메뉴 건너뛰기




Volumn 189, Issue 7, 2010, Pages 1129-1142

The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOPORIN; NUP188 PROTEIN; NUP205; NUP93 PROTEIN; UNCLASSIFIED DRUG;

EID: 77954388089     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.200912045     Document Type: Article
Times cited : (105)

References (52)
  • 2
    • 11344290169 scopus 로고    scopus 로고
    • The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation
    • DOI 10.1016/j.molcel.2004.12.010, PII S1097276504007658
    • Antonin, W., C. Franz, U. Haselmann, C. Antony, and I.W. Mattaj. 2005. The integral membrane nucleoporin pom121 functionally links nuclear pore complex assembly and nuclear envelope formation. Mol. Cell. 17:83-92. doi:10.1016/j.molcel.2004.12.010 (Pubitemid 40075367)
    • (2005) Molecular Cell , vol.17 , Issue.1 , pp. 83-92
    • Antonin, W.1    Franz, C.2    Haselmann, U.3    Antony, C.4    Mattaj, I.W.5
  • 3
    • 44449138334 scopus 로고    scopus 로고
    • Nuclear pore complex assembly through the cell cycle: Regulation and membrane organization
    • doi:10.1016/j.febslet.2008.02.067
    • Antonin, W., J. Ellenberg, and E. Dultz. 2008. Nuclear pore complex assembly through the cell cycle: regulation and membrane organization. FEBS Lett. 582:2004-2016. doi:10.1016/j.febslet.2008.02.067
    • (2008) FEBS Lett. , vol.582 , pp. 2004-2016
    • Antonin, W.1    Ellenberg, J.2    Dultz, E.3
  • 4
    • 34548590272 scopus 로고    scopus 로고
    • NSF- And SNARE-mediated membrane fusion is required for nuclear envelope formation and completion of nuclear pore complex assembly in Xenopus laevis egg extracts
    • DOI 10.1242/jcs.010181
    • Baur, T., K. Ramadan, A. Schlundt, J. Kartenbeck, and H.H. Meyer. 2007. NSFand SNARE-mediated membrane fusion is required for nuclear envelope formation and completion of nuclear pore complex assembly in Xenopus laevis egg extracts. J. Cell Sci. 120:2895-2903. doi:10.1242/jcs.010181 (Pubitemid 47394263)
    • (2007) Journal of Cell Science , vol.120 , Issue.16 , pp. 2895-2903
    • Baur, T.1    Ramadan, K.2    Schlundt, A.3    Kartenbeck, J.4    Meyer, H.H.5
  • 5
    • 34948891095 scopus 로고    scopus 로고
    • Snapshots of nuclear pore complexes in action captured by cryo-electron tomography
    • doi:10.1038/nature06170
    • Beck, M., V. Lucić, F. Förster, W. Baumeister, and O. Medalia. 2007. Snapshots of nuclear pore complexes in action captured by cryo-electron tomography. Nature. 449:611-615. doi:10.1038/nature06170
    • (2007) Nature , vol.449 , pp. 611-615
    • Beck, M.1    Lucić, V.2    Förster, F.3    Baumeister, W.4    Medalia, O.5
  • 6
    • 0025236701 scopus 로고
    • Replication of purified DNA in Xenopus egg extract is dependent on nuclear assembly
    • Blow, J.J., and A.M. Sleeman. 1990. Replication of purified DNA in Xenopus egg extract is dependent on nuclear assembly. J. Cell Sci. 95:383-391.
    • (1990) J. Cell Sci. , vol.95 , pp. 383-391
    • Blow, J.J.1    Sleeman, A.M.2
  • 7
    • 0037417808 scopus 로고    scopus 로고
    • Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex
    • doi:10.1073/pnas.252749899
    • Boehmer, T., J. Enninga, S. Dales, G. Blobel, and H. Zhong. 2003. Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex. Proc. Natl. Acad. Sci. USA. 100:981-985. doi:10.1073/pnas.252749899
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 981-985
    • Boehmer, T.1    Enninga, J.2    Dales, S.3    Blobel, G.4    Zhong, H.5
  • 8
    • 57149118232 scopus 로고    scopus 로고
    • Structural evidence for common ancestry of the nuclear pore complex and vesicle coats
    • doi:10.1126/science.1165886
    • Brohawn, S.G., N.C. Leksa, E.D. Spear, K.R. Rajashankar, and T.U. Schwartz. 2008. Structural evidence for common ancestry of the nuclear pore complex and vesicle coats. Science. 322:1369-1373. doi:10.1126/science.1165886
    • (2008) Science , vol.322 , pp. 1369-1373
    • Brohawn, S.G.1    Leksa, N.C.2    Spear, E.D.3    Rajashankar, K.R.4    Schwartz, T.U.5
  • 9
    • 34548627531 scopus 로고    scopus 로고
    • Structural biology of nucleocytoplasmic transport
    • doi:10.1146/ annurev.biochem.76.052705.161529
    • Cook, A., F. Bono, M. Jinek, and E. Conti. 2007. Structural biology of nucleocytoplasmic transport. Annu. Rev. Biochem. 76:647-671. doi:10.1146/ annurev.biochem.76.052705.161529
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 647-671
    • Cook, A.1    Bono, F.2    Jinek, M.3    Conti, E.4
  • 10
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • doi:10.1016/ j.tcb.2008.07.009
    • D'Angelo, M.A., and M.W. Hetzer. 2008. Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol. 18:456-466. doi:10.1016/ j.tcb.2008.07.009
    • (2008) Trends Cell Biol. , vol.18 , pp. 456-466
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 11
    • 33645962474 scopus 로고    scopus 로고
    • Nuclear pores form de novo from both sides of the nuclear envelope
    • doi:10.1126/science.1124196
    • D'Angelo, M.A., D.J. Anderson, E. Richard, and M.W. Hetzer. 2006. Nuclear pores form de novo from both sides of the nuclear envelope. Science. 312:440-443. doi:10.1126/science.1124196
    • (2006) Science , vol.312 , pp. 440-443
    • D'Angelo, M.A.1    Anderson, D.J.2    Richard, E.3    Hetzer, M.W.4
  • 12
    • 33750349837 scopus 로고    scopus 로고
    • Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase
    • doi:10.1038/nature05170
    • Deng, M., and M. Hochstrasser. 2006. Spatially regulated ubiquitin ligation by an ER/nuclear membrane ligase. Nature. 443:827-831. doi:10.1038/nature05170
    • (2006) Nature , vol.443 , pp. 827-831
    • Deng, M.1    Hochstrasser, M.2
  • 13
    • 0032933745 scopus 로고    scopus 로고
    • Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
    • doi:10.1016/S0960-9822(99)80044-X
    • Englmeier, L., J.C. Olivo, and I.W. Mattaj. 1999. Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr. Biol. 9:30-41. doi:10.1016/S0960- 9822(99)80044-X
    • (1999) Curr. Biol. , vol.9 , pp. 30-41
    • Englmeier, L.1    Olivo, J.C.2    Mattaj, I.W.3
  • 14
    • 0031453253 scopus 로고    scopus 로고
    • Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking
    • doi:10.1146/annurev.genet.31.1.277
    • Fabre, E., and E. Hurt. 1997. Yeast genetics to dissect the nuclear pore complex and nucleocytoplasmic trafficking. Annu. Rev. Genet. 31:277-313. doi:10.1146/annurev.genet.31.1.277
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 277-313
    • Fabre, E.1    Hurt, E.2
  • 15
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • DOI 10.1016/S0092-8674(00)80371-2
    • Fornerod, M., M. Ohno, M. Yoshida, and I.W. Mattaj. 1997. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 90:1051-1060. doi:10.1016/S0092-8674(00)80371-2 (Pubitemid 27408519)
    • (1997) Cell , vol.90 , Issue.6 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 16
    • 27144544970 scopus 로고    scopus 로고
    • Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates
    • DOI 10.1038/sj.emboj.7600825, PII 7600825
    • Franz, C., P. Askjaer, W. Antonin, C.L. Iglesias, U. Haselmann, M. Schelder, A. de Marco, M. Wilm, C. Antony, and I.W. Mattaj. 2005. Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates. EMBO J. 24:3519-3531. doi:10.1038/sj.emboj.7600825 (Pubitemid 41509360)
    • (2005) EMBO Journal , vol.24 , Issue.20 , pp. 3519-3531
    • Franz, C.1    Askjaer, P.2    Antonin, W.3    Iglesias, C.L.4    Haselmann, U.5    Schelder, M.6    De Marco, A.7    Wilm, M.8    Antony, C.9    Mattaj, I.W.10
  • 17
    • 33947270331 scopus 로고    scopus 로고
    • MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly
    • doi:10.1038/sj.embor.7400889
    • Franz, C., R. Walczak, S. Yavuz, R. Santarella, M. Gentzel, P. Askjaer, V. Galy, M. Hetzer, I.W. Mattaj, and W. Antonin. 2007. MEL-28/ELYS is required for the recruitment of nucleoporins to chromatin and postmitotic nuclear pore complex assembly. EMBO Rep. 8:165-172. doi:10.1038/sj.embor.7400889
    • (2007) EMBO Rep. , vol.8 , pp. 165-172
    • Franz, C.1    Walczak, R.2    Yavuz, S.3    Santarella, R.4    Gentzel, M.5    Askjaer, P.6    Galy, V.7    Hetzer, M.8    Mattaj, I.W.9    Antonin, W.10
  • 18
    • 0344875469 scopus 로고    scopus 로고
    • Caenorhabditis elegans Nucleoporins Nup93 and Nup205 Determine the Limit of Nuclear Pore Complex Size Exclusion in Vivo
    • DOI 10.1091/mbc.E03-04-0237
    • Galy, V., I.W. Mattaj, and P. Askjaer. 2003. Caenorhabditis elegans nucleoporins Nup93 and Nup205 determine the limit of nuclear pore complex size exclusion in vivo. Mol. Biol. Cell. 14:5104-5115. doi:10.1091/mbc.E03-04-0237 (Pubitemid 37484824)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.12 , pp. 5104-5115
    • Galy, V.1    Mattaj, I.W.2    Askjaer, P.3
  • 19
    • 0034514672 scopus 로고    scopus 로고
    • Yeast nuclear pore complex assembly defects determined by nuclear envelope reconstruction
    • DOI 10.1006/jsbi.2000.4305
    • Gomez-Ospina, N., G. Morgan, T.H. Giddings Jr., B. Kosova, E. Hurt, and M. Winey. 2000. Yeast nuclear pore complex assembly defects determined by nuclear envelope reconstruction. J. Struct. Biol. 132:1-5. doi:10.1006/jsbi. 2000.4305 (Pubitemid 32095232)
    • (2000) Journal of Structural Biology , vol.132 , Issue.1 , pp. 1-5
    • Gomez-Ospina, N.1    Morgan, G.2    Giddings Jr., T.H.3    Kosova, B.4    Hurt, E.5    Winey, M.6
  • 20
    • 0030824317 scopus 로고    scopus 로고
    • Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly
    • Grandi, P., T. Dang, N. Pané, A. Shevchenko, M. Mann, D. Forbes, and E. Hurt. 1997. Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205-kDa protein and is required for correct nuclear pore assembly. Mol. Biol. Cell. 8:2017-2038. (Pubitemid 27451118)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.10 , pp. 2017-2038
    • Grandi, P.1    Dang, T.2    Pane, N.3    Shevchenko, A.4    Mann, M.5    Forbes, D.6    Hurt, E.7
  • 21
    • 0037547118 scopus 로고    scopus 로고
    • Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores
    • DOI 10.1016/S1097-2765(03)00116-3
    • Harel, A., A.V. Orjalo, T. Vincent, A. Lachish-Zalait, S. Vasu, S. Shah, E. Zimmerman, M. Elbaum, and D.J. Forbes. 2003. Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores. Mol. Cell. 11:853-864. doi:10.1016/S1097-2765(03)00116-3 (Pubitemid 36566309)
    • (2003) Molecular Cell , vol.11 , Issue.4 , pp. 853-864
    • Harel, A.1    Orjalo, A.V.2    Vincent, T.3    Lachish-Zalait, A.4    Vasu, S.5    Shah, S.6    Zimmerman, E.7    Elbaum, M.8    Forbes, D.J.9
  • 22
    • 44949151696 scopus 로고    scopus 로고
    • Nup53 is required for nuclear envelope and nuclear pore complex assembly
    • doi:10.1091/mbc.E07-08-0820
    • Hawryluk-Gara, L.A., M. Platani, R. Santarella, R.W. Wozniak, and I.W. Mattaj. 2008. Nup53 is required for nuclear envelope and nuclear pore complex assembly. Mol. Biol. Cell. 19:1753-1762. doi:10.1091/mbc.E07-08-0820
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 1753-1762
    • Hawryluk-Gara, L.A.1    Platani, M.2    Santarella, R.3    Wozniak, R.W.4    Mattaj, I.W.5
  • 23
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function, and dynamics of the nuclear periphery
    • doi:10.1146/annurev.cellbio.21.090704.151152
    • Hetzer, M.W., T.C. Walther, and I.W. Mattaj. 2005. Pushing the envelope: structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21:347-380. doi:10.1146/annurev.cellbio.21.090704.151152
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 347-380
    • Hetzer, M.W.1    Walther, T.C.2    Mattaj, I.W.3
  • 24
    • 0037340827 scopus 로고    scopus 로고
    • Nuclear pore complexes exceeding eightfold rotational symmetry
    • doi:10.1016/S1047-8477(02)00626-3
    • Hinshaw, J.E., and R.A. Milligan. 2003. Nuclear pore complexes exceeding eightfold rotational symmetry. J. Struct. Biol. 141:259-268. doi:10.1016/S1047-8477(02)00626-3
    • (2003) J. Struct. Biol. , vol.141 , pp. 259-268
    • Hinshaw, J.E.1    Milligan, R.A.2
  • 25
    • 33748310680 scopus 로고    scopus 로고
    • Karyopherin-mediated import of integral inner nuclear membrane proteins
    • doi:10.1038/nature05075
    • King, M.C., C.P. Lusk, and G. Blobel. 2006. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature. 442:1003-1007. doi:10.1038/nature05075
    • (2006) Nature , vol.442 , pp. 1003-1007
    • King, M.C.1    Lusk, C.P.2    Blobel, G.3
  • 26
    • 35748981206 scopus 로고    scopus 로고
    • A pathway separate from the central channel through the nuclear pore complex for inorganic ions and small macromolecules
    • doi:10.1074/jbc.M703720200
    • Kramer, A., Y. Ludwig, V. Shahin, and H. Oberleithner. 2007. A pathway separate from the central channel through the nuclear pore complex for inorganic ions and small macromolecules. J. Biol. Chem. 282:31437-31443. doi:10.1074/jbc.M703720200
    • (2007) J. Biol. Chem. , vol.282 , pp. 31437-31443
    • Kramer, A.1    Ludwig, Y.2    Shahin, V.3    Oberleithner, H.4
  • 27
    • 34247364639 scopus 로고    scopus 로고
    • Highway to the inner nuclear membrane: Rules for the road
    • doi:10.1038/nrm2165
    • Lusk, C.P., G. Blobel, and M.C. King. 2007. Highway to the inner nuclear membrane: rules for the road. Nat. Rev. Mol. Cell Biol. 8:414-420. doi:10.1038/nrm2165
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 414-420
    • Lusk, C.P.1    Blobel, G.2    King, M.C.3
  • 28
    • 65649114446 scopus 로고    scopus 로고
    • The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly
    • doi:10.1083/jcb.200810029
    • Makio, T., L.H. Stanton, C.C. Lin, D.S. Goldfarb, K. Weis, and R.W. Wozniak. 2009. The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly. J. Cell Biol. 185:459-473. doi:10.1083/jcb.200810029
    • (2009) J. Cell Biol. , vol.185 , pp. 459-473
    • Makio, T.1    Stanton, L.H.2    Lin, C.C.3    Goldfarb, D.S.4    Weis, K.5    Wozniak, R.W.6
  • 30
    • 0345871035 scopus 로고    scopus 로고
    • Sorting out the nuclear envelope from the endoplasmic reticulum
    • doi:10.1038/nrm1263
    • Mattaj, I.W. 2004. Sorting out the nuclear envelope from the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 5:65-69. doi:10.1038/nrm1263
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 65-69
    • Mattaj, I.W.1
  • 31
    • 0029011832 scopus 로고
    • Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation
    • doi:10.1083/jcb.129.6.1459
    • Meier, E., B.R. Miller, and D.J. Forbes. 1995. Nuclear pore complex assembly studied with a biochemical assay for annulate lamellae formation. J. Cell Biol. 129:1459-1472. doi:10.1083/jcb.129.6.1459
    • (1995) J. Cell Biol. , vol.129 , pp. 1459-1472
    • Meier, E.1    Miller, B.R.2    Forbes, D.J.3
  • 32
    • 68749090845 scopus 로고    scopus 로고
    • Herpesvirus assembly: An update
    • doi:10.1016/j.virusres.2009.03.018
    • Mettenleiter, T.C., B.G. Klupp, and H. Granzow. 2009. Herpesvirus assembly: an update. Virus Res. 143:222-234. doi:10.1016/j.virusres.2009.03.018
    • (2009) Virus Res. , vol.143 , pp. 222-234
    • Mettenleiter, T.C.1    Klupp, B.G.2    Granzow, H.3
  • 33
    • 69849093363 scopus 로고    scopus 로고
    • Characterisation of the passive permeability barrier of nuclear pore complexes
    • doi:10.1038/emboj.2009.200
    • Mohr, D., S. Frey, T. Fischer, T. Güttler, and D. Görlich. 2009. Characterisation of the passive permeability barrier of nuclear pore complexes. EMBO J. 28:2541-2553. doi:10.1038/emboj.2009.200
    • (2009) EMBO J. , vol.28 , pp. 2541-2553
    • Mohr, D.1    Frey, S.2    Fischer, T.3    Güttler, T.4    Görlich, D.5
  • 34
    • 33947522224 scopus 로고    scopus 로고
    • Passive and facilitated transport in nuclear pore complexes is largely uncoupled
    • doi:10.1074/jbc.M608329200
    • Naim, B., V. Brumfeld, R. Kapon, V. Kiss, R. Nevo, and Z. Reich. 2007. Passive and facilitated transport in nuclear pore complexes is largely uncoupled. J. Biol. Chem. 282:3881-3888. doi:10.1074/jbc.M608329200
    • (2007) J. Biol. Chem. , vol.282 , pp. 3881-3888
    • Naim, B.1    Brumfeld, V.2    Kapon, R.3    Kiss, V.4    Nevo, R.5    Reich, Z.6
  • 35
    • 0029894532 scopus 로고    scopus 로고
    • The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex
    • doi:10.1083/jcb.133.6.1153
    • Nehrbass, U., M.P. Rout, S. Maguire, G. Blobel, and R.W. Wozniak. 1996. The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. J. Cell Biol. 133:1153-1162. doi:10.1083/jcb.133.6.1153
    • (1996) J. Cell Biol. , vol.133 , pp. 1153-1162
    • Nehrbass, U.1    Rout, M.P.2    Maguire, S.3    Blobel, G.4    Wozniak, R.W.5
  • 36
    • 0035312838 scopus 로고    scopus 로고
    • Enhancement of translation by the epsilon element is independent of the sequence of the 460 region of 16S rRNA
    • doi:10.1093/nar/29.7.1420
    • O'Connor, M., and A.E. Dahlberg. 2001. Enhancement of translation by the epsilon element is independent of the sequence of the 460 region of 16S rRNA. Nucleic Acids Res. 29:1420-1425. doi:10.1093/nar/29.7.1420
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1420-1425
    • O'Connor, M.1    Dahlberg, A.E.2
  • 37
    • 11244316478 scopus 로고    scopus 로고
    • Energy- And temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • doi:10.1083/jcb.200409149
    • Ohba, T., E.C. Schirmer, T. Nishimoto, and L. Gerace. 2004. Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore. J. Cell Biol. 167:1051-1062. doi:10.1083/jcb. 200409149
    • (2004) J. Cell Biol. , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 38
    • 34250885134 scopus 로고    scopus 로고
    • Phosphomimetic mutation of the mitotically phosphorylated serine 1880 compromises the interaction of the transmembrane nucleoporin gp210 with the nuclear pore complex
    • doi:10.1016/j.yexcr.2007.05.011
    • Onischenko, E.A., E. Crafoord, and E. Hallberg. 2007. Phosphomimetic mutation of the mitotically phosphorylated serine 1880 compromises the interaction of the transmembrane nucleoporin gp210 with the nuclear pore complex. Exp. Cell Res. 313:2744-2751. doi:10.1016/j.yexcr.2007.05.011
    • (2007) Exp. Cell Res. , vol.313 , pp. 2744-2751
    • Onischenko, E.A.1    Crafoord, E.2    Hallberg, E.3
  • 39
    • 0025666495 scopus 로고
    • Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: In vivo evidence for the interaction of p55 with the nuclear lamina
    • doi:10.1083/jcb.111.6.2225
    • Powell, L., and B. Burke. 1990. Internuclear exchange of an inner nuclear membrane protein (p55) in heterokaryons: in vivo evidence for the interaction of p55 with the nuclear lamina. J. Cell Biol. 111:2225-2234. doi:10.1083/jcb.111.6.2225
    • (1990) J. Cell Biol. , vol.111 , pp. 2225-2234
    • Powell, L.1    Burke, B.2
  • 40
    • 33845227470 scopus 로고    scopus 로고
    • ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division
    • doi:10.1073/pnas.0608484103
    • Rasala, B.A., A.V. Orjalo, Z. Shen, S. Briggs, and D.J. Forbes. 2006. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Proc. Natl. Acad. Sci. USA. 103:17801-17806. doi:10.1073/pnas.0608484103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17801-17806
    • Rasala, B.A.1    Orjalo, A.V.2    Shen, Z.3    Briggs, S.4    Forbes, D.J.5
  • 41
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • DOI 10.1093/emboj/20.6.1320
    • Ribbeck, K., and D. Görlich. 2001. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20:1320-1330. doi:10.1093/emboj/20.6. 1320 (Pubitemid 32233972)
    • (2001) EMBO Journal , vol.20 , Issue.6 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 42
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of mistic, a membrane-integrating protein for membrane protein expression
    • DOI 10.1126/science.1106392
    • Roosild, T.P., J. Greenwald, M. Vega, S. Castronovo, R. Riek, and S. Choe. 2005. NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science. 307:1317-1321. doi:10.1126/science.1106392 (Pubitemid 40299982)
    • (2005) Science , vol.307 , Issue.5713 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 43
    • 0035907248 scopus 로고    scopus 로고
    • The Nuclear Pore Complex as a Transport Machine
    • DOI 10.1074/jbc.R100015200
    • Rout, M.P., and J.D. Aitchison. 2001. The nuclear pore complex as a transport machine. J. Biol. Chem. 276:16593-16596. doi:10.1074/jbc.R100015200 (Pubitemid 37411446)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.20 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 44
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • doi:10.1083/jcb.148.4.635
    • Rout, M.P., J.D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B.T. Chait. 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635-651. doi:10.1083/jcb.148.4.635
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 45
    • 0034729194 scopus 로고    scopus 로고
    • Yeast nucleoporins involved in passive nuclear envelope permeability
    • DOI 10.1083/jcb.149.5.1027
    • Shulga, N., N. Mosammaparast, R. Wozniak, and D.S. Goldfarb. 2000. Yeast nucleoporins involved in passive nuclear envelope permeability. J. Cell Biol. 149:1027-1038. doi:10.1083/jcb.149.5.1027 (Pubitemid 30354253)
    • (2000) Journal of Cell Biology , vol.149 , Issue.5 , pp. 1027-1038
    • Shulga, N.1    Mosammaparast, N.2    Wozniak, R.3    Goldfarb, D.S.4
  • 46
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • doi:10.1083/jcb.130.1.15
    • Soullam, B., and H.J. Worman. 1995. Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol. 130:15-27. doi:10.1083/jcb.130.1.15
    • (1995) J. Cell Biol. , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 47
    • 33645978219 scopus 로고    scopus 로고
    • Direct membrane protein-DNA interactions required early in nuclear envelope assembly
    • DOI 10.1083/jcb.200512078
    • Ulbert, S., M. Platani, S. Boue, and I.W. Mattaj. 2006. Direct membrane protein- DNA interactions required early in nuclear envelope assembly. J. Cell Biol. 173:469-476. doi:10.1083/jcb.200512078 (Pubitemid 43765194)
    • (2006) Journal of Cell Biology , vol.173 , Issue.4 , pp. 469-476
    • Ulbert, S.1    Platani, M.2    Boue, S.3    Mattaj, I.W.4
  • 48
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • doi:10.1083/jcb.200108007
    • Vasu, S., S. Shah, A. Orjalo, M. Park, W.H. Fischer, and D.J. Forbes. 2001. Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J. Cell Biol. 155:339-354. doi:10.1083/jcb.200108007
    • (2001) J. Cell Biol. , vol.155 , pp. 339-354
    • Vasu, S.1    Shah, S.2    Orjalo, A.3    Park, M.4    Fischer, W.H.5    Forbes, D.J.6
  • 50
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • DOI 10.1016/S0092-8674(03)00082-5
    • Weis, K. 2003. Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell. 112:441-451. doi:10.1016/S0092- 8674(03)00082-5 (Pubitemid 36263078)
    • (2003) Cell , vol.112 , Issue.4 , pp. 441-451
    • Weis, K.1
  • 51
    • 0029900425 scopus 로고    scopus 로고
    • Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p
    • DOI 10.1083/jcb.133.6.1141
    • Zabel, U., V. Doye, H. Tekotte, R. Wepf, P. Grandi, and E.C. Hurt. 1996. Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J. Cell Biol. 133:1141-1152. doi:10.1083/jcb.133.6. 1141 (Pubitemid 26192319)
    • (1996) Journal of Cell Biology , vol.133 , Issue.6 , pp. 1141-1152
    • Zabel, U.1    Doye, V.2    Tekotte, H.3    Wepf, R.4    Grandi, P.5    Hurt, E.C.6
  • 52
    • 59149091333 scopus 로고    scopus 로고
    • Inner nuclear membrane protein transport is mediated by multiple mechanisms
    • doi:10.1042/BST0361373
    • Zuleger, N., N. Korfali, and E.C. Schirmer. 2008. Inner nuclear membrane protein transport is mediated by multiple mechanisms. Biochem. Soc. Trans. 36:1373-1377. doi:10.1042/BST0361373
    • (2008) Biochem. Soc. Trans. , vol.36 , pp. 1373-1377
    • Zuleger, N.1    Korfali, N.2    Schirmer, E.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.