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Volumn 193, Issue 1, 2011, Pages 109-123

System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; EMERIN; GLYCINE; NUCLEOPORIN; NUCLEOPORIN 35; PHENYLALANINE; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 79955502505     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201009068     Document Type: Article
Times cited : (88)

References (62)
  • 2
    • 34547229757 scopus 로고    scopus 로고
    • Early sorting of inner nuclear membrane proteins is conserved
    • doi:10.1073/pnas.0703186104
    • Braunagel, S.C., S.T. Williamson, Q. Ding, X. Wu, and M.D. Summers. 2007. Early sorting of inner nuclear membrane proteins is conserved. Proc. Natl. Acad. Sci. USA. 104:9307-9312. doi:10.1073/pnas.0703186104
    • (2007) Proc. Natl. Acad. Sci. USA. , vol.104 , pp. 9307-9312
    • Braunagel, S.C.1    Williamson, S.T.2    Ding, Q.3    Wu, X.4    Summers, M.D.5
  • 3
    • 0000125636 scopus 로고
    • An electron microscope study of the nuclear membrane
    • doi:10.1038/163280a0
    • Callan, H.G., J.T. Randall, and S.G. Tomlin. 1949. An electron microscope study of the nuclear membrane. Nature. 163:280. doi:10.1038/163280a0
    • (1949) Nature , vol.163 , pp. 280
    • Callan, H.G.1    Randall, J.T.2    Tomlin, S.G.3
  • 7
    • 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
  • 8
    • 0029975651 scopus 로고    scopus 로고
    • The thermolability of nuclear protein import in tsBN2 cells is suppressed by microinjected Ran-GTP or Ran-GDP, but not by RanQ69L or RanT24N
    • Dickmanns, A., F.R. Bischoff, C. Marshallsay, R. Lührmann, H. Ponstingl, and E. Fanning. 1996. The thermolability of nuclear protein import in tsBN2 cells is suppressed by microinjected Ran-GTP or Ran-GDP, but not by RanQ69L or RanT24N. J. Cell Sci. 109:1449-1457.
    • (1996) J. Cell Sci. , vol.109 , pp. 1449-1457
    • Dickmanns, A.1    Bischoff, F.R.2    Marshallsay, C.3    Lührmann, R.4    Ponstingl, H.5    Fanning, E.6
  • 9
    • 0030763228 scopus 로고    scopus 로고
    • Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis
    • doi:10.1083/jcb.138.6.1193
    • Ellenberg, J., E.D. Siggia, J.E. Moreira, C.L. Smith, J.F. Presley, H.J. Worman, and J. Lippincott-Schwartz. 1997. Nuclear membrane dynamics and reassembly in living cells: targeting of an inner nuclear membrane protein in interphase and mitosis. J. Cell Biol. 138:1193-1206. doi:10.1083/jcb.138.6.1193
    • (1997) J. Cell Biol. , vol.138 , pp. 1193-1206
    • Ellenberg, J.1    Siggia, E.D.2    Moreira, J.E.3    Smith, C.L.4    Presley, J.F.5    Worman, H.J.6    Lippincott-Schwartz, J.7
  • 10
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • doi:10. 1016/0092-8674(93)90355-T
    • Foisner, R., and L. Gerace. 1993. Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell. 73:1267-1279. doi:10.1016/0092-8674(93)90355-T
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 11
    • 0022516246 scopus 로고
    • Synthetic peptides as nuclear localization signals
    • doi:10.1038/322641a0
    • Goldfarb, D.S., J. Gariépy, G. Schoolnik, and R.D. Kornberg. 1986. Synthetic peptides as nuclear localization signals. Nature. 322:641-644. doi:10.1038/322641a0
    • (1986) Nature , vol.322 , pp. 641-644
    • Goldfarb, D.S.1    Gariépy, J.2    Schoolnik, G.3    Kornberg, R.D.4
  • 12
    • 15444374750 scopus 로고    scopus 로고
    • The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein
    • doi:10.1083/jcb.200411026
    • Goodchild, R.E., and W.T. Dauer. 2005. The AAA+ protein torsinA interacts with a conserved domain present in LAP1 and a novel ER protein. J. Cell Biol. 168:855-862. doi:10.1083/jcb.200411026
    • (2005) J. Cell Biol. , vol.168 , pp. 855-862
    • Goodchild, R.E.1    Dauer, W.T.2
  • 14
    • 18244401885 scopus 로고    scopus 로고
    • Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex
    • doi:10.1091/mbc.E04-10-0857
    • Hawryluk-Gara, L.A., E.K. Shibuya, and R.W. Wozniak. 2005. Vertebrate Nup53 interacts with the nuclear lamina and is required for the assembly of a Nup93-containing complex. Mol. Biol. Cell. 16:2382-2394. doi:10.1091/mbc.E04-10-0857
    • (2005) Mol. Biol. Cell. , vol.16 , pp. 2382-2394
    • Hawryluk-Gara, L.A.1    Shibuya, E.K.2    Wozniak, R.W.3
  • 15
    • 0026776959 scopus 로고
    • Architecture and design of the nuclear pore complex
    • doi:10. 1016/0092-8674(92)90635-P
    • Hinshaw, J.E., B.O. Carragher, and R.A. Milligan. 1992. Architecture and design of the nuclear pore complex. Cell. 69:1133-1141. doi:10.1016/0092-8674(92)90635-P
    • (1992) Cell , vol.69 , pp. 1133-1141
    • Hinshaw, J.E.1    Carragher, B.O.2    Milligan, R.A.3
  • 16
    • 2942533937 scopus 로고    scopus 로고
    • Sun2 is a novel mammalian inner nuclear membrane protein
    • doi:10.1074/jbc.M313157200
    • Hodzic, D.M., D.B. Yeater, L. Bengtsson, H. Otto, and P.D. Stahl. 2004. Sun2 is a novel mammalian inner nuclear membrane protein. J. Biol. Chem. 279:25805-25812. doi:10.1074/jbc.M313157200
    • (2004) J. Biol. Chem. , vol.279 , pp. 25805-25812
    • Hodzic, D.M.1    Yeater, D.B.2    Bengtsson, L.3    Otto, H.4    Stahl, P.D.5
  • 17
    • 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
  • 18
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes
    • doi:10.1006/jmbi.2000.4315
    • Krogh, A., B. Larsson, G. von Heijne, and E.L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580. doi:10.1006/jmbi.2000.4315
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 20
    • 33847367253 scopus 로고    scopus 로고
    • Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta
    • doi:10.1242/jcs.03355
    • Ma, Y., S. Cai, Q. Lv, Q. Jiang, Q. Zhang, Z. Sodmergen, Z. Zhai, and C. Zhang. 2007. Lamin B receptor plays a role in stimulating nuclear envelope production and targeting membrane vesicles to chromatin during nuclear envelope assembly through direct interaction with importin beta. J. Cell Sci. 120:520-530. doi:10.1242/jcs.03355
    • (2007) J. Cell Sci. , vol.120 , pp. 520-530
    • Ma, Y.1    Cai, S.2    Lv, Q.3    Jiang, Q.4    Zhang, Q.5    Sodmergen, Z.6    Zhai, Z.7    Zhang, C.8
  • 23
    • 0032576573 scopus 로고    scopus 로고
    • Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p
    • doi:10.1083/jcb.143.7.1813
    • Marelli, M., J.D. Aitchison, and R.W. Wozniak. 1998. Specific binding of the karyopherin Kap121p to a subunit of the nuclear pore complex containing Nup53p, Nup59p, and Nup170p. J. Cell Biol. 143:1813-1830. doi:10.1083/jcb.143.7.1813
    • (1998) J. Cell Biol. , vol.143 , pp. 1813-1830
    • Marelli, M.1    Aitchison, J.D.2    Wozniak, R.W.3
  • 24
    • 0028949732 scopus 로고
    • cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane
    • doi:10.1074/jbc.270.15.8822
    • Martin, L., C. Crimaudo, and L. Gerace. 1995. cDNA cloning and characterization of lamina-associated polypeptide 1C (LAP1C), an integral protein of the inner nuclear membrane. J. Biol. Chem. 270:8822-8828. doi:10.1074/jbc.270.15.8822
    • (1995) J. Biol. Chem. , vol.270 , pp. 8822-8828
    • Martin, L.1    Crimaudo, C.2    Gerace, L.3
  • 25
    • 0242383489 scopus 로고    scopus 로고
    • Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery
    • doi:10.1007/s00018-003-3038-3
    • Mattout-Drubezki, A., and Y. Gruenbaum. 2003. Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery. Cell. Mol. Life Sci. 60:2053-2063. doi:10.1007/s00018-003-3038-3
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2053-2063
    • Mattout-Drubezki, A.1    Gruenbaum, Y.2
  • 26
    • 10744224439 scopus 로고    scopus 로고
    • Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria
    • doi:10. 1016/S0092-8674(03)00926-7
    • Mootha, V.K., J. Bunkenborg, J.V. Olsen, M. Hjerrild, J.R. Wisniewski, E. Stahl, M.S. Bolouri, H.N. Ray, S. Sihag, M. Kamal, et al. 2003. Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria. Cell. 115:629-640. doi:10.1016/S0092-8674(03)00926-7
    • (2003) Cell , vol.115 , pp. 629-640
    • Mootha, V.K.1    Bunkenborg, J.2    Olsen, J.V.3    Hjerrild, M.4    Wisniewski, J.R.5    Stahl, E.6    Bolouri, M.S.7    Ray, H.N.8    Sihag, S.9    Kamal, M.10
  • 28
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization
    • doi:10. 1016/S0968-0004(98)01336-X
    • Nakai, K., and P. Horton. 1999. PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem. Sci. 24:34-36. doi:10.1016/S0968-0004(98)01336-X
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-36
    • Nakai, K.1    Horton, P.2
  • 29
    • 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
  • 30
  • 31
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • doi:10.1126/science.1074952
    • Patterson, G.H., and J. Lippincott-Schwartz. 2002. A photoactivatable GFP for selective photolabeling of proteins and cells. Science. 297:1873-1877. doi:10.1126/science.1074952
    • (2002) Science , vol.297 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 32
    • 0035654399 scopus 로고    scopus 로고
    • Kinetic modelling approaches to in vivo imaging
    • doi:10.1038/35103000
    • Phair, R.D., and T. Misteli. 2001. Kinetic modelling approaches to in vivo imaging. Nat. Rev. Mol. Cell Biol. 2:898-907. doi:10.1038/35103000
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 898-907
    • Phair, R.D.1    Misteli, T.2
  • 33
    • 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
  • 34
    • 30844455364 scopus 로고    scopus 로고
    • The nuclear envelope: form and reformation
    • doi:10.1016/j.ceb.2005.12.004
    • Prunuske, A.J., and K.S. Ullman. 2006. The nuclear envelope: form and reformation. Curr. Opin. Cell Biol. 18:108-116. doi:10.1016/j.ceb.2005.12.004
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 108-116
    • Prunuske, A.J.1    Ullman, K.S.2
  • 35
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • doi:10.1083/jcb.110.4.883
    • Reichelt, R., A. Holzenburg, E.L. Buhle Jr., M. Jarnik, A. Engel, and U. Aebi. 1990. Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110:883-894. doi:10.1083/jcb.110.4.883
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle Jr., E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 36
    • 0028834428 scopus 로고
    • Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins
    • doi:10. 1016/0092-8674(95)90181-7
    • Rexach, M., and G. Blobel. 1995. Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell. 83:683-692. doi:10.1016/0092-8674(95)90181-7
    • (1995) Cell , vol.83 , pp. 683-692
    • Rexach, M.1    Blobel, G.2
  • 37
    • 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
    • (2001) EMBO J , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Görlich, D.2
  • 38
    • 0034201441 scopus 로고    scopus 로고
    • EMBOSS: the European Molecular Biology Open Software Suite
    • doi:10. 1016/S0168-9525(00)02024-2
    • Rice, P., I. Longden, and A. Bleasby. 2000. EMBOSS: the European Molecular Biology Open Software Suite. Trends Genet. 16:276-277. doi:10.1016/S0168-9525(00)02024-2
    • (2000) Trends Genet , vol.16 , pp. 276-277
    • Rice, P.1    Longden, I.2    Bleasby, A.3
  • 39
    • 0033549555 scopus 로고    scopus 로고
    • A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein
    • Rolls, M.M., P.A. Stein, S.S. Taylor, E. Ha, F. McKeon, and T.A. Rapoport. 1999. A visual screen of a GFP-fusion library identifies a new type of nuclear envelope membrane protein. J. Cell Biol. 146:29-44.
    • (1999) J. Cell Biol. , vol.146 , pp. 29-44
    • Rolls, M.M.1    Stein, P.A.2    Taylor, S.S.3    Ha, E.4    McKeon, F.5    Rapoport, T.A.6
  • 41
    • 4344645948 scopus 로고    scopus 로고
    • Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of proteins destined for the inner nuclear membrane
    • doi:10.1073/pnas.0404934101
    • Saksena, S., Y. Shao, S.C. Braunagel, M.D. Summers, and A.E. Johnson. 2004. Cotranslational integration and initial sorting at the endoplasmic reticulum translocon of proteins destined for the inner nuclear membrane. Proc. Natl. Acad. Sci. USA. 101:12537-12542. doi:10.1073/pnas.0404934101
    • (2004) Proc. Natl. Acad. Sci. USA. , vol.101 , pp. 12537-12542
    • Saksena, S.1    Shao, Y.2    Braunagel, S.C.3    Summers, M.D.4    Johnson, A.E.5
  • 42
    • 33744915536 scopus 로고    scopus 로고
    • Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope
    • doi:10.1038/nsmb1098
    • Saksena, S., M.D. Summers, J.K. Burks, A.E. Johnson, and S.C. Braunagel. 2006. Importin-alpha-16 is a translocon-associated protein involved in sorting membrane proteins to the nuclear envelope. Nat. Struct. Mol. Biol. 13:500-508. doi:10.1038/nsmb1098
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 500-508
    • Saksena, S.1    Summers, M.D.2    Burks, J.K.3    Johnson, A.E.4    Braunagel, S.C.5
  • 43
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • doi:10.1083/jcb.200702026
    • Salpingidou, G., A. Smertenko, I. Hausmanowa-Petrucewicz, P.J. Hussey, and C.J. Hutchison. 2007. A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J. Cell Biol. 178:897-904. doi:10.1083/jcb.200702026
    • (2007) J. Cell Biol. , vol.178 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.J.4    Hutchison, C.J.5
  • 44
    • 24144448719 scopus 로고    scopus 로고
    • Effects of organelle shape on fluorescence recovery after photobleaching
    • doi:10.1529/biophysj.104.057885
    • Sbalzarini, I.F., A. Mezzacasa, A. Helenius, and P. Koumoutsakos. 2005. Effects of organelle shape on fluorescence recovery after photobleaching. Biophys. J. 89:1482-1492. doi:10.1529/biophysj.104.057885
    • (2005) Biophys. J. , vol.89 , pp. 1482-1492
    • Sbalzarini, I.F.1    Mezzacasa, A.2    Helenius, A.3    Koumoutsakos, P.4
  • 45
    • 33646179555 scopus 로고    scopus 로고
    • Simulations of (an)isotropic diffusion on curved biological surfaces
    • doi:10.1529/biophysj.105.073809
    • Sbalzarini, I.F., A. Hayer, A. Helenius, and P. Koumoutsakos. 2006. Simulations of (an)isotropic diffusion on curved biological surfaces. Biophys. J. 90:878-885. doi:10.1529/biophysj.105.073809
    • (2006) Biophys. J. , vol.90 , pp. 878-885
    • Sbalzarini, I.F.1    Hayer, A.2    Helenius, A.3    Koumoutsakos, P.4
  • 46
    • 34249668426 scopus 로고    scopus 로고
    • Proteins that associate with lamins: many faces, many functions
    • doi:10.1016/j.yexcr.2007.03.012
    • Schirmer, E.C., and R. Foisner. 2007. Proteins that associate with lamins: many faces, many functions. Exp. Cell Res. 313:2167-2179. doi:10.1016/j.yexcr.2007.03.012
    • (2007) Exp. Cell Res. , vol.313 , pp. 2167-2179
    • Schirmer, E.C.1    Foisner, R.2
  • 47
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • doi:10.1126/science.1088176
    • Schirmer, E.C., L. Florens, T. Guan, J.R. Yates III, and L. Gerace. 2003. Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science. 301:1380-1382. doi:10.1126/science.1088176
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates III, J.R.4    Gerace, L.5
  • 48
    • 0024263203 scopus 로고
    • Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina
    • doi:10.1083/jcb.107.6.2029
    • Senior, A., and L. Gerace. 1988. Integral membrane proteins specific to the inner nuclear membrane and associated with the nuclear lamina. J. Cell Biol. 107:2029-2036. doi:10.1083/jcb.107.6.2029
    • (1988) J. Cell Biol. , vol.107 , pp. 2029-2036
    • Senior, A.1    Gerace, L.2
  • 49
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells
    • doi:10.1016/j.jsb.2003.11.013
    • Shimi, T., T. Koujin, M. Segura-Totten, K.L. Wilson, T. Haraguchi, and Y. Hiraoka. 2004. Dynamic interaction between BAF and emerin revealed by FRAP, FLIP, and FRET analyses in living HeLa cells. J. Struct. Biol. 147:31-41. doi:10.1016/j.jsb.2003.11.013
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Haraguchi, T.5    Hiraoka, Y.6
  • 50
    • 33646061361 scopus 로고    scopus 로고
    • HURP is a Ranimportin beta-regulated protein that stabilizes kinetochore microtubules in the vicinity of chromosomes
    • doi:10.1016/j.cub.2006.02.070
    • Silljé, H.H., S. Nagel, R. Körner, and E.A. Nigg. 2006. HURP is a Ranimportin beta-regulated protein that stabilizes kinetochore microtubules in the vicinity of chromosomes. Curr. Biol. 16:731-742. doi:10.1016/j.cub.2006.02.070
    • (2006) Curr. Biol. , vol.16 , pp. 731-742
    • Silljé, H.H.1    Nagel, S.2    Körner, R.3    Nigg, E.A.4
  • 51
    • 0027940369 scopus 로고
    • Colocalization of vertebrate lamin B and lamin B receptor (LBR) in nuclear envelopes and in LBR-induced membrane stacks of the yeast Saccharomyces cerevisiae
    • doi:10.1073/pnas.91.21.10124
    • Smith, S., and G. Blobel. 1994. Colocalization of vertebrate lamin B and lamin B receptor (LBR) in nuclear envelopes and in LBR-induced membrane stacks of the yeast Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 91:10124-10128. doi:10.1073/pnas.91.21.10124
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 10124-10128
    • Smith, S.1    Blobel, G.2
  • 52
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • doi:10.1083/jcb.120.5.1093
    • Soullam, B., and H.J. Worman. 1993. The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J. Cell Biol. 120:1093-1100. doi:10.1083/jcb.120.5.1093
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 53
    • 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
  • 55
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: nuclear pore complex structure, assembly, and function
    • doi:10. 1016/S1534-5807(03)00162-X
    • Suntharalingam, M., and S.R. Wente. 2003. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell. 4:775-789. doi:10.1016/S1534-5807(03)00162-X
    • (2003) Dev. Cell. , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 56
    • 77954388089 scopus 로고    scopus 로고
    • The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex
    • doi:10.1083/jcb.200912045
    • Theerthagiri, G., N. Eisenhardt, H. Schwarz, and W. Antonin. 2010. The nucleoporin Nup188 controls passage of membrane proteins across the nuclear pore complex. J. Cell Biol. 189:1129-1142. doi:10.1083/jcb.200912045
    • (2010) J. Cell Biol. , vol.189 , pp. 1129-1142
    • Theerthagiri, G.1    Eisenhardt, N.2    Schwarz, H.3    Antonin, W.4
  • 57
    • 77954886484 scopus 로고    scopus 로고
    • A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane
    • doi:10.1038/emboj.2010.119
    • Turgay, Y., R. Ungricht, A. Rothballer, A. Kiss, G. Csucs, P. Horvath, and U. Kutay. 2010. A classical NLS and the SUN domain contribute to the targeting of SUN2 to the inner nuclear membrane. EMBO J. 29:2262-2275. doi:10.1038/emboj.2010.119
    • (2010) EMBO J , vol.29 , pp. 2262-2275
    • Turgay, Y.1    Ungricht, R.2    Rothballer, A.3    Kiss, A.4    Csucs, G.5    Horvath, P.6    Kutay, U.7
  • 58
    • 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
    • (2006) J. Cell Biol. , vol.173 , pp. 469-476
    • Ulbert, S.1    Platani, M.2    Boue, S.3    Mattaj, I.W.4
  • 59
    • 2342451968 scopus 로고
    • A lamin B receptor in the nuclear envelope
    • doi:10.1073/pnas.85.22.8531
    • Worman, H.J., J. Yuan, G. Blobel, and S.D. Georgatos. 1988. A lamin B receptor in the nuclear envelope. Proc. Natl. Acad. Sci. USA. 85:8531-8534. doi:10.1073/pnas.85.22.8531
    • (1988) Proc. Natl. Acad. Sci. USA. , vol.85 , pp. 8531-8534
    • Worman, H.J.1    Yuan, J.2    Blobel, G.3    Georgatos, S.D.4
  • 60
    • 0036538599 scopus 로고    scopus 로고
    • Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane
    • Wu, W., F. Lin, and H.J. Worman. 2002. Intracellular trafficking of MAN1, an integral protein of the nuclear envelope inner membrane. J. Cell Sci. 115:1361-1371.
    • (2002) J. Cell Sci. , vol.115 , pp. 1361-1371
    • Wu, W.1    Lin, F.2    Worman, H.J.3
  • 61
    • 0022803355 scopus 로고
    • A domain of SV40 capsid polypeptide VP1 that specifies migration into the cell nucleus
    • Wychowski, C., D. Benichou, and M. Girard. 1986. A domain of SV40 capsid polypeptide VP1 that specifies migration into the cell nucleus. EMBO J. 5:2569-2576.
    • (1986) EMBO J , vol.5 , pp. 2569-2576
    • Wychowski, C.1    Benichou, D.2    Girard, M.3
  • 62
    • 17544383469 scopus 로고    scopus 로고
    • Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
    • doi:10.1074/jbc.271.25.14653
    • Ye, Q., and H.J. Worman. 1996. Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J. Biol. Chem. 271:14653-14656. doi:10.1074/jbc.271.25.14653
    • (1996) J. Biol. Chem. , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2


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