메뉴 건너뛰기




Volumn 16, Issue 2, 2006, Pages 237-244

Karyopherin flexibility in nucleocytoplasmic transport

Author keywords

[No Author keywords available]

Indexed keywords

EXPORTIN 1; EXPORTIN CSE1P; EXPORTIN LOS1; EXPORTIN XPO T; EXPORTIN XPO1P; ISOPROTEIN; KARYOPHERIN; KARYOPHERIN BETA; NUCLEAR PROTEIN; TRANSPORTIN; TRANSPORTIN M9; TRANSPORTIN RAN; UNCLASSIFIED DRUG;

EID: 33646482468     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2006.03.010     Document Type: Review
Times cited : (175)

References (26)
  • 1
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome. Nucleocytoplasmic transport throughout the cell cycle
    • Weis K. 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
    • 0346457106 scopus 로고    scopus 로고
    • Conformational variability of nucleo-cytoplasmic transport factors
    • This study uses SAXS to demonstrate considerable variability between different β-karyopherins and also between the same karyopherin bound to different partners.
    • Fukuhara N., Fernandez E., Ebert J., Conti E., and Svergun D. Conformational variability of nucleo-cytoplasmic transport factors. J Biol Chem 279 (2004) 2176-2181. This study uses SAXS to demonstrate considerable variability between different β-karyopherins and also between the same karyopherin bound to different partners.
    • (2004) J Biol Chem , vol.279 , pp. 2176-2181
    • Fukuhara, N.1    Fernandez, E.2    Ebert, J.3    Conti, E.4    Svergun, D.5
  • 4
    • 9744248734 scopus 로고    scopus 로고
    • Architecture of CRM1/exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex
    • A combination of X-ray crystallography, homology modelling and EM was employed to generate a structural model of human CRM1, the primary nuclear protein export factor. In contrast to other β-karyopherins, residues critical for the recognition of the leucine-rich NES are identified as being located on the outer convex surface of the molecule.
    • Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U., Soler-Lopez M., Baudin F., Mattaj I.W., and Müller C.W. Architecture of CRM1/exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell 16 (2004) 761-775. A combination of X-ray crystallography, homology modelling and EM was employed to generate a structural model of human CRM1, the primary nuclear protein export factor. In contrast to other β-karyopherins, residues critical for the recognition of the leucine-rich NES are identified as being located on the outer convex surface of the molecule.
    • (2004) Mol Cell , vol.16 , pp. 761-775
    • Petosa, C.1    Schoehn, G.2    Askjaer, P.3    Bauer, U.4    Moulin, M.5    Steuerwald, U.6    Soler-Lopez, M.7    Baudin, F.8    Mattaj, I.W.9    Müller, C.W.10
  • 5
    • 11144257756 scopus 로고    scopus 로고
    • Structural basis for the assembly of a nuclear export complex
    • The X-ray crystal structure of the Cse1p-RanGTP-Kap60p nuclear export complex shows the unusually large interaction interface between the three molecules. The paper proposes that the large energy of interaction may be balanced by mechanical distortion of Cse1p to generate a 'spring-loaded' molecule that can be easily disassembled following RanGTP hydrolysis in the cytoplasm.
    • Matsuura Y., and Stewart M. Structural basis for the assembly of a nuclear export complex. Nature 432 (2004) 872-877. The X-ray crystal structure of the Cse1p-RanGTP-Kap60p nuclear export complex shows the unusually large interaction interface between the three molecules. The paper proposes that the large energy of interaction may be balanced by mechanical distortion of Cse1p to generate a 'spring-loaded' molecule that can be easily disassembled following RanGTP hydrolysis in the cytoplasm.
    • (2004) Nature , vol.432 , pp. 872-877
    • Matsuura, Y.1    Stewart, M.2
  • 6
    • 20844458749 scopus 로고    scopus 로고
    • The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding
    • The X-ray crystal structure of Cse1p alone shows a 'closed' structure in which the N terminus binds to a region around HEAT repeat 15 near the centre of the molecule. As a result, there is a considerable alteration in the Cse1p helicoidal pitch compared with its 'open' structure in the Cse1p-RanGTP-Kap60p complex.
    • Cook A., Fernandez E., Lindner D., Ebert J., Schlenstedt G., and Conti E. The structure of the nuclear export receptor Cse1 in its cytosolic state reveals a closed conformation incompatible with cargo binding. Mol Cell 18 (2005) 355-367. The X-ray crystal structure of Cse1p alone shows a 'closed' structure in which the N terminus binds to a region around HEAT repeat 15 near the centre of the molecule. As a result, there is a considerable alteration in the Cse1p helicoidal pitch compared with its 'open' structure in the Cse1p-RanGTP-Kap60p complex.
    • (2005) Mol Cell , vol.18 , pp. 355-367
    • Cook, A.1    Fernandez, E.2    Lindner, D.3    Ebert, J.4    Schlenstedt, G.5    Conti, E.6
  • 7
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp
    • Chook Y.M., and Blobel G. Structure of the nuclear transport complex karyopherin-β2-Ran x GppNHp. Nature 399 (1999) 230-237
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 8
    • 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. 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    Muller, C.W.4
  • 9
    • 20444468112 scopus 로고    scopus 로고
    • Structural basis for nuclear import complex dissociation by RanGTP
    • The X-ray crystal structure of the yeast importin-β homologue, Kap95p, complexed with RanGTP shows how the pitch of the helicoid is increased due to an interaction between the Ran switch I loop and HEAT repeats 12-15 in the C-terminal arch. This change in helicoidal pitch is proposed to facilitate the release of the IBB domain when RanGTP binds in the nucleus.
    • Lee S.J., Matsuura Y., Liu S.M., and Stewart M. Structural basis for nuclear import complex dissociation by RanGTP. Nature 435 (2005) 693-696. The X-ray crystal structure of the yeast importin-β homologue, Kap95p, complexed with RanGTP shows how the pitch of the helicoid is increased due to an interaction between the Ran switch I loop and HEAT repeats 12-15 in the C-terminal arch. This change in helicoidal pitch is proposed to facilitate the release of the IBB domain when RanGTP binds in the nucleus.
    • (2005) Nature , vol.435 , pp. 693-696
    • Lee, S.J.1    Matsuura, Y.2    Liu, S.M.3    Stewart, M.4
  • 10
    • 19444383899 scopus 로고    scopus 로고
    • Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p
    • The X-ray crystal structure of Kap95p bound to the high-affinity site on nucleoporin Nup1p shows the basis of the increased strength of the interaction and indicates how such an interaction could accelerate import complex disassembly.
    • Liu S.M., and Stewart M. Structural basis for the high-affinity binding of nucleoporin Nup1p to the Saccharomyces cerevisiae importin-β homologue, Kap95p. J Mol Biol 349 (2005) 515-525. The X-ray crystal structure of Kap95p bound to the high-affinity site on nucleoporin Nup1p shows the basis of the increased strength of the interaction and indicates how such an interaction could accelerate import complex disassembly.
    • (2005) J Mol Biol , vol.349 , pp. 515-525
    • Liu, S.M.1    Stewart, M.2
  • 11
    • 0033612390 scopus 로고    scopus 로고
    • Structural view of the Ran-importin β interaction at 2.3 Å resolution
    • Vetter I.R., Arndt A., Kutay U., Görlich D., and Wittinghofer A. Structural view of the Ran-importin β interaction at 2.3 Å resolution. Cell 97 (1999) 635-646
    • (1999) Cell , vol.97 , pp. 635-646
    • Vetter, I.R.1    Arndt, A.2    Kutay, U.3    Görlich, D.4    Wittinghofer, A.5
  • 12
    • 0034616910 scopus 로고    scopus 로고
    • Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking
    • Bayliss R., Littlewood T., and Stewart M. Structural basis for the interaction between FxFG nucleoporin repeats and importin-β in nuclear trafficking. Cell 102 (2000) 99-108
    • (2000) Cell , vol.102 , pp. 99-108
    • Bayliss, R.1    Littlewood, T.2    Stewart, M.3
  • 13
    • 0037184968 scopus 로고    scopus 로고
    • GLFG and FxFG nucleoporins bind to overlapping sites on importin-β
    • Bayliss R., Littlewood T., Strawn L.A., Wente S.R., and Stewart M. GLFG and FxFG nucleoporins bind to overlapping sites on importin-β. J Biol Chem 277 (2002) 50597-50606
    • (2002) J Biol Chem , vol.277 , pp. 50597-50606
    • Bayliss, R.1    Littlewood, T.2    Strawn, L.A.3    Wente, S.R.4    Stewart, M.5
  • 14
    • 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. 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    Bednenko, J.2    Gillespie, M.T.3    Gerace, L.4
  • 15
    • 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. 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
  • 16
    • 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. Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-α. J Mol Biol 297 (2000) 1183-1194
    • (2000) J Mol Biol , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 17
    • 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
  • 18
    • 0041731883 scopus 로고    scopus 로고
    • Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport
    • Bednenko J., Cingolani G., and Gerace L. Importin β contains a COOH-terminal nucleoporin binding region important for nuclear transport. J Cell Biol 162 (2003) 391-401
    • (2003) J Cell Biol , vol.162 , pp. 391-401
    • Bednenko, J.1    Cingolani, G.2    Gerace, L.3
  • 20
    • 0037018838 scopus 로고    scopus 로고
    • Uncoupling Kapβ2 substrate dissociation from Ran binding
    • Chook Y.M., Jung A., Rosen M.K., and Blobel B. Uncoupling Kapβ2 substrate dissociation from Ran binding. Biochemistry 41 (2002) 6955-6966
    • (2002) Biochemistry , vol.41 , pp. 6955-6966
    • Chook, Y.M.1    Jung, A.2    Rosen, M.K.3    Blobel, B.4
  • 21
    • 0344827223 scopus 로고    scopus 로고
    • Molecular recognition in nuclear trafficking
    • Stewart M. Molecular recognition in nuclear trafficking. Science 302 (2003) 1513-1514
    • (2003) Science , vol.302 , pp. 1513-1514
    • Stewart, M.1
  • 22
    • 0030960586 scopus 로고    scopus 로고
    • Dominant negative mutants of importin-β block multiple pathways of import and export through the nuclear pore complex
    • Kutay U., Izaurralde E., Bischoff R.L., Mattaj I.W., and Görlich D. Dominant negative mutants of importin-β block multiple pathways of import and export through the nuclear pore complex. EMBO J 16 (1997) 1153-1163
    • (1997) EMBO J , vol.16 , pp. 1153-1163
    • Kutay, U.1    Izaurralde, E.2    Bischoff, R.L.3    Mattaj, I.W.4    Görlich, D.5
  • 23
    • 15244359121 scopus 로고    scopus 로고
    • Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy
    • Golas M.M., Sander B., Will C.L., Lührmann R., and Stark H. Major conformational change in the complex SF3b upon integration into the spliceosomal U11/U12 di-snRNP as revealed by electron cryomicroscopy. Mol Cell 17 (2005) 869-883
    • (2005) Mol Cell , vol.17 , pp. 869-883
    • Golas, M.M.1    Sander, B.2    Will, C.L.3    Lührmann, R.4    Stark, H.5
  • 24
  • 25
    • 0141995069 scopus 로고    scopus 로고
    • The nuclear pore complex: nucleocytoplasmic transport and beyond
    • Fahrenkrog B., and Aebi U. The nuclear pore complex: nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 4 (2003) 757-766
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 757-766
    • Fahrenkrog, B.1    Aebi, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.