acta 1793, 1571-1578
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 1571-1578
    • Lee, M.S.1    Huang, Y.H.2    Huang, S.P.3    Lin, R.I.4    Wu, S.F.5    Li, C.6
  • 114
    • 84875536742 scopus 로고    scopus 로고
    • The quantitative assessment of the role played by basic amino acid clusters in the nuclear uptake of human ribosomal protein L7
    • Tai, L. R., Chou, C. W., Lee, I. F., Kirby, R. and Lin, A. (2013) The quantitative assessment of the role played by basic amino acid clusters in the nuclear uptake of human ribosomal protein L7. Exp. Cell Res. 319, 367-375
    • (2013) Exp. Cell Res. , vol.319 , pp. 367-375
    • Tai, L.R.1    Chou, C.W.2    Lee, I.F.3    Kirby, R.4    Lin, A.5
  • 115
    • 55849092067 scopus 로고    scopus 로고
    • Chemokine receptor CCR2 undergoes transportin1-dependent nuclear translocation
    • Favre, N., Camps, M., Arod, C., Chabert, C., Rommel, C. and Pasquali, C. (2008) Chemokine receptor CCR2 undergoes transportin1-dependent nuclear translocation. Proteomics 8, 4560-4576
    • (2008) Proteomics , vol.8 , pp. 4560-4576
    • Favre, N.1    Camps, M.2    Arod, C.3    Chabert, C.4    Rommel, C.5    Pasquali, C.6
  • 116
    • 84871881617 scopus 로고    scopus 로고
    • Identification of cargo proteins specific for the nucleocytoplasmic transport carrier transportin by combination of an in vitro transport system and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics
    • Kimura, M., Kose, S., Okumura, N., Imai, K., Furuta, M., Sakiyama, N., Tomii, K., Horton, P., Takao, T. and Imamoto, N. (2013) Identification of cargo proteins specific for the nucleocytoplasmic transport carrier transportin by combination of an in vitro transport system and stable isotope labeling by amino acids in cell culture (SILAC)-based quantitative proteomics. Mol. Cell. Proteomics 12, 145-157
    • (2013) Mol. Cell. Proteomics , vol.12 , pp. 145-157
    • Kimura, M.1    Kose, S.2    Okumura, N.3    Imai, K.4    Furuta, M.5    Sakiyama, N.6    Tomii, K.7    Horton, P.8    Takao, T.9    Imamoto, N.10
  • 117
    • 0040251482 scopus 로고    scopus 로고
    • Importin β, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells
    • Jakel, S. and Gorlich, D. (1998) Importin β, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells. EMBO J. 17, 4491-4502
    • (1998) EMBO J. , vol.17 , pp. 4491-4502
    • Jakel, S.1    Gorlich, D.2
  • 118
    • 34948906397 scopus 로고    scopus 로고
    • Nuclear import of c-Jun. Is mediated by multiple transport receptors
    • Waldmann, I., Walde, S. and Kehlenbach, R. H. (2007) Nuclear import of c-Jun. is mediated by multiple transport receptors. J. Biol. Chem. 282, 27685-27692
    • (2007) J. Biol. Chem. , vol.282 , pp. 27685-27692
    • Waldmann, I.1    Walde, S.2    Kehlenbach, R.H.3
  • 119
    • 0034763206 scopus 로고    scopus 로고
    • Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin
    • Dean, K. A., Von Ahsen, O., Gorlich, D. and Fried, H. M. (2001) Signal recognition particle protein 19 is imported into the nucleus by importin 8 (RanBP8) and transportin. J. Cell Sci. 114, 3479-3485 PubMed
    • (2001) J. Cell Sci. , vol.114 , pp. 3479-3485
    • Dean, K.A.1    Von Ahsen, O.2    Gorlich, D.3    Fried, H.M.4
  • 120
    • 0347611086 scopus 로고    scopus 로고
    • Cell cycle regulated transport controlled by alterations in the nuclear pore complex
    • Makhnevych, T., Lusk, C. P., Anderson, A. M., Aitchison, J. D. and Wozniak, R. W. (2003) Cell cycle regulated transport controlled by alterations in the nuclear pore complex. Cell 115, 813-823
    • (2003) Cell , vol.115 , pp. 813-823
    • Makhnevych, T.1    Lusk, C.P.2    Anderson, A.M.3    Aitchison, J.D.4    Wozniak, R.W.5
  • 121
    • 0030722506 scopus 로고    scopus 로고
    • A distinct nuclear import pathway used by ribosomal proteins
    • Rout, M. P., Blobel, G. and Aitchison, J. D. (1997) A distinct nuclear import pathway used by ribosomal proteins. Cell 89, 715-725
    • (1997) Cell , vol.89 , pp. 715-725
    • Rout, M.P.1    Blobel, G.2    Aitchison, J.D.3
  • 122
    • 0030984329 scopus 로고    scopus 로고
    • Cloning and characterization of human karyopherin β3
    • Yaseen, N. R. and Blobel, G. (1997) Cloning and characterization of human karyopherin β3. Proc. Natl. Acad. Sci. U. S. A. 94, 4451-4456
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 4451-4456
    • Yaseen, N.R.1    Blobel, G.2
  • 123
    • 0035696925 scopus 로고    scopus 로고
    • Core histones and linker histones are imported into the nucleus by different pathways
    • Baake, M., Bauerle, M., Doenecke, D. and Albig, W. (2001) Core histones and linker histones are imported into the nucleus by different pathways. Eur. J. Cell Biol. 80, 669-677
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 669-677
    • Baake, M.1    Bauerle, M.2    Doenecke, D.3    Albig, W.4
  • 124
    • 0034859839 scopus 로고    scopus 로고
    • Multiple pathways contribute to nuclear import of core histones
    • Muhlhausser, P., Muller, E. C., Otto, A. and Kutay, U. (2001) Multiple pathways contribute to nuclear import of core histones. EMBO Rep. 2, 690-696
    • (2001) EMBO Rep. , vol.2 , pp. 690-696
    • Muhlhausser, P.1    Muller, E.C.2    Otto, A.3    Kutay, U.4
  • 126
    • 34547099863 scopus 로고    scopus 로고
    • Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import
    • Blackwell, Jr, J. S., Wilkinson, S. T., Mosammaparast, N. and Pemberton, L. F. (2007) Mutational analysis of H3 and H4 N termini reveals distinct roles in nuclear import. J. Biol. Chem. 282, 20142-20150
    • (2007) J. Biol. Chem. , vol.282 , pp. 20142-20150
    • Blackwell, J.S.1    Wilkinson, S.T.2    Mosammaparast, N.3    Pemberton, L.F.4
  • 127
    • 0032168565 scopus 로고    scopus 로고
    • Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
    • Kaffman, A., Rank, N. M. and O'Shea, E. K. (1998) Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121. Genes Dev. 12, 2673-2683
    • (1998) Genes Dev. , vol.12 , pp. 2673-2683
    • Kaffman, A.1    Rank, N.M.2    O'Shea, E.K.3
  • 128
    • 0035947627 scopus 로고    scopus 로고
    • Nuclear import of Spo12p, a protein essential for meiosis
    • Chaves, S. R. and Blobel, G. (2001) Nuclear import of Spo12p, a protein essential for meiosis. J. Biol. Chem. 276, 17712-17717
    • (2001) J. Biol. Chem. , vol.276 , pp. 17712-17717
    • Chaves, S.R.1    Blobel, G.2
  • 129
    • 0035153830 scopus 로고    scopus 로고
    • Pse1/Kap121-dependent nuclear localization of the major yeast multidrug resistance (MDR) transcription factor Pdr1
    • Delahodde, A., Pandjaitan, R., Corral-Debrinski, M. and Jacq, C. (2001) Pse1/Kap121-dependent nuclear localization of the major yeast multidrug resistance (MDR) transcription factor Pdr1. Mol. Microbiol. 39, 304-312
    • (2001) Mol. Microbiol. , vol.39 , pp. 304-312
    • Delahodde, A.1    Pandjaitan, R.2    Corral-Debrinski, M.3    Jacq, C.4
  • 130
    • 0035877849 scopus 로고    scopus 로고
    • Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress
    • Isoyama, T., Murayama, A., Nomoto, A. and Kuge, S. (2001) Nuclear import of the yeast AP-1-like transcription factor Yap1p is mediated by transport receptor Pse1p, and this import step is not affected by oxidative stress. J. Biol. Chem. 276, 21863-21869
    • (2001) J. Biol. Chem. , vol.276 , pp. 21863-21869
    • Isoyama, T.1    Murayama, A.2    Nomoto, A.3    Kuge, S.4
  • 131
    • 0036210710 scopus 로고    scopus 로고
    • Kap121p-mediated nuclear import is required for mating and cellular differentiation in yeast
    • Leslie, D. M., Grill, B., Rout, M. P., Wozniak, R. W. and Aitchison, J. D. (2002) Kap121p-mediated nuclear import is required for mating and cellular differentiation in yeast. Mol. Cell. Biol. 22, 2544-2555
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2544-2555
    • Leslie, D.M.1    Grill, B.2    Rout, M.P.3    Wozniak, R.W.4    Aitchison, J.D.5
  • 132
    • 4544352379 scopus 로고    scopus 로고
    • Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import
    • Leslie, D. M., Zhang, W., Timney, B. L., Chait, B. T., Rout, M. P., Wozniak, R. W. and Aitchison, J. D. (2004) Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import. Mol. Cell. Biol. 24, 8487-8503
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8487-8503
    • Leslie, D.M.1    Zhang, W.2    Timney, B.L.3    Chait, B.T.4    Rout, M.P.5    Wozniak, R.W.6    Aitchison, J.D.7
  • 133
    • 0347379904 scopus 로고    scopus 로고
    • Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae
    • Ueta, R., Fukunaka, A. and Yamaguchi-Iwai, Y. (2003) Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae. J. Biol. Chem. 278, 50120-50127
    • (2003) J. Biol. Chem. , vol.278 , pp. 50120-50127
    • Ueta, R.1    Fukunaka, A.2    Yamaguchi-Iwai, Y.3
  • 134
    • 84872265426 scopus 로고    scopus 로고
    • Mitosis-specific regulation of nuclear transport by the spindle assembly checkpoint protein Mad1p
    • Cairo, L. V., Ptak, C. and Wozniak, R. W. (2013) Mitosis-specific regulation of nuclear transport by the spindle assembly checkpoint protein Mad1p. Mol. Cell 49, 109-120
    • (2013) Mol. Cell , vol.49 , pp. 109-120
    • Cairo, L.V.1    Ptak, C.2    Wozniak, R.W.3
  • 135
    • 0037191049 scopus 로고    scopus 로고
    • Karyopherins in nuclear pore biogenesis: A role for Kap121p in the assembly of Nup53p into nuclear pore complexes
    • Lusk, C. P., Makhnevych, T., Marelli, M., Aitchison, J. D. and Wozniak, R. W. (2002) Karyopherins in nuclear pore biogenesis: a role for Kap121p in the assembly of Nup53p into nuclear pore complexes. J. Cell Biol. 159, 267-278
    • (2002) J. Cell Biol. , vol.159 , pp. 267-278
    • Lusk, C.P.1    Makhnevych, T.2    Marelli, M.3    Aitchison, J.D.4    Wozniak, R.W.5
  • 136
    • 0033553882 scopus 로고    scopus 로고
    • Transportin-SR, a nuclear import receptor for SR proteins
    • Kataoka, N., Bachorik, J. L. and Dreyfuss, G. (1999) Transportin-SR, a nuclear import receptor for SR proteins. J. Cell Biol. 145, 1145-1152
    • (1999) J. Cell Biol. , vol.145 , pp. 1145-1152
    • Kataoka, N.1    Bachorik, J.L.2    Dreyfuss, G.3
  • 137
    • 0034677884 scopus 로고    scopus 로고
    • A human importin-β family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins
    • Lai, M. C., Lin, R. I., Huang, S. Y., Tsai, C. W. and Tarn, W. Y. (2000) A human importin-β family protein, transportin-SR2, interacts with the phosphorylated RS domain of SR proteins. J. Biol. Chem. 275, 7950-7957
    • (2000) J. Biol. Chem. , vol.275 , pp. 7950-7957
    • Lai, M.C.1    Lin, R.I.2    Huang, S.Y.3    Tsai, C.W.4    Tarn, W.Y.5
  • 138
    • 0035964258 scopus 로고    scopus 로고
    • Transportin-SR2 mediates nuclear import of phosphorylated SR proteins
    • Lai, M. C., Lin, R. I. and Tarn, W. Y. (2001) Transportin-SR2 mediates nuclear import of phosphorylated SR proteins. Proc. Natl. Acad. Sci. U. S. A. 98, 10154-10159
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10154-10159
    • Lai, M.C.1    Lin, R.I.2    Tarn, W.Y.3
  • 139
    • 0038043222 scopus 로고    scopus 로고
    • Phosphorylation-dependent and -independent nuclear import of RS domain-containing splicing factors and regulators
    • Yun, C. Y., Velazquez-Dones, A. L., Lyman, S. K. and Fu, X. D. (2003) Phosphorylation-dependent and -independent nuclear import of RS domain-containing splicing factors and regulators. J. Biol. Chem. 278, 18050-18055
    • (2003) J. Biol. Chem. , vol.278 , pp. 18050-18055
    • Yun, C.Y.1    Velazquez-Dones, A.L.2    Lyman, S.K.3    Fu, X.D.4
  • 140
    • 0036329228 scopus 로고    scopus 로고
    • A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1
    • Allemand, E., Dokudovskaya, S., Bordonne, R. and Tazi, J. (2002) A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1. Mol. Biol. Cell 13, 2436-2447
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2436-2447
    • Allemand, E.1    Dokudovskaya, S.2    Bordonne, R.3    Tazi, J.4
  • 141
    • 0037451327 scopus 로고    scopus 로고
    • A novel splicing regulator shares a nuclear import pathway with SR proteins
    • Lai, M. C., Kuo, H. W., Chang, W. C. and Tarn, W. Y. (2003) A novel splicing regulator shares a nuclear import pathway with SR proteins. EMBO J. 22, 1359-1369
    • (2003) EMBO J. , vol.22 , pp. 1359-1369
    • Lai, M.C.1    Kuo, H.W.2    Chang, W.C.3    Tarn, W.Y.4
  • 142
    • 0032522343 scopus 로고    scopus 로고
    • Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p
    • Senger, B., Simos, G., Bischoff, F. R., Podtelejnikov, A., Mann, M. and Hurt, E. (1998) Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J. 17, 2196-2207
    • (1998) EMBO J. , vol.17 , pp. 2196-2207
    • Senger, B.1    Simos, G.2    Bischoff, F.R.3    Podtelejnikov, A.4    Mann, M.5    Hurt, E.6
  • 144
    • 79959831970 scopus 로고    scopus 로고
    • Transportin-SR is required for proper splicing of resistance genes and plant immunity
    • Xu, S., Zhang, Z., Jing, B., Gannon, P., Ding, J., Xu, F., Li, X. and Zhang, Y. (2011) Transportin-SR is required for proper splicing of resistance genes and plant immunity. PLoS Genet. 7, e1002159
    • (2011) PLoS Genet. , vol.7 , pp. e1002159
    • Xu, S.1    Zhang, Z.2    Jing, B.3    Gannon, P.4    Ding, J.5    Xu, F.6    Li, X.7    Zhang, Y.8
  • 145
    • 82655186588 scopus 로고    scopus 로고
    • 3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus
    • 3 depletion is determined by capsid and detectable after viral cDNA enters the nucleus. Retrovirology 8, 98
    • (2011) Retrovirology , vol.8 , pp. 98
    • De Iaco, A.1    Luban, J.2


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