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Volumn 23, Issue 20, 2003, Pages 7271-7284

Sec13 shuttles between the nucleus and the cytoplasm and stably interacts with Nup96 at the nuclear pore complex

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARTIC ACID; NUCLEOPORIN; PROTEIN NUP96; PROTEIN SEC13; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0141529759     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.20.7271-7284.2003     Document Type: Article
Times cited : (74)

References (56)
  • 1
    • 0029592161 scopus 로고
    • Nup120p: A yeast nucleoporin required for NPC distribution and mRNA transport
    • Aitchison, J. D., G. Blobel, and M. P. Rout. 1995. Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transport. J. Cell Biol. 131:1659-1675.
    • (1995) J. Cell Biol. , vol.131 , pp. 1659-1675
    • Aitchison, J.D.1    Blobel, G.2    Rout, M.P.3
  • 3
    • 0037154983 scopus 로고    scopus 로고
    • The contribution of nuclear compartmentalization to gene regulation
    • Carmo-Fonseca, M. 2002. The contribution of nuclear compartmentalization to gene regulation. Cell 108:513-521.
    • (2002) Cell , vol.108 , pp. 513-521
    • Carmo-Fonseca, M.1
  • 7
    • 0022458304 scopus 로고
    • Identification and characterisation of a nuclear pore complex protein
    • Davis, L. I., and G. Blobel. 1986. Identification and characterisation of a nuclear pore complex protein. Cell 45:699-709.
    • (1986) Cell , vol.45 , pp. 699-709
    • Davis, L.I.1    Blobel, G.2
  • 8
    • 0031038521 scopus 로고    scopus 로고
    • C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure
    • Dockendorff, T. C., C. V. Heath, A. L. Goldstein, C. A. Snay, and C. N. Cole. 1997. C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure. Mol. Cell. Biol. 17:906-920. (Erratum, Mol. Cell. Biol. 17:2347-2350.)
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 906-920
    • Dockendorff, T.C.1    Heath, C.V.2    Goldstein, A.L.3    Snay, C.A.4    Cole, C.N.5
  • 9
    • 0031038521 scopus 로고    scopus 로고
    • Erratum
    • Dockendorff, T. C., C. V. Heath, A. L. Goldstein, C. A. Snay, and C. N. Cole. 1997. C-terminal truncations of the yeast nucleoporin Nup145p produce a rapid temperature-conditional mRNA export defect and alterations to nuclear structure. Mol. Cell. Biol. 17:906-920. (Erratum, Mol. Cell. Biol. 17:2347-2350.)
    • Mol. Cell. Biol. , vol.17 , pp. 2347-2350
  • 10
    • 0000174510 scopus 로고    scopus 로고
    • Fluorescence photobleaching techniques
    • D. Spector, R. Goldman, and L. Leinwand (ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • Ellenberg, J., and J. Lippincott-Schwartz. 1997. Fluorescence photobleaching techniques, p. 79.1-79.23. In D. Spector, R. Goldman, and L. Leinwand (ed.), Cells: a laboratory manual, vol. 2. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y.
    • (1997) Cells: A Laboratory Manual , vol.2 , pp. 791-7923
    • Ellenberg, J.1    Lippincott-Schwartz, J.2
  • 11
    • 0031004754 scopus 로고    scopus 로고
    • Defining the essential functional regions of the nucleoporin Nup145p
    • Emtage, J., M. Bucci, J. Watkins, and S. Wente. 1997. Defining the essential functional regions of the nucleoporin Nup145p. J. Cell Sci. 110:911-925.
    • (1997) J. Cell Sci. , vol.110 , pp. 911-925
    • Emtage, J.1    Bucci, M.2    Watkins, J.3    Wente, S.4
  • 12
    • 0037154838 scopus 로고    scopus 로고
    • Role of nucleoporin induction in releasing an mRNA nuclear export block
    • Enninga, J., D. E. Levy, G. Blobel, and B. M. Fontoura. 2002. Role of nucleoporin induction in releasing an mRNA nuclear export block. Science 295:1523-1525.
    • (2002) Science , vol.295 , pp. 1523-1525
    • Enninga, J.1    Levy, D.E.2    Blobel, G.3    Fontoura, B.M.4
  • 13
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 14
  • 15
    • 0033594084 scopus 로고    scopus 로고
    • A conserved biogenesis pathway for nucleoporins: Proteolytic processing of a 186-kilodalton precursor generates nup98 and the novel nucleoporin, nup96
    • Fontoura, B. M., G. Blobel, and M. J. Matunis. 1999. A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates nup98 and the novel nucleoporin, nup96. J. Cell Biol. 144:1097-1112.
    • (1999) J. Cell Biol. , vol.144 , pp. 1097-1112
    • Fontoura, B.M.1    Blobel, G.2    Matunis, M.J.3
  • 16
    • 0034613189 scopus 로고    scopus 로고
    • The nucleoporin nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import
    • Fontoura, B. M., G. Blobel, and N. R. Yaseen. 2000. The nucleoporin nup98 is a site for GDP/GTP exchange on ran and termination of karyopherin beta 2-mediated nuclear import. J. Biol. Chem. 275:31289-31296.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31289-31296
    • Fontoura, B.M.1    Blobel, G.2    Yaseen, N.R.3
  • 17
    • 0035853099 scopus 로고    scopus 로고
    • The nucleoporin Nup98 associates with the intranucear filamentous protein network of TPR
    • Fontoura, B. M. A., S. Dales, G. Blobel, and H. Zhong. 2001. The nucleoporin Nup98 associates with the intranucear filamentous protein network of TPR. Proc. Natl. Acad. Sci. USA 98:3208-3213.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3208-3213
    • Fontoura, B.M.A.1    Dales, S.2    Blobel, G.3    Zhong, H.4
  • 18
  • 19
    • 0029982655 scopus 로고    scopus 로고
    • Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p
    • Goldstein, A. L., C. A. Snay, C. V. Heath, and C. N. Cole. 1996. Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p. Mol. Biol. Cell 7:917-934.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 917-934
    • Goldstein, A.L.1    Snay, C.A.2    Heath, C.V.3    Cole, C.N.4
  • 20
    • 0028786983 scopus 로고
    • Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex
    • Guan, T., S. Muller, G. Klier, N. Pante, J. M. Blevitt, M. Haner, B. Paschal, U. Aebi, and L. Gerace. 1995. Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex. Mol. Biol. Cell 6:1591-1603.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1591-1603
    • Guan, T.1    Muller, S.2    Klier, G.3    Pante, N.4    Blevitt, J.M.5    Haner, M.6    Paschal, B.7    Aebi, U.8    Gerace, L.9
  • 21
    • 0034493602 scopus 로고    scopus 로고
    • Dynamics of transitional endoplasmic reticulum sites in vertebrate cells
    • Hammond, A. T., and B. S. Glick. 2000. Dynamics of transitional endoplasmic reticulum sites in vertebrate cells. Mol. Biol. Cell 11:3013-3030.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3013-3030
    • Hammond, A.T.1    Glick, B.S.2
  • 23
    • 0036306726 scopus 로고    scopus 로고
    • The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly
    • Hetzer, M., O. J. Gruss, and I. W. Mattaj. 2002. The Ran GTPase as a marker of chromosome position in spindle formation and nuclear envelope assembly. Nat. Cell Biol. 4:E177-E184.
    • (2002) Nat. Cell Biol. , vol.4
    • Hetzer, M.1    Gruss, O.J.2    Mattaj, I.W.3
  • 24
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., J. Halladay, and E. A. Craig. 1996. Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144:1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 25
  • 26
    • 0032145891 scopus 로고    scopus 로고
    • Transport from the endoplasmic reticulum to the Golgi
    • Kaiser, C., and S. Ferro-Novick. 1998. Transport from the endoplasmic reticulum to the Golgi. Curr. Opin. Cell Biol. 10:477-482.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 477-482
    • Kaiser, C.1    Ferro-Novick, S.2
  • 27
    • 0027503111 scopus 로고
    • Purification and characterization of a nuclear pore glycoprotein complex containing p62
    • Kita, K., S. Omata, and T. Horigome. 1993. Purification and characterization of a nuclear pore glycoprotein complex containing p62. J. Biol. Chem. 113:377-382.
    • (1993) J. Biol. Chem. , vol.113 , pp. 377-382
    • Kita, K.1    Omata, S.2    Horigome, T.3
  • 28
    • 0034782753 scopus 로고    scopus 로고
    • Targeting of Ran: Variation on a common theme?
    • Kunzler, M., and E. Hurt. 2001. Targeting of Ran: variation on a common theme? J. Cell Sci. 114:3233-3241.
    • (2001) J. Cell Sci. , vol.114 , pp. 3233-3241
    • Kunzler, M.1    Hurt, E.2
  • 29
    • 0036469369 scopus 로고    scopus 로고
    • Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins
    • Lutzmann, M., R. Kunze, A. Buerer, U. Aebi, and E. Hurt. 2002. Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J. 21:387-397.
    • (2002) EMBO J. , vol.21 , pp. 387-397
    • Lutzmann, M.1    Kunze, R.2    Buerer, A.3    Aebi, U.4    Hurt, E.5
  • 30
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M. J., E. Coutavas, and G. Blobel. 1996. A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J. Cell Biol. 135:1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 32
    • 0034846391 scopus 로고    scopus 로고
    • The arrest of secretion response in yeast: Signaling from the secretory path to the nucleus by Wsc proteins and Pkc1p
    • Nanduri, J., and A. M. Tartakoff. 2001. The arrest of secretion response in yeast: signaling from the secretory path to the nucleus by Wsc proteins and Pkc1p. Mol. Cell 8:281-289.
    • (2001) Mol. Cell , vol.8 , pp. 281-289
    • Nanduri, J.1    Tartakoff, A.M.2
  • 33
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • Phair, R. D., and T. Misteli. 2000. High mobility of proteins in the mammalian cell nucleus. Nature 404:604-609.
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 34
    • 0033613132 scopus 로고    scopus 로고
    • Autoproteolysis in nucleoporin biogenesis
    • Rosenblum, J. S., and G. Blobel. 1999. Autoproteolysis in nucleoporin biogenesis. Proc. Natl. Acad. Sci. USA 96:11370-11375.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11370-11375
    • Rosenblum, J.S.1    Blobel, G.2
  • 35
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout, M. P., and J. D. Aitchison. 2001. The nuclear pore complex as a transport machine. J. Biol. Chem. 276:16593-16596.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 36
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • 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.
    • (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
  • 37
    • 2942578315 scopus 로고    scopus 로고
    • Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly
    • Ryan, K. J., and S. R. Wente. 2002. Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly. BMC Genet. 3:17.
    • (2002) BMC Genet. , vol.3 , pp. 17
    • Ryan, K.J.1    Wente, S.R.2
  • 38
    • 0034022647 scopus 로고    scopus 로고
    • The nuclear pore complex: A protein machine bridging the nucleus and cytoplasm
    • Ryan, K. J., and S. R. Wente. 2000. The nuclear pore complex: a protein machine bridging the nucleus and cytoplasm. Curr. Opin. Cell Biol. 12:361-371.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 361-371
    • Ryan, K.J.1    Wente, S.R.2
  • 39
  • 40
    • 0029906009 scopus 로고    scopus 로고
    • Analysis of the physical properties and molecular modeling of Sec13: A WD repeat protein involved in vesicular traffic
    • Saxena, K., C. Gaitatzes, M. T. Walsh, M. Eck, E. J. Neer, and T. F. Smith. 1996. Analysis of the physical properties and molecular modeling of Sec13: a WD repeat protein involved in vesicular traffic. Biochemistry 35:15215-15221.
    • (1996) Biochemistry , vol.35 , pp. 15215-15221
    • Saxena, K.1    Gaitatzes, C.2    Walsh, M.T.3    Eck, M.4    Neer, E.J.5    Smith, T.F.6
  • 41
    • 0030911425 scopus 로고    scopus 로고
    • Mex67p which is an essential factor for nuclear mRNA export binds to both poly(A)+ RNA and nuclear pores
    • Segref, A., K. Sharma, V. Doye, A. Hellwig, J. Huber, R. Luhrmann, and E. C. Hurt. 1997. Mex67p which is an essential factor for nuclear mRNA export binds to both poly(A)+ RNA and nuclear pores. EMBO J. 16:3256-3271.
    • (1997) EMBO J. , vol.16 , pp. 3256-3271
    • Segref, A.1    Sharma, K.2    Doye, V.3    Hellwig, A.4    Huber, J.5    Luhrmann, R.6    Hurt, E.C.7
  • 43
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou, S., C. Wimmer, M. Rieger, V. Doye, H. Tekotte, C. Weise, S. Emig, A. Segref, and E. C. Hurt. 1996. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84:265-275.
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6    Emig, S.7    Segref, A.8    Hurt, E.C.9
  • 44
  • 45
    • 0027458374 scopus 로고
    • A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm
    • Sukegawa, J., and G. Blobel. 1993. A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm. Cell 72:29-38.
    • (1993) Cell , vol.72 , pp. 29-38
    • Sukegawa, J.1    Blobel, G.2
  • 46
    • 0000505092 scopus 로고    scopus 로고
    • The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus
    • Tang, B. L., F. Peter, J. Krijnse-Locker, S. H. Low, G. Griffiths, and W. Hong. 1997. The mammalian homolog of yeast Sec13p is enriched in the intermediate compartment and is essential for protein transport from the endoplasmic reticulum to the Golgi apparatus. Mol. Cell. Biol. 17:256-266.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 256-266
    • Tang, B.L.1    Peter, F.2    Krijnse-Locker, J.3    Low, S.H.4    Griffiths, G.5    Hong, W.6
  • 47
    • 0030789735 scopus 로고    scopus 로고
    • Two functionally distinct domains generated by in vivo cleavage of Nup145p: A novel biogenesis pathway for nucleoporins
    • Teixeira, M. T., S. Siniossoglou, S. Podtelejnikov, J. C. Benichou, M. Mann, B. Dujon, E. Hurt, and E. Fabre. 1997. Two functionally distinct domains generated by in vivo cleavage of Nup145p: a novel biogenesis pathway for nucleoporins. EMBO J. 16:5086-5097.
    • (1997) EMBO J. , vol.16 , pp. 5086-5097
    • Teixeira, M.T.1    Siniossoglou, S.2    Podtelejnikov, S.3    Benichou, J.C.4    Mann, M.5    Dujon, B.6    Hurt, E.7    Fabre, E.8
  • 48
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • 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. 155:339-353.
    • (2001) J. Cell Biol. , vol.155 , pp. 339-353
    • Vasu, S.1    Shah, S.2    Orjalo, A.3    Park, M.4    Fischer, W.H.5    Forbes, D.J.6
  • 49
    • 0035370938 scopus 로고    scopus 로고
    • Nuclear pores and nuclear assembly
    • Vasu, S. K., and D. J. Forbes. 2001. Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13:363-375.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 363-375
    • Vasu, S.K.1    Forbes, D.J.2
  • 51
    • 84924192549 scopus 로고    scopus 로고
    • Maintenance of Golgi structure and function depends on the integrity of endoplasmic reticulum export
    • Ward, T. H., R. S. Polishchuck, S. Caplan, K. Hirschberg, and J. Lippincott-Schwartz. 2001. Maintenance of Golgi structure and function depends on the integrity of endoplasmic reticulum export. J. Cell Biol. 155:557-570.
    • (2001) J. Cell Biol. , vol.155 , pp. 557-570
    • Ward, T.H.1    Polishchuck, R.S.2    Caplan, S.3    Hirschberg, K.4    Lippincott-Schwartz, J.5
  • 52
    • 0036966365 scopus 로고    scopus 로고
    • Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not
    • Wiesmeijer, K., C. Molenaar, I. M. Bekeer, H. J. Tanke, and R. W. Dirks. 2002. Mobile foci of Sp100 do not contain PML: PML bodies are immobile but PML and Sp100 proteins are not. J. Struct. Biol. 140:180-188.
    • (2002) J. Struct. Biol. , vol.140 , pp. 180-188
    • Wiesmeijer, K.1    Molenaar, C.2    Bekeer, I.M.3    Tanke, H.J.4    Dirks, R.W.5
  • 53
    • 0035853083 scopus 로고    scopus 로고
    • Disruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and function
    • Wu, X., L. H. Kasper, R. T. Mantcheva, G. T. Mantchev, M. J. Springett, and J. M. van Deursen. 2001. Disruption of the FG nucleoporin NUP98 causes selective changes in nuclear pore complex stoichiometry and function. Proc. Natl. Acad. Sci. USA 98:3191-3196.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3191-3196
    • Wu, X.1    Kasper, L.H.2    Mantcheva, R.T.3    Mantchev, G.T.4    Springett, M.J.5    Van Deursen, J.M.6
  • 54
    • 0030984329 scopus 로고    scopus 로고
    • Cloning and characterization of human karyopherin beta3
    • Yaseen, N. R., and G. Blobel. 1997. Cloning and characterization of human karyopherin beta3. Proc. Natl. Acad. Sci. USA 94:4451-4456.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4451-4456
    • Yaseen, N.R.1    Blobel, G.2
  • 55
    • 0033543574 scopus 로고    scopus 로고
    • GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358
    • 274
    • Yaseen, N. R., and G. Blobel. 274. GTP hydrolysis links initiation and termination of nuclear import on the nucleoporin nup358. J. Biol. Chem. 274:26493-26502.
    • J. Biol. Chem. , vol.274 , pp. 26493-26502
    • Yaseen, N.R.1    Blobel, G.2


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