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Volumn 14, Issue 10, 2004, Pages 547-556

Karyopherins: From nuclear-transport mediators to nuclear-function regulators

Author keywords

[No Author keywords available]

Indexed keywords

KARYOPHERIN; RNA;

EID: 4644278442     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2004.09.004     Document Type: Review
Times cited : (281)

References (91)
  • 1
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • I.G. Macara Transport into and out of the nucleus Microbiol. Mol. Biol. Rev. 65 2001 570 594
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • MacAra, I.G.1
  • 2
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • K. Weis Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle Cell 112 2003 441 451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 3
    • 0345374584 scopus 로고    scopus 로고
    • The structure of importin-β bound to SREBP-2: Nuclear import of a transcription factor
    • S.J. Lee The structure of importin-β bound to SREBP-2: nuclear import of a transcription factor Science 302 2003 1571 1575
    • (2003) Science , vol.302 , pp. 1571-1575
    • Lee, S.J.1
  • 4
    • 0036923972 scopus 로고    scopus 로고
    • Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β
    • G. Cingolani Molecular basis for the recognition of a nonclassical nuclear localization signal by importin β Mol. Cell 10 2002 1345 1353
    • (2002) Mol. Cell , vol.10 , pp. 1345-1353
    • Cingolani, G.1
  • 5
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-β bound to the IBB domain of importin-α
    • G. Cingolani 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
  • 6
    • 0346457106 scopus 로고    scopus 로고
    • Conformational variability of nucleo-cytoplasmic transport factors
    • N. Fukuhara Conformational variability of nucleo-cytoplasmic transport factors J. Biol. Chem. 279 2004 2176 2181
    • (2004) J. Biol. Chem. , vol.279 , pp. 2176-2181
    • Fukuhara, N.1
  • 7
    • 0037016722 scopus 로고    scopus 로고
    • Pathways mediating the nuclear import of histones H3 and H4 in yeast
    • N. Mosammaparast Pathways mediating the nuclear import of histones H3 and H4 in yeast J. Biol. Chem. 277 2002 862 868
    • (2002) J. Biol. Chem. , vol.277 , pp. 862-868
    • Mosammaparast, N.1
  • 8
    • 0035897406 scopus 로고    scopus 로고
    • Nuclear import of histone H2A and H2B is mediated by a network of karyopherins
    • N. Mosammaparast Nuclear import of histone H2A and H2B is mediated by a network of karyopherins J. Cell Biol. 153 2001 251 262
    • (2001) J. Cell Biol. , vol.153 , pp. 251-262
    • Mosammaparast, N.1
  • 9
    • 0034859839 scopus 로고    scopus 로고
    • Multiple pathways contribute to nuclear import of core histones
    • P. Muhlhausser Multiple pathways contribute to nuclear import of core histones EMBO Rep. 2 2001 690 696
    • (2001) EMBO Rep. , vol.2 , pp. 690-696
    • Muhlhausser, P.1
  • 10
    • 0040251482 scopus 로고    scopus 로고
    • Importin β, transportin, RanBP5 and anBP7 mediate nuclear import of ribosomal proteins in mammalian cells
    • S. Jakel, and D. Gorlich Importin β, transportin, RanBP5 and anBP7 mediate nuclear import of ribosomal proteins in mammalian cells EMBO J. 17 1998 4491 4502
    • (1998) EMBO J. , vol.17 , pp. 4491-4502
    • Jakel, S.1    Gorlich, D.2
  • 11
    • 0030722506 scopus 로고    scopus 로고
    • A distinct nuclear import pathway used by ribosomal proteins
    • M.P. Rout A distinct nuclear import pathway used by ribosomal proteins Cell 89 1997 715 725
    • (1997) Cell , vol.89 , pp. 715-725
    • Rout, M.P.1
  • 12
    • 0037370443 scopus 로고    scopus 로고
    • Intersection of the Kap123p-mediated nuclear import and ribosome export pathways
    • Y. Sydorskyy Intersection of the Kap123p-mediated nuclear import and ribosome export pathways Mol. Cell. Biol. 23 2003 2042 2054
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2042-2054
    • Sydorskyy, Y.1
  • 13
    • 0037011167 scopus 로고    scopus 로고
    • A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B
    • N. Mosammaparast A role for nucleosome assembly protein 1 in the nuclear transport of histones H2A and H2B EMBO J. 21 2002 6527 6538
    • (2002) EMBO J. , vol.21 , pp. 6527-6538
    • Mosammaparast, N.1
  • 14
    • 0034646512 scopus 로고    scopus 로고
    • PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation
    • M. Ohno PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation Cell 101 2000 187 198
    • (2000) Cell , vol.101 , pp. 187-198
    • Ohno, M.1
  • 15
    • 0034623941 scopus 로고    scopus 로고
    • Identification of a functional nuclear export sequence in BRCA1
    • J.A. Rodriguez, and B.R. Henderson Identification of a functional nuclear export sequence in BRCA1 J. Biol. Chem. 275 2000 38589 38596
    • (2000) J. Biol. Chem. , vol.275 , pp. 38589-38596
    • Rodriguez, J.A.1    Henderson, B.R.2
  • 16
    • 0347988235 scopus 로고    scopus 로고
    • Nuclear export of microRNA precursors
    • E. Lund Nuclear export of microRNA precursors Science 303 2004 95 98
    • (2004) Science , vol.303 , pp. 95-98
    • Lund, E.1
  • 17
    • 0347361541 scopus 로고    scopus 로고
    • Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs
    • R. Yi Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs Genes Dev. 17 2003 3011 3016
    • (2003) Genes Dev. , vol.17 , pp. 3011-3016
    • Yi, R.1
  • 18
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • M.P. Rout The yeast nuclear pore complex: composition, architecture, and transport mechanism J. Cell Biol. 148 2000 635 651
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1
  • 19
    • 0037008997 scopus 로고    scopus 로고
    • Proteomic analysis of the mammalian nuclear pore complex
    • J.M. Cronshaw Proteomic analysis of the mammalian nuclear pore complex J. Cell Biol. 158 2002 915 927
    • (2002) J. Cell Biol. , vol.158 , pp. 915-927
    • Cronshaw, J.M.1
  • 20
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • M. Suntharalingam, and S.R. Wente Peering through the pore: nuclear pore complex structure, assembly, and function Dev. Cell 4 2003 775 789
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 21
    • 0242391971 scopus 로고    scopus 로고
    • Virtual gating and nuclear transport: The hole picture
    • M.P. Rout Virtual gating and nuclear transport: the hole picture Trends Cell Biol. 13 2003 622 628
    • (2003) Trends Cell Biol. , vol.13 , pp. 622-628
    • Rout, M.P.1
  • 22
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • K. Ribbeck, and D. Gorlich The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion EMBO J. 21 2002 2664 2671
    • (2002) EMBO J. , vol.21 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 23
    • 0035931750 scopus 로고    scopus 로고
    • Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import
    • I. Ben-Efraim, and L. Gerace Gradient of increasing affinity of importin β for nucleoporins along the pathway of nuclear import J. Cell Biol. 152 2001 411 417
    • (2001) J. Cell Biol. , vol.152 , pp. 411-417
    • Ben-Efraim, I.1    Gerace, L.2
  • 24
    • 0142180053 scopus 로고    scopus 로고
    • A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex
    • B. Pyhtila, and M. Rexach A gradient of affinity for the karyopherin Kap95p along the yeast nuclear pore complex J. Biol. Chem. 278 2003 42699 42709
    • (2003) J. Biol. Chem. , vol.278 , pp. 42699-42709
    • Pyhtila, B.1    Rexach, M.2
  • 25
    • 0032489840 scopus 로고    scopus 로고
    • Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr
    • S. Shah Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr J. Cell Biol. 141 1998 31 49
    • (1998) J. Cell Biol. , vol.141 , pp. 31-49
    • Shah, S.1
  • 26
    • 0035802121 scopus 로고    scopus 로고
    • The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex
    • D. Denning The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p at the nuclear pore complex J. Cell Biol. 154 2001 937 950
    • (2001) J. Cell Biol. , vol.154 , pp. 937-950
    • Denning, D.1
  • 27
    • 0037043339 scopus 로고    scopus 로고
    • The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import
    • T.C. Walther The cytoplasmic filaments of the nuclear pore complex are dispensable for selective nuclear protein import J. Cell Biol. 158 2002 63 77
    • (2002) J. Cell Biol. , vol.158 , pp. 63-77
    • Walther, T.C.1
  • 28
    • 0033578298 scopus 로고    scopus 로고
    • The direction of transport through the nuclear pore can be inverted
    • M.V. Nachury, and K. Weis The direction of transport through the nuclear pore can be inverted Proc. Natl. Acad. Sci. U. S. A. 96 1999 9622 9627
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9622-9627
    • Nachury, M.V.1    Weis, K.2
  • 29
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • L.A. Strawn Minimal nuclear pore complexes define FG repeat domains essential for transport Nat. Cell Biol. 6 2004 197 206
    • (2004) Nat. Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.A.1
  • 30
    • 0034729194 scopus 로고    scopus 로고
    • Yeast nucleoporins involved in passive nuclear envelope permeability
    • N. Shulga Yeast nucleoporins involved in passive nuclear envelope permeability J. Cell Biol. 149 2000 1027 1038
    • (2000) J. Cell Biol. , vol.149 , pp. 1027-1038
    • Shulga, N.1
  • 31
    • 0347611086 scopus 로고    scopus 로고
    • Cell cycle regulated transport controlled by alterations in the nuclear pore complex
    • T. Makhnevych Cell cycle regulated transport controlled by alterations in the nuclear pore complex Cell 115 2003 813 823
    • (2003) Cell , vol.115 , pp. 813-823
    • Makhnevych, T.1
  • 32
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2-Ran-GppNHp
    • Y.M. Chook, and G. Blobel Structure of the nuclear transport complex karyopherin-β2-Ran-GppNHp Nature 399 1999 230 237
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 33
    • 0037018838 scopus 로고    scopus 로고
    • Uncoupling Kapβ2 substrate dissociation and ran binding
    • Y.M. Chook Uncoupling Kapβ2 substrate dissociation and ran binding Biochemistry 41 2002 6955 6966
    • (2002) Biochemistry , vol.41 , pp. 6955-6966
    • Chook, Y.M.1
  • 34
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • M. Fornerod CRM1 is an export receptor for leucine-rich nuclear export signals Cell 90 1997 1051 1060
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1
  • 35
    • 0036469888 scopus 로고    scopus 로고
    • Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains
    • S. Jakel Importins fulfil a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains EMBO J. 21 2002 377 386
    • (2002) EMBO J. , vol.21 , pp. 377-386
    • Jakel, S.1
  • 36
    • 0033536178 scopus 로고    scopus 로고
    • Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation
    • R.E. Carazo-Salas Generation of GTP-bound Ran by RCC1 is required for chromatin-induced mitotic spindle formation Nature 400 1999 178 181
    • (1999) Nature , vol.400 , pp. 178-181
    • Carazo-Salas, R.E.1
  • 37
    • 0033591373 scopus 로고    scopus 로고
    • Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran
    • A. Wilde, and Y. Zheng Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran Science 284 1999 1359 1362
    • (1999) Science , vol.284 , pp. 1359-1362
    • Wilde, A.1    Zheng, Y.2
  • 38
    • 0033591386 scopus 로고    scopus 로고
    • Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran
    • T. Ohba Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran Science 284 1999 1356 1358
    • (1999) Science , vol.284 , pp. 1356-1358
    • Ohba, T.1
  • 39
    • 0035951480 scopus 로고    scopus 로고
    • Role of importin-β in coupling Ran to downstream targets in microtubule assembly
    • C. Wiese Role of importin-β in coupling Ran to downstream targets in microtubule assembly Science 291 2001 653 656
    • (2001) Science , vol.291 , pp. 653-656
    • Wiese, C.1
  • 40
    • 0035846901 scopus 로고    scopus 로고
    • Importin β is a mitotic target of the small GTPase Ran in spindle assembly
    • M.V. Nachury Importin β is a mitotic target of the small GTPase Ran in spindle assembly Cell 104 2001 95 106
    • (2001) Cell , vol.104 , pp. 95-106
    • Nachury, M.V.1
  • 41
    • 17744380396 scopus 로고    scopus 로고
    • Ran induces spindle assembly by reversing the inhibitory effect of importin is α on TPX2 activity
    • O.J. Gruss Ran induces spindle assembly by reversing the inhibitory effect of importin is α on TPX2 activity Cell 104 2001 83 93
    • (2001) Cell , vol.104 , pp. 83-93
    • Gruss, O.J.1
  • 42
    • 0030298137 scopus 로고    scopus 로고
    • A complex of NuMA and cytoplasmic dynein is essential for mitotic spindle assembly
    • A. Merdes A complex of NuMA and cytoplasmic dynein is essential for mitotic spindle assembly Cell 87 1996 447 458
    • (1996) Cell , vol.87 , pp. 447-458
    • Merdes, A.1
  • 43
    • 0034717818 scopus 로고    scopus 로고
    • TPX2, a novel Xenopus MAP involved in spindle pole organization
    • T. Wittmann TPX2, A novel Xenopus MAP involved in spindle pole organization J. Cell Biol. 149 2000 1405 1418
    • (2000) J. Cell Biol. , vol.149 , pp. 1405-1418
    • Wittmann, T.1
  • 44
    • 0037046812 scopus 로고    scopus 로고
    • Ran binds to chromatin by two distinct mechanisms
    • D. Bilbao-Cortes Ran binds to chromatin by two distinct mechanisms Curr. Biol. 12 2002 1151 1156
    • (2002) Curr. Biol. , vol.12 , pp. 1151-1156
    • Bilbao-Cortes, D.1
  • 45
    • 0035947299 scopus 로고    scopus 로고
    • Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B
    • M.E. Nemergut Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B Science 292 2001 1540 1543
    • (2001) Science , vol.292 , pp. 1540-1543
    • Nemergut, M.E.1
  • 46
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts
    • P. Kalab Visualization of a Ran-GTP gradient in interphase and mitotic Xenopus egg extracts Science 295 2002 2452 2456
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1
  • 47
    • 4143086570 scopus 로고    scopus 로고
    • Mitotic functions of the Ran GTPase network: The importance of being in the right place at the right time
    • B. Di Fiore Mitotic functions of the Ran GTPase network: the importance of being in the right place at the right time Cell Cycle 3 2004 305 313
    • (2004) Cell Cycle , vol.3 , pp. 305-313
    • Di Fiore, B.1
  • 48
    • 0038699131 scopus 로고    scopus 로고
    • The small GTPase Ran: Interpreting the signs
    • B.B. Quimby, and M. Dasso The small GTPase Ran: interpreting the signs Curr. Opin. Cell Biol. 15 2003 338 344
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 338-344
    • Quimby, B.B.1    Dasso, M.2
  • 49
    • 0038686567 scopus 로고    scopus 로고
    • The Ran GTPase regulates kinetochore function
    • A. Arnaoutov, and M. Dasso The Ran GTPase regulates kinetochore function Dev. Cell 5 2003 99 111
    • (2003) Dev. Cell , vol.5 , pp. 99-111
    • Arnaoutov, A.1    Dasso, M.2
  • 50
    • 0033638971 scopus 로고    scopus 로고
    • GTP hydrolysis by Ran is required for nuclear envelope assembly
    • M. Hetzer GTP hydrolysis by Ran is required for nuclear envelope assembly Mol. Cell 5 2000 1013 1024
    • (2000) Mol. Cell , vol.5 , pp. 1013-1024
    • Hetzer, M.1
  • 51
    • 0034717035 scopus 로고    scopus 로고
    • Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts
    • C. Zhang, and P.R. Clarke Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts Science 288 2000 1429 1432
    • (2000) Science , vol.288 , pp. 1429-1432
    • Zhang, C.1    Clarke, P.R.2
  • 52
    • 0042238022 scopus 로고    scopus 로고
    • RanGTP mediates nuclear pore complex assembly
    • T.C. Walther RanGTP mediates nuclear pore complex assembly Nature 424 2003 689 694
    • (2003) Nature , vol.424 , pp. 689-694
    • Walther, T.C.1
  • 53
    • 0345374574 scopus 로고    scopus 로고
    • Importin β negatively regulates nuclear membrane fusion and nuclear pore complex assembly
    • A. Harel Importin β negatively regulates nuclear membrane fusion and nuclear pore complex assembly Mol. Biol. Cell 14 2003 4387 4396
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4387-4396
    • Harel, A.1
  • 54
    • 0242668887 scopus 로고    scopus 로고
    • The conserved Nup107-160 complex is critical for nuclear pore complex assembly
    • T.C. Walther The conserved Nup107-160 complex is critical for nuclear pore complex assembly Cell 113 2003 195 206
    • (2003) Cell , vol.113 , pp. 195-206
    • Walther, T.C.1
  • 55
    • 0037547118 scopus 로고    scopus 로고
    • Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores
    • A. Harel Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores Mol. Cell 11 2003 853 864
    • (2003) Mol. Cell , vol.11 , pp. 853-864
    • Harel, A.1
  • 56
    • 0344670185 scopus 로고    scopus 로고
    • The Ran GTPase cycle is required for yeast nuclear pore complex assembly
    • K.J. Ryan The Ran GTPase cycle is required for yeast nuclear pore complex assembly J. Cell Biol. 160 2003 1041 1053
    • (2003) J. Cell Biol. , vol.160 , pp. 1041-1053
    • Ryan, K.J.1
  • 57
    • 0037418871 scopus 로고    scopus 로고
    • A role for Ran-GTP and Crm1 in blocking re-replication
    • R. Yamaguchi, and J. Newport A role for Ran-GTP and Crm1 in blocking re-replication Cell 113 2003 115 125
    • (2003) Cell , vol.113 , pp. 115-125
    • Yamaguchi, R.1    Newport, J.2
  • 59
    • 0035575518 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Ran, β and beyond
    • S. Kuersten Nucleocytoplasmic transport: Ran, β and beyond Trends Cell Biol. 11 2001 497 503
    • (2001) Trends Cell Biol. , vol.11 , pp. 497-503
    • Kuersten, S.1
  • 60
    • 0032168565 scopus 로고    scopus 로고
    • Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121
    • A. Kaffman Phosphorylation regulates association of the transcription factor Pho4 with its import receptor Pse1/Kap121 Genes Dev. 12 1998 2673 2683
    • (1998) Genes Dev. , vol.12 , pp. 2673-2683
    • Kaffman, A.1
  • 61
    • 0032481048 scopus 로고    scopus 로고
    • The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus
    • A. Kaffman The receptor Msn5 exports the phosphorylated transcription factor Pho4 out of the nucleus Nature 396 1998 482 486
    • (1998) Nature , vol.396 , pp. 482-486
    • Kaffman, A.1
  • 62
    • 0344270855 scopus 로고    scopus 로고
    • Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): A potential regulatory mechanism for PDK-1 function
    • M.A. Lim Nuclear translocation of 3′-phosphoinositide-dependent protein kinase 1 (PDK-1): a potential regulatory mechanism for PDK-1 function Proc. Natl. Acad. Sci. U. S. A. 100 2003 14006 14011
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 14006-14011
    • Lim, M.A.1
  • 63
    • 1542284074 scopus 로고    scopus 로고
    • Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6
    • M. Geymonat Clb6/Cdc28 and Cdc14 regulate phosphorylation status and cellular localization of Swi6 Mol. Cell. Biol. 24 2004 2277 2285
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 2277-2285
    • Geymonat, M.1
  • 64
    • 0034597816 scopus 로고    scopus 로고
    • Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
    • T.A. McKinsey Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation Nature 408 2000 106 111
    • (2000) Nature , vol.408 , pp. 106-111
    • McKinsey, T.A.1
  • 65
    • 2342436343 scopus 로고    scopus 로고
    • Nuclear import and activity of histone deacetylase in Xenopus oocytes is regulated by phosphorylation
    • D.A. Smillie Nuclear import and activity of histone deacetylase in Xenopus oocytes is regulated by phosphorylation J. Cell Sci. 117 2004 1857 1866
    • (2004) J. Cell Sci. , vol.117 , pp. 1857-1866
    • Smillie, D.A.1
  • 66
    • 1042278767 scopus 로고    scopus 로고
    • Nuclear transport and cancer: From mechanism to intervention
    • T.R. Kau Nuclear transport and cancer: from mechanism to intervention Nat. Rev. Cancer 4 2004 106 117
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 106-117
    • Kau, T.R.1
  • 67
    • 1542467522 scopus 로고    scopus 로고
    • DNA damage response-mediated degradation of HO endonuclease via the ubiquitin system involves its nuclear export
    • L. Kaplun DNA damage response-mediated degradation of HO endonuclease via the ubiquitin system involves its nuclear export J. Biol. Chem. 278 2003 48727 48734
    • (2003) J. Biol. Chem. , vol.278 , pp. 48727-48734
    • Kaplun, L.1
  • 68
    • 0037011124 scopus 로고    scopus 로고
    • Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C(Cdh1)
    • M. Jaquenoud Cell cycle-dependent nuclear export of Cdh1p may contribute to the inactivation of APC/C(Cdh1) EMBO J. 21 2002 6515 6526
    • (2002) EMBO J. , vol.21 , pp. 6515-6526
    • Jaquenoud, M.1
  • 69
    • 0036500167 scopus 로고    scopus 로고
    • Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site
    • L.M. Boustany, and M.S. Cyert Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site Genes Dev. 16 2002 608 619
    • (2002) Genes Dev. , vol.16 , pp. 608-619
    • Boustany, L.M.1    Cyert, M.S.2
  • 70
    • 0037080980 scopus 로고    scopus 로고
    • Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor
    • W. Gorner Acute glucose starvation activates the nuclear localization signal of a stress-specific yeast transcription factor EMBO J. 21 2002 135 144
    • (2002) EMBO J. , vol.21 , pp. 135-144
    • Gorner, W.1
  • 71
    • 0033523996 scopus 로고    scopus 로고
    • The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae
    • M.J. DeVit, and M. Johnston The nuclear exportin Msn5 is required for nuclear export of the Mig1 glucose repressor of Saccharomyces cerevisiae Curr. Biol. 9 1999 1231 1241
    • (1999) Curr. Biol. , vol.9 , pp. 1231-1241
    • Devit, M.J.1    Johnston, M.2
  • 72
    • 2542476990 scopus 로고    scopus 로고
    • Arginine methylation of RNA helicase a determines its subcellular localization
    • W.A. Smith Arginine methylation of RNA helicase A determines its subcellular localization J. Biol. Chem. 279 2004 22795 22798
    • (2004) J. Biol. Chem. , vol.279 , pp. 22795-22798
    • Smith, W.A.1
  • 73
    • 0348134742 scopus 로고    scopus 로고
    • Mono- versus polyubiquitination: Differential control of p53 fate by Mdm2
    • M. Li Mono- versus polyubiquitination: differential control of p53 fate by Mdm2 Science 302 2003 1972 1975
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1
  • 74
    • 1642499415 scopus 로고    scopus 로고
    • Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs
    • M.T. Bohnsack Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs RNA 10 2004 185 191
    • (2004) RNA , vol.10 , pp. 185-191
    • Bohnsack, M.T.1
  • 75
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • M.E. Lindsay Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export J. Cell Biol. 153 2001 1391 1402
    • (2001) J. Cell Biol. , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1
  • 76
    • 0037047430 scopus 로고    scopus 로고
    • Npap60/Nup50 is a tri-stable switch that stimulates importin-α: β-mediated nuclear protein import
    • M.E. Lindsay Npap60/Nup50 is a tri-stable switch that stimulates importin-α:β-mediated nuclear protein import Cell 110 2002 349 360
    • (2002) Cell , vol.110 , pp. 349-360
    • Lindsay, M.E.1
  • 77
    • 0032849246 scopus 로고    scopus 로고
    • Kap104p-mediated nuclear import. Nuclear localization signals in mRNA-binding proteins and the role of Ran and RNA
    • D.C. Lee, and J.D. Aitchison Kap104p-mediated nuclear import. Nuclear localization signals in mRNA-binding proteins and the role of Ran and RNA J. Biol. Chem. 274 1999 29031 29037
    • (1999) J. Biol. Chem. , vol.274 , pp. 29031-29037
    • Lee, D.C.1    Aitchison, J.D.2
  • 78
    • 0032522343 scopus 로고    scopus 로고
    • Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p
    • B. Senger Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p EMBO J. 17 1998 2196 2207
    • (1998) EMBO J. , vol.17 , pp. 2196-2207
    • Senger, B.1
  • 79
    • 0033612576 scopus 로고    scopus 로고
    • Nuclear import of the TATA-binding protein: Mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting
    • L.F. Pemberton Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting J. Cell Biol. 145 1999 1407 1417
    • (1999) J. Cell Biol. , vol.145 , pp. 1407-1417
    • Pemberton, L.F.1
  • 80
    • 2342501365 scopus 로고    scopus 로고
    • Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization
    • J.M. Casolari Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization Cell 117 2004 427 439
    • (2004) Cell , vol.117 , pp. 427-439
    • Casolari, J.M.1
  • 81
    • 0037127047 scopus 로고    scopus 로고
    • Systems analysis of Ran transport
    • A.E. Smith Systems analysis of Ran transport Science 295 2002 488 491
    • (2002) Science , vol.295 , pp. 488-491
    • Smith, A.E.1
  • 82
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • H. Fried, and U. Kutay Nucleocytoplasmic transport: taking an inventory Cell. Mol. Life Sci. 60 2003 1659 1688
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 83
    • 0041312658 scopus 로고    scopus 로고
    • Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7
    • A. Fassati Nuclear import of HIV-1 intracellular reverse transcription complexes is mediated by importin 7 EMBO J. 22 2003 3675 3685
    • (2003) EMBO J. , vol.22 , pp. 3675-3685
    • Fassati, A.1
  • 84
    • 2342447986 scopus 로고    scopus 로고
    • Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor
    • N.D. Freedman, and K.R. Yamamoto Importin 7 and importin α/importin β are nuclear import receptors for the glucocorticoid receptor Mol. Biol. Cell 15 2004 2276 2286
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2276-2286
    • Freedman, N.D.1    Yamamoto, K.R.2
  • 85
    • 1542267816 scopus 로고    scopus 로고
    • Transportin2 functions as importin and mediates nuclear import of HuR
    • S. Guttinger Transportin2 functions as importin and mediates nuclear import of HuR Proc. Natl. Acad. Sci. U. S. A. 101 2004 2918 2923
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2918-2923
    • Guttinger, S.1
  • 86
    • 0034645038 scopus 로고    scopus 로고
    • Mechanism of metabolic control. Target of rapamycin signaling links nitrogen quality to the activity of the Rtg1 and Rtg3 transcription factors
    • A. Komeili Mechanism of metabolic control. Target of rapamycin signaling links nitrogen quality to the activity of the Rtg1 and Rtg3 transcription factors J. Cell Biol. 151 2000 863 878
    • (2000) J. Cell Biol. , vol.151 , pp. 863-878
    • Komeili, A.1
  • 87
    • 2442642835 scopus 로고    scopus 로고
    • Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13
    • J.E. Ploski Paired-type homeodomain transcription factors are imported into the nucleus by karyopherin 13 Mol. Cell. Biol. 24 2004 4824 4834
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4824-4834
    • Ploski, J.E.1
  • 88
    • 4644226779 scopus 로고    scopus 로고
    • Regulated nuclear accumulation of the yeast hsp70 Ssa4p in ethanol-stressed cells is mediated by the N-terminal domain, requires the nuclear carrier Nmd5p and protein kinase C
    • X. Quan Regulated nuclear accumulation of the yeast hsp70 Ssa4p in ethanol-stressed cells is mediated by the N-terminal domain, requires the nuclear carrier Nmd5p and protein kinase C FASEB J. 18 2004 899 901
    • (2004) FASEB J. , vol.18 , pp. 899-901
    • Quan, X.1
  • 89
    • 1642528962 scopus 로고    scopus 로고
    • Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR
    • A. Rebane Transportins 1 and 2 are redundant nuclear import factors for hnRNP A1 and HuR RNA 10 2004 590 599
    • (2004) RNA , vol.10 , pp. 590-599
    • Rebane, A.1
  • 90
    • 0242641546 scopus 로고    scopus 로고
    • Exportin 6: A novel nuclear export receptor that is specific for profilin-actin complexes
    • T. Stuven Exportin 6: a novel nuclear export receptor that is specific for profilin-actin complexes EMBO J. 22 2003 5928 5940
    • (2003) EMBO J. , vol.22 , pp. 5928-5940
    • Stuven, T.1
  • 91
    • 0347379904 scopus 로고    scopus 로고
    • Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae
    • R. Ueta Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae J. Biol. Chem. 278 2003 50120 50127
    • (2003) J. Biol. Chem. , vol.278 , pp. 50120-50127
    • Ueta, R.1


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