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Volumn 22, Issue 6, 2011, Pages 880-891

Nuclear import of an intact preassembled proteasome particle

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; HISTONE H3; HOLOENZYME; NUCLEOPORIN; PROTEASOME; RAN PROTEIN;

EID: 79952836890     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E10-07-0595     Document Type: Article
Times cited : (29)

References (81)
  • 1
    • 32044461117 scopus 로고    scopus 로고
    • Subcellular distribution of components of the ubiquitin-proteasome system in non-diseased human and rat brain
    • DOI 10.1369/jhc.5B6752.2005
    • Adori C, Low P, Moszkovkin G, Bagdy G, Laszlo L, Kovacs GG (2006). Subcellular distribution of components of the ubiquitin-proteasome system in nondiseased human and rat brain. J Histochem Cytochem 54, 263-267. (Pubitemid 43201647)
    • (2006) Journal of Histochemistry and Cytochemistry , vol.54 , Issue.2 , pp. 263-267
    • Adori, C.1    Low, P.2    Moszkovkin, G.3    Bagdy, G.4    Laszlo, L.5    Kovacs, G.G.6
  • 3
    • 0031170858 scopus 로고    scopus 로고
    • Visualization of prosomes (MCP-proteasomes), intermediate filament and actin networks by "instantaneous fixation" preserving the cytoskeleton
    • Arcangeletti C, Sutterlin R, Aebi U, De Conto F, Missorini S, Chezzi C, Scherrer K (1997). Visualization of prosomes (MCP-proteasomes), intermediate filament and actin networks by "instantaneous fixation" preserving the cytoskeleton. J Struct Biol 119, 35-58.
    • (1997) J Struct Biol , vol.119 , pp. 35-58
    • Arcangeletti, C.1    Sutterlin, R.2    Aebi, U.3    De Conto, F.4    Missorini, S.5    Chezzi, C.6    Scherrer, K.7
  • 4
    • 0038686574 scopus 로고    scopus 로고
    • Proteasome disassembly and downregulation is correlated with viability during stationary phase
    • DOI 10.1016/S0960-9822(03)00417-2
    • Bajorek M, Finley D, Glickman MH (2003). Proteasome disassembly and downregulation is correlated with viability during stationary phase. Curr Biol 13, 1140-1144. (Pubitemid 36815263)
    • (2003) Current Biology , vol.13 , Issue.13 , pp. 1140-1144
    • Bajorek, M.1    Finley, D.2    Glickman, M.H.3
  • 6
    • 60849118366 scopus 로고    scopus 로고
    • Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2
    • Effantin G, Rosenzweig R, Glickman MH, Steven AC (2009). Electron microscopic evidence in support of alpha-solenoid models of proteasomal subunits Rpn1 and Rpn2. J Mol Biol 386, 1204-1211.
    • (2009) J Mol Biol , vol.386 , pp. 1204-1211
    • Effantin, G.1    Rosenzweig, R.2    Glickman, M.H.3    Steven, A.C.4
  • 7
    • 0032510103 scopus 로고    scopus 로고
    • Nuclear localization signal-independent and importin/karyopherin- independent nuclear import of beta-catenin
    • Fagotto F, Gluck U, Gumbiner BM (1998). Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of beta-catenin. Curr Biol 8, 181-190. (Pubitemid 28126609)
    • (1998) Current Biology , vol.8 , Issue.4 , pp. 181-190
    • Fagotto, F.1    Gluck, U.2    Gumbiner, B.M.3
  • 8
    • 1842813943 scopus 로고    scopus 로고
    • The nuclear pore complex: A jack of all trades?
    • Fahrenkrog B, Koser J, Aebi U (2004). The nuclear pore complex: a jack of all trades? Trends Biochem Sci 29, 175-182.
    • (2004) Trends Biochem Sci , vol.29 , pp. 175-182
    • Fahrenkrog, B.1    Koser, J.2    Aebi, U.3
  • 9
    • 0025162266 scopus 로고
    • Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored
    • Finlay DR, Forbes DJ (1990). Reconstitution of biochemically altered nuclear pores: transport can be eliminated and restored. Cell 60, 17-29.
    • (1990) Cell , vol.60 , pp. 17-29
    • Finlay, D.R.1    Forbes, D.J.2
  • 10
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D (2009). Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78, 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 11
    • 0020619710 scopus 로고
    • Spontaneous formation of nucleus-like structures around bacteriophage DNA microinjected into Xenopus eggs
    • Forbes DJ, Kirschner MW, Newport JW (1983). Spontaneous formation of nucleus-like structures around bacteriophage DNA microinjected into Xenopus eggs. Cell 34, 13-23.
    • (1983) Cell , vol.34 , pp. 13-23
    • Forbes, D.J.1    Kirschner, M.W.2    Newport, J.W.3
  • 12
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • DOI 10.1007/s00018-003-3070-3
    • Fried H, Kutay U (2003). Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci 60, 1659-1688. (Pubitemid 37041364)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.8 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 13
    • 67349089027 scopus 로고    scopus 로고
    • Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base
    • Funakoshi M, Tomko RJ Jr, Kobayashi H, Hochstrasser M (2009). Multiple assembly chaperones govern biogenesis of the proteasome regulatory particle base. Cell 137, 887-899.
    • (2009) Cell , vol.137 , pp. 887-899
    • Funakoshi, M.1    Tomko Jr., R.J.2    Kobayashi, H.3    Hochstrasser, M.4
  • 14
    • 18244396127 scopus 로고    scopus 로고
    • Subcellular redistribution of components of the ubiquitin-proteasome pathway during lens differentiation and maturation
    • DOI 10.1167/iovs.04-0563
    • Girao H, Pereira P, Taylor A, Shang F (2005). Subcellular redistribution of components of the ubiquitin-proteasome pathway during lens differentiation and maturation. Invest Ophthalmol Visual Sci 46, 1386-1392. (Pubitemid 41685880)
    • (2005) Investigative Ophthalmology and Visual Science , vol.46 , Issue.4 , pp. 1386-1392
    • Girao, H.1    Pereira, P.2    Taylor, A.3    Shang, F.4
  • 15
    • 43149097612 scopus 로고    scopus 로고
    • Purification and characterization of proteasomes from Saccharomyces cerevisiae
    • 21.5.1-25.5.17
    • Glickman M, Coux O (2001). Purification and characterization of proteasomes from Saccharomyces cerevisiae. Curr Protoc Protein Sci 21.5.1-25.5.17.
    • (2001) Curr Protoc Protein Sci
    • Glickman, M.1    Coux, O.2
  • 16
    • 0034515298 scopus 로고    scopus 로고
    • Getting in and out of the proteasome
    • Glickman MH (2000). Getting in and out of the proteasome. Semin Cell Dev Biol 11, 149-158.
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 149-158
    • Glickman, M.H.1
  • 17
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A (2002). The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82, 373-428.
    • (2002) Physiol Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 18
    • 0031815994 scopus 로고    scopus 로고
    • The regulatory particle of the Saccharomyces cerevisiae proteasome
    • Glickman MH, Rubin DM, Fried VA, Finley D (1998). The regulatory particle of the Saccharomyces cerevisiae proteasome. Mol Cell Biol 18, 3149-3162.
    • (1998) Mol Cell Biol , vol.18 , pp. 3149-3162
    • Glickman, M.H.1    Rubin, D.M.2    Fried, V.A.3    Finley, D.4
  • 20
    • 0036092459 scopus 로고    scopus 로고
    • The intracellular localization of the proteasome
    • Gordon C (2002). The intracellular localization of the proteasome. Curr Top Microbiol Immunol 268, 175-184.
    • (2002) Curr Top Microbiol Immunol , vol.268 , pp. 175-184
    • Gordon, C.1
  • 21
    • 0029853631 scopus 로고    scopus 로고
    • Identification of different roles for RanGDP and RanGTP in nuclear protein import
    • Gorlich D, Pante N, Kutay U, Aebi U, Bischoff FR (1996). Identification of different roles for RanGDP and RanGTP in nuclear protein import. EMBO J 15, 5584-5594. (Pubitemid 26385618)
    • (1996) EMBO Journal , vol.15 , Issue.20 , pp. 5584-5594
    • Gorlich, D.1    Pante, N.2    Kutay, U.3    Aebi, U.4    Bischoff, F.R.5
  • 22
  • 23
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • DOI 10.1016/j.molcel.2004.10.026, PII S1097276504006471
    • Harel A, Forbes DJ (2004). Importin beta: conducting a much larger cellular symphony. Mol Cell 16, 319-330. (Pubitemid 39504787)
    • (2004) Molecular Cell , vol.16 , Issue.3 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 25
    • 0036747385 scopus 로고    scopus 로고
    • The ins and outs of APC and beta-catenin nuclear transport
    • DOI 10.1093/embo-reports/kvf181
    • Henderson BR, Fagotto F (2002). The ins and outs of APC and beta-catenin nuclear transport. EMBO Rep 3, 834-839. (Pubitemid 35154107)
    • (2002) EMBO Reports , vol.3 , Issue.9 , pp. 834-839
    • Henderson, B.R.1    Fagotto, F.2
  • 28
    • 71549126814 scopus 로고    scopus 로고
    • Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes
    • Hetzer MW, Wente SR (2009). Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. Dev Cell 17, 606-616.
    • (2009) Dev Cell , vol.17 , pp. 606-616
    • Hetzer, M.W.1    Wente, S.R.2
  • 29
    • 0026344571 scopus 로고
    • Cell cycle control of higher-order chromatin assembly around naked DNA in vitro
    • Hirano T, Mitchison TJ (1991). Cell cycle control of higher-order chromatin assembly around naked DNA in vitro. J Cell Biol 115, 1479-1489. (Pubitemid 21909990)
    • (1991) Journal of Cell Biology , vol.115 , Issue.6 , pp. 1479-1489
    • Hirano, T.1    Mitchison, T.J.2
  • 30
    • 0037017403 scopus 로고    scopus 로고
    • The importin-beta binding domain of snurportin1 is responsible for the Ran- And energy-independent nuclear import of spliceosomal U snRNPs in vitro
    • DOI 10.1083/jcb.200108114
    • Huber J, Dickmanns A, Luhrmann R (2002). The importin-beta binding domain of snurportin1 is responsible for the Ran- and energy-independent nuclear import of spliceosomal U snRNPs in vitro. J Cell Biol 156, 467-479. (Pubitemid 34839895)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 467-479
    • Huber, J.1    Dickmanns, A.2    Luhrmann, R.3
  • 33
    • 0037147328 scopus 로고    scopus 로고
    • What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome
    • Kajava AV (2002). What curves alpha-solenoids? Evidence for an alpha-helical toroid structure of Rpn1 and Rpn2 proteins of the 26 S proteasome. J Biol Chem 277, 49791-49798.
    • (2002) J Biol Chem , vol.277 , pp. 49791-49798
    • Kajava, A.V.1
  • 34
    • 65849109465 scopus 로고    scopus 로고
    • Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones
    • Kaneko T, Hamazaki J, Iemura S, Sasaki K, Furuyama K, Natsume T, Tanaka K, Murata S (2009). Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones. Cell 137, 914-925.
    • (2009) Cell , vol.137 , pp. 914-925
    • Kaneko, T.1    Hamazaki, J.2    Iemura, S.3    Sasaki, K.4    Furuyama, K.5    Natsume, T.6    Tanaka, K.7    Murata, S.8
  • 35
    • 0029004815 scopus 로고
    • A 20S complex containing CDC27 and CDC16 catalyzes the mitosisspecific conjugation of ubiquitin to cyclin B
    • King RW, Peters JM, Tugendreich S, Rolfe M, Hieter P, Kirschner MW (1995). A 20S complex containing CDC27 and CDC16 catalyzes the mitosisspecific conjugation of ubiquitin to cyclin B. Cell 81, 279-288.
    • (1995) Cell , vol.81 , pp. 279-288
    • King, R.W.1    Peters, J.M.2    Tugendreich, S.3    Rolfe, M.4    Hieter, P.5    Kirschner, M.W.6
  • 36
    • 0028964821 scopus 로고
    • Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1
    • Klebe C, Bischoff FR, Ponstingl H, Wittinghofer A (1995). Interaction of the nuclear GTP-binding protein Ran with its regulatory proteins RCC1 and RanGAP1. Biochemistry 34, 639-647.
    • (1995) Biochemistry , vol.34 , pp. 639-647
    • Klebe, C.1    Bischoff, F.R.2    Ponstingl, H.3    Wittinghofer, A.4
  • 37
    • 54049107641 scopus 로고    scopus 로고
    • Some assembly required: Dedicated chaperones in eukaryotic proteasome biogenesis
    • Kusmierczyk AR, Hochstrasser M (2008). Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis. Biol Chem 389, 1143-1151.
    • (2008) Biol Chem , vol.389 , pp. 1143-1151
    • Kusmierczyk, A.R.1    Hochstrasser, M.2
  • 38
    • 0030960586 scopus 로고    scopus 로고
    • Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex
    • DOI 10.1093/emboj/16.6.1153
    • Kutay U, Izaurralde E, Bischoff FR, Mattaj IW, Gorlich D (1997). Dominant-negative mutants of importin-beta block multiple pathways of import and export through the nuclear pore complex. EMBO J 16, 1153-1163. (Pubitemid 27136082)
    • (1997) EMBO Journal , vol.16 , Issue.6 , pp. 1153-1163
    • Kutay, U.1    Izaurralde, E.2    Bischoff, F.R.3    Mattaj, I.W.4    Gorlich, D.5
  • 39
    • 0036296150 scopus 로고    scopus 로고
    • 20 S proteasomes are imported as precursor complexes into the nucleus of yeast
    • DOI 10.1006/jmbi.2002.5443
    • Lehmann A, Janek K, Braun B, Kloetzel PM, Enenkel C (2002). 20 S proteasomes are imported as precursor complexes into the nucleus of yeast. J Mol Biol 317, 401-413. (Pubitemid 34722179)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.3 , pp. 401-413
    • Lehmann, A.1    Janek, K.2    Braun, B.3    Kloetzel, P.-M.4    Enenkel, C.5
  • 40
  • 41
    • 0020622592 scopus 로고
    • Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components
    • Lohka MJ, Masui Y (1983). Formation in vitro of sperm pronuclei and mitotic chromosomes induced by amphibian ooplasmic components. Science 220, 719-721. (Pubitemid 13081946)
    • (1983) Science , vol.220 , Issue.4598 , pp. 719-721
    • Lohka, M.J.1    Masui, Y.2
  • 42
    • 0037078333 scopus 로고    scopus 로고
    • Influence of cargo size on Ran and energy requirements for nuclear protein import
    • DOI 10.1083/jcb.200204163
    • Lyman SK, Guan T, Bednenko J, Wodrich H, Gerace L (2002). Influence of cargo size on Ran and energy requirements for nuclear protein import. J Cell Biol 159, 55-67. (Pubitemid 35191518)
    • (2002) Journal of Cell Biology , vol.159 , Issue.1 , pp. 55-67
    • Lyman, S.K.1    Guan, T.2    Bednenko, J.3    Wodrich, H.4    Gerace, L.5
  • 43
    • 0030047960 scopus 로고    scopus 로고
    • Assembly of the nuclear pore: Biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA
    • Macaulay C, Forbes DJ (1996). Assembly of the nuclear pore: biochemically distinct steps revealed with NEM, GTP gamma S, and BAPTA. J Cell Biol 132, 5-20.
    • (1996) J Cell Biol , vol.132 , pp. 5-20
    • Macaulay, C.1    Forbes, D.J.2
  • 44
    • 0035970007 scopus 로고    scopus 로고
    • Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation
    • DOI 10.1073/pnas.031566998
    • Mattsson K, Pokrovskaja K, Kiss C, Klein G, Szekely L (2001). Proteins associated with the promyelocytic leukemia gene product (PML)-containing nuclear body move to the nucleolus upon inhibition of proteasome-dependent protein degradation. Proc Natl Acad Sci USA 98, 1012-1017. (Pubitemid 32121178)
    • (2001) Proceedings of the National Academy of Sciences of the United States of America , vol.98 , Issue.3 , pp. 1012-1017
    • Mattsson, K.1    Pokrovskaja, K.2    Kiss, C.3    Klein, G.4    Szekely, L.5
  • 45
    • 0032700056 scopus 로고    scopus 로고
    • The import pathway of human and Thermoplasma 20S proteasomes into HeLa cell nuclei is different from that of classical NLS-bearing proteins
    • Mayr J, Wang HR, Nederlof P, Baumeister W (1999). The import pathway of human and Thermoplasma 20S proteasomes into HeLa cell nuclei is different from that of classical NLS-bearing proteins. Biol Chem 380, 1183-1192.
    • (1999) Biol Chem , vol.380 , pp. 1183-1192
    • Mayr, J.1    Wang, H.R.2    Nederlof, P.3    Baumeister, W.4
  • 46
    • 43149121353 scopus 로고    scopus 로고
    • Molular basis for the recognition of snurportin 1 by importin beta
    • Mitrousis G, Olia AS, Walker-Kopp N, Cingolani G (2008). Molular basis for the recognition of snurportin 1 by importin beta. J Biol Chem 283, 7877-7884.
    • (2008) J Biol Chem , vol.283 , pp. 7877-7884
    • Mitrousis, G.1    Olia, A.S.2    Walker-Kopp, N.3    Cingolani, G.4
  • 49
    • 0024978338 scopus 로고
    • Cyclin synthesis drives the early embryonic cell cycle
    • Murray AW, Kirschner MW (1989). Cyclin synthesis drives the early embryonic cell cycle. Nature 339, 275-280.
    • (1989) Nature , vol.339 , pp. 275-280
    • Murray, A.W.1    Kirschner, M.W.2
  • 50
    • 0020407569 scopus 로고
    • A major developmental transition in early Xenopus embryos: I. characterization and timing of cellular changes at the midblastula stage
    • Newport J, Kirschner M (1982). A major developmental transition in early Xenopus embryos: I. characterization and timing of cellular changes at the midblastula stage. Cell 30, 675-686.
    • (1982) Cell , vol.30 , pp. 675-686
    • Newport, J.1    Kirschner, M.2
  • 51
    • 0028267689 scopus 로고
    • Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type
    • Olink-Coux M, Arcangeletti C, Pinardi F, Minisini R, Huesca M, Chezzi C, Scherrer K (1994). Cytolocation of prosome antigens on intermediate filament subnetworks of cytokeratin, vimentin and desmin type. J Cell Sci 107, Pt 3353-366.
    • (1994) J Cell Sci , vol.107 , Issue.PART , pp. 3353-3366
    • Olink-Coux, M.1    Arcangeletti, C.2    Pinardi, F.3    Minisini, R.4    Huesca, M.5    Chezzi, C.6    Scherrer, K.7
  • 53
    • 0036175701 scopus 로고    scopus 로고
    • Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm
    • DOI 10.1091/mbc.01-06-0308
    • Pante N, Kann M (2002). Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol Biol Cell 13, 425-434. (Pubitemid 34165072)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.2 , pp. 425-434
    • Pante, N.1    Kann, M.2
  • 54
    • 67149121057 scopus 로고    scopus 로고
    • Hexameric assembly of the proteasomal ATPases is templated through their C termini
    • Park S, Roelofs J, Kim W, Robert J, Schmidt M, Gygi SP, Finley D (2009). Hexameric assembly of the proteasomal ATPases is templated through their C termini. Nature 459, 866-870.
    • (2009) Nature , vol.459 , pp. 866-870
    • Park, S.1    Roelofs, J.2    Kim, W.3    Robert, J.4    Schmidt, M.5    Gygi, S.P.6    Finley, D.7
  • 55
    • 14544299215 scopus 로고    scopus 로고
    • Mechanisms of receptor-mediated nuclear import and nuclear export
    • DOI 10.1111/j.1600-0854.2005.00270.x
    • Pemberton LF, Paschal BM (2005). Mechanisms of receptor-mediated nuclear import and nuclear export. Traffic 6, 187-198. (Pubitemid 40298153)
    • (2005) Traffic , vol.6 , Issue.3 , pp. 187-198
    • Pemberton, L.F.1    Paschal, B.M.2
  • 57
    • 0028234770 scopus 로고
    • Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters JM, Franke WW, Kleinschmidt JA (1994). Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem 269, 7709-7718. (Pubitemid 24217985)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7709-7718
    • Peters, J.-M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 58
    • 0026265918 scopus 로고
    • Ultrastructure of the approximately 26S complex containing the approximately 20S cylinder particle (multicatalytic proteinase/proteasome)
    • Peters JM, Harris JR, Kleinschmidt JA (1991). Ultrastructure of the approximately 26S complex containing the approximately 20S cylinder particle (multicatalytic proteinase/proteasome). Eur J Cell Biol 56, 422-432.
    • (1991) Eur J Cell Biol , vol.56 , pp. 422-432
    • Peters, J.M.1    Harris, J.R.2    Kleinschmidt, J.A.3
  • 59
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • DOI 10.1038/nrm1336
    • Pickart CM, Cohen RE (2004). Proteasomes and their kin: proteases in the machine age. Nat Rev Mol Cell Biol 5, 177-187. (Pubitemid 38325799)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 61
    • 0030703686 scopus 로고    scopus 로고
    • Dynamics of proteasome distribution in living cells
    • DOI 10.1093/emboj/16.20.6087
    • Reits EA, Benham AM, Plougastel B, Neefjes J, Trowsdale J (1997). Dynamics of proteasome distribution in living cells. EMBO J 16, 6087-6094. (Pubitemid 27458328)
    • (1997) EMBO Journal , vol.16 , Issue.20 , pp. 6087-6094
    • Reits, E.A.J.1    Benham, A.M.2    Plougastel, B.3    Neefjes, J.4    Trowsdale, J.5
  • 62
    • 0037013954 scopus 로고    scopus 로고
    • The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion
    • DOI 10.1093/emboj/21.11.2664
    • Ribbeck K, Gorlich D (2002). The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion. EMBO J 21, 2664-2671. (Pubitemid 34619382)
    • (2002) EMBO Journal , vol.21 , Issue.11 , pp. 2664-2671
    • Ribbeck, K.1    Gorlich, D.2
  • 63
    • 67149112112 scopus 로고    scopus 로고
    • Chaperone-mediated pathway of proteasome regulatory particle assembly
    • Roelofs J et al. (2009). Chaperone-mediated pathway of proteasome regulatory particle assembly. Nature 459, 861-865.
    • (2009) Nature , vol.459 , pp. 861-865
    • Roelofs, J.1
  • 65
    • 70350228414 scopus 로고    scopus 로고
    • Importin beta regulates the seeding of chromatin with initiation sites for nuclear pore assembly
    • Rotem A, Gruber R, Shorer H, Shaulov L, Klein E, Harel A (2009). Importin beta regulates the seeding of chromatin with initiation sites for nuclear pore assembly. Mol Biol Cell 20, 4031-4042.
    • (2009) Mol Biol Cell , vol.20 , pp. 4031-4042
    • Rotem, A.1    Gruber, R.2    Shorer, H.3    Shaulov, L.4    Klein, E.5    Harel, A.6
  • 67
    • 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
    • DOI 10.1083/jcb.141.1.31
    • Shah S, Tugendreich S, Forbes D (1998). Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr. J Cell Biol 141, 31-49. (Pubitemid 28182639)
    • (1998) Journal of Cell Biology , vol.141 , Issue.1 , pp. 31-49
    • Shah, S.1    Tugendreich, S.2    Forbes, D.3
  • 68
    • 33847176295 scopus 로고    scopus 로고
    • Molular mechanism of the nuclear protein import cycle
    • Stewart M (2007). Molular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 8, 195-208.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 69
    • 0034913423 scopus 로고    scopus 로고
    • Importin-beta-like nuclear transport receptors
    • reviews3008.1-3008.9
    • Strom AC, Weis K (2001). Importin-beta-like nuclear transport receptors. Genome Biol 2, reviews3008.1-3008.9.
    • (2001) Genome Biol , vol.2
    • Strom, A.C.1    Weis, K.2
  • 70
    • 59449095881 scopus 로고    scopus 로고
    • Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process
    • Tonoki A, Kuranaga E, Tomioka T, Hamazaki J, Murata S, Tanaka K, Miura M (2009). Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol Cell Biol 29, 1095-1106.
    • (2009) Mol Cell Biol , vol.29 , pp. 1095-1106
    • Tonoki, A.1    Kuranaga, E.2    Tomioka, T.3    Hamazaki, J.4    Murata, S.5    Tanaka, K.6    Miura, M.7
  • 72
    • 85052429959 scopus 로고    scopus 로고
    • The nuclear ubiquitin-proteasome system: Visualization of proteasomes, protein aggregates, and proteolysis in the cell nucleus
    • von Mikecz A, Chen M, Rockel T, Scharf A (2008). The nuclear ubiquitin-proteasome system: visualization of proteasomes, protein aggregates, and proteolysis in the cell nucleus. Methods Mol Biol 463, 191-202.
    • (2008) Methods Mol Biol , vol.463 , pp. 191-202
    • Von Mikecz, A.1    Chen, M.2    Rockel, T.3    Scharf, A.4
  • 74
    • 0030919574 scopus 로고    scopus 로고
    • Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences
    • Wang HR, Kania M, Baumeister W, Nederlof PM (1997). Import of human and Thermoplasma 20S proteasomes into nuclei of HeLa cells requires functional NLS sequences. Eur J Cell Biol 73, 105-113.
    • (1997) Eur J Cell Biol , vol.73 , pp. 105-113
    • Wang, H.R.1    Kania, M.2    Baumeister, W.3    Nederlof, P.M.4
  • 75
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis K (2003). Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112, 441-451.
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 76
    • 4444237601 scopus 로고    scopus 로고
    • The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alphabeta and proteasome functions
    • DOI 10.1074/jbc.M403551200
    • Wendler P, Lehmann A, Janek K, Baumgart S, Enenkel C (2004). The bipartite nuclear localization sequence of Rpn2 is required for nuclear import of proteasomal base complexes via karyopherin alpha beta and proteasome functions. J Biol Chem 279, 37751-37762. (Pubitemid 39195489)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37751-37762
    • Wendler, P.1    Lehmann, A.2    Janek, K.3    Baumgart, S.4    Enenkel, C.5
  • 78
    • 0344528638 scopus 로고    scopus 로고
    • Proteasome activator subunit PA28 alpha and related Ki antigen (PA28 gamma) are absent from the nuclear fraction purified by sucrose gradient centrifugation
    • Wojcik C (1999). Proteasome activator subunit PA28 alpha and related Ki antigen (PA28 gamma) are absent from the nuclear fraction purified by sucrose gradient centrifugation. Int J Biochem Cell Biol 31, 273-276.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 273-276
    • Wojcik, C.1
  • 80
    • 0032910953 scopus 로고    scopus 로고
    • Beta-Catenin can be transported into the nucleus in a ran-unassisted manner
    • Yokoya F, Imamoto N, Tachibana T, Yoneda Y (1999). Beta-catenin can be transported into the nucleus in a Ran-unassisted manner. Mol Biol Cell 10, 1119-1131. (Pubitemid 29193735)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.4 , pp. 1119-1131
    • Yokoya, F.1    Imamoto, N.2    Tachibana, T.3    Yoneda, Y.4
  • 81
    • 69249099667 scopus 로고    scopus 로고
    • S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function
    • Zmijewski JW, Banerjee S, Abraham E (2009). S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function. J Biol Chem 284, 22213-22221
    • (2009) J Biol Chem , vol.284 , pp. 22213-22221
    • Zmijewski, J.W.1    Banerjee, S.2    Abraham, E.3


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