메뉴 건너뛰기




Volumn 10, Issue 3, 2011, Pages 425-433

Unexpected role of nucleoporins in coordination of cell cycle progression

Author keywords

Cell cycle; Centrosomes; Kinetochores; Mitotic spindle; NPC

Indexed keywords

NUCLEOPORIN;

EID: 79851498250     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.10.3.14721     Document Type: Review
Times cited : (39)

References (74)
  • 1
    • 77953893804 scopus 로고    scopus 로고
    • The nuclear pore complex: Bridging nuclear transport and gene regulation
    • Strambio-De-Castillia C, Niepel M, Rout MP. The nuclear pore complex: bridging nuclear transport and gene regulation. Nat Rev Mol Cell Biol 2010; 11:490-501.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 490-501
    • Strambio-De-Castillia, C.1    Niepel, M.2    Rout, M.P.3
  • 2
    • 67649947773 scopus 로고    scopus 로고
    • Sizing up the nucleus: Nuclear shape, size and nuclear-envelope assembly
    • Webster M, Witkin KL, Cohen-Fix O. Sizing up the nucleus: nuclear shape, size and nuclear-envelope assembly. J Cell Sci 2009; 122:1477-86.
    • (2009) J Cell Sci , vol.122 , pp. 1477-1486
    • Webster, M.1    Witkin, K.L.2    Cohen-Fix, O.3
  • 3
    • 80052406907 scopus 로고    scopus 로고
    • Three-Dimensional Organization of Chromatids by Nuclear Envelope-Associated Structures
    • Blobel G. Three-Dimensional Organization of Chromatids by Nuclear Envelope-Associated Structures. Cold Spring Harb Symp Quant Biol 2010.
    • Cold Spring Harb Symp Quant Biol 2010
    • Blobel, G.1
  • 4
    • 77957660297 scopus 로고    scopus 로고
    • Nuclear pore biogenesis into an intact nuclear envelope
    • Doucet CM, Hetzer MW. Nuclear pore biogenesis into an intact nuclear envelope. Chromosoma 2010; 119:469-77.
    • (2010) Chromosoma , vol.119 , pp. 469-477
    • Doucet, C.M.1    Hetzer, M.W.2
  • 5
    • 39149125768 scopus 로고    scopus 로고
    • Towards reconciling structure and function in the nuclear pore complex
    • Lim RY, Aebi U, Fahrenkrog B. Towards reconciling structure and function in the nuclear pore complex. Histochem Cell Biol 2008; 129:105-16.
    • (2008) Histochem Cell Biol , vol.129 , pp. 105-116
    • Lim, R.Y.1    Aebi, U.2    Fahrenkrog, B.3
  • 6
    • 0040419373 scopus 로고
    • Experimental studies on amphibian oocyte nuclei. I. Investigation of the structure of the nuclear membrane by means of the electron microscope
    • Callan HG, Tomlin SG. Experimental studies on amphibian oocyte nuclei. I. Investigation of the structure of the nuclear membrane by means of the electron microscope. Proc R Soc Lond B Biol Sci 1950; 137:367-78.
    • (1950) Proc R Soc Lond B Biol Sci , vol.137 , pp. 367-378
    • Callan, H.G.1    Tomlin, S.G.2
  • 7
    • 0014059126 scopus 로고
    • Octagonal nuclear pores
    • Gall JG. Octagonal nuclear pores. J Cell Biol 1967; 32:391-9.
    • (1967) J Cell Biol , vol.32 , pp. 391-399
    • Gall, J.G.1
  • 8
    • 0016298328 scopus 로고
    • On the attachment of the nuclear pore complex
    • Aaronson RP, Blobel G. On the attachment of the nuclear pore complex. J Cell Biol 1974; 62:746-54.
    • (1974) J Cell Biol , vol.62 , pp. 746-754
    • Aaronson, R.P.1    Blobel, G.2
  • 10
    • 73249130542 scopus 로고    scopus 로고
    • Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture
    • Frenkiel-Krispin D, Maco B, Aebi U, Medalia O. Structural analysis of a metazoan nuclear pore complex reveals a fused concentric ring architecture. J Mol Biol 2010; 395:578-86.
    • (2010) J Mol Biol , vol.395 , pp. 578-586
    • Frenkiel-Krispin, D.1    Maco, B.2    Aebi, U.3    Medalia, O.4
  • 11
    • 70350755470 scopus 로고    scopus 로고
    • Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice
    • Brohawn SG, Schwartz TU. Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice. Nat Struct Mol Biol 2009; 16:1173-7.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1173-1177
    • Brohawn, S.G.1    Schwartz, T.U.2
  • 12
    • 37349009269 scopus 로고    scopus 로고
    • Architecture of a Coat for the Nuclear Pore Membrane
    • DOI 10.1016/j.cell.2007.11.038, PII S0092867407015425
    • Hsia KC, Stavropoulos P, Blobel G, Hoelz A. Architecture of a coat for the nuclear pore membrane. Cell 2007; 131:1313-26. (Pubitemid 350297420)
    • (2007) Cell , vol.131 , Issue.7 , pp. 1313-1326
    • Hsia, K.-C.1    Stavropoulos, P.2    Blobel, G.3    Hoelz, A.4
  • 14
    • 17044415652 scopus 로고    scopus 로고
    • Modularity within the architecture of the nuclear pore complex
    • Schwartz TU. Modularity within the architecture of the nuclear pore complex. Curr Opin Struct Biol 2005; 15:221-6.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 221-226
    • Schwartz, T.U.1
  • 17
    • 67649435612 scopus 로고    scopus 로고
    • Nuclear pore proteins and cancer
    • Xu S, Powers MA. Nuclear pore proteins and cancer. Semin Cell Dev Biol 2009; 20:620-30.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 620-630
    • Xu, S.1    Powers, M.A.2
  • 18
    • 33744967486 scopus 로고    scopus 로고
    • Dynamic Nuclear Pore Complexes: Life on the Edge
    • DOI 10.1016/j.cell.2006.05.027, PII S009286740600674X
    • Tran EJ, Wente SR. Dynamic nuclear pore complexes: life on the edge. Cell 2006; 125:1041-53. (Pubitemid 43866205)
    • (2006) Cell , vol.125 , Issue.6 , pp. 1041-1053
    • Tran, E.J.1    Wente, S.R.2
  • 20
    • 71549126814 scopus 로고    scopus 로고
    • Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes
    • Hetzer MW, Wente SR. Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. Dev Cell 2009; 17:606-16.
    • (2009) Dev Cell , vol.17 , pp. 606-616
    • Hetzer, M.W.1    Wente, S.R.2
  • 21
    • 11144310642 scopus 로고    scopus 로고
    • Popping out of the nucleus
    • DOI 10.1038/432815a
    • Hoelz A, Blobel G. Cell biology: popping out of the nucleus. Nature 2004; 432:815-6. (Pubitemid 40037133)
    • (2004) Nature , vol.432 , Issue.7019 , pp. 815-816
    • Hoelz, A.1    Blobel, G.2
  • 22
    • 67649452381 scopus 로고    scopus 로고
    • The role of the nuclear transport system in cell differentiation
    • Yasuhara N, Oka M, Yoneda Y. The role of the nuclear transport system in cell differentiation. Semin Cell Dev Biol 2009; 20:590-9.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 590-599
    • Yasuhara, N.1    Oka, M.2    Yoneda, Y.3
  • 23
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: Insights from virology
    • DOI 10.1016/S0968-0004(03)00142-7
    • Cullen BR. Nuclear mRNA export: insights from virology. Trends Biochem Sci 2003; 28:419-24. (Pubitemid 36976744)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.8 , pp. 419-424
    • Cullen, B.R.1
  • 24
    • 0037899299 scopus 로고    scopus 로고
    • Complex formation among the RNA export proteins Nup98, Rae1/Gle2, and TAP
    • DOI 10.1074/jbc.M302061200
    • Blevins MB, Smith AM, Phillips EM, Powers MA. Complex formation among the RNA export proteins Nup98, Rae1/Gle2 and TAP. J Biol Chem 2003; 278:20979-88. (Pubitemid 36806407)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.23 , pp. 20979-20988
    • Blevins, M.B.1    Smith, A.M.2    Phillips, E.M.3    Powers, M.A.4
  • 25
    • 34648816826 scopus 로고    scopus 로고
    • Exporting RNA from the nucleus to the cytoplasm
    • DOI 10.1038/nrm2255, PII NRM2255
    • Kohler A, Hurt E. Exporting RNA from the nucleus to the cytoplasm. Nat Rev Mol Cell Biol 2007; 8:761-73. (Pubitemid 47462133)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 761-773
    • Kohler, A.1    Hurt, E.2
  • 26
    • 33847176295 scopus 로고    scopus 로고
    • Molecular mechanism of the nuclear protein import cycle
    • Stewart M. Molecular mechanism of the nuclear protein import cycle. Nat Rev Mol Cell Biol 2007; 8:195-208.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 195-208
    • Stewart, M.1
  • 27
    • 65449152302 scopus 로고    scopus 로고
    • Translocation through the nuclear pore: Kaps pave the way
    • Peters R. Translocation through the nuclear pore: Kaps pave the way. Bioessays 2009; 31:466-77.
    • (2009) Bioessays , vol.31 , pp. 466-477
    • Peters, R.1
  • 28
    • 60749108426 scopus 로고    scopus 로고
    • Orchestrating nuclear envelope disassembly and reassembly during mitosis
    • Guttinger S, Laurell E, Kutay U. Orchestrating nuclear envelope disassembly and reassembly during mitosis. Nat Rev Mol Cell Biol 2009; 10:178-91.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 178-191
    • Guttinger, S.1    Laurell, E.2    Kutay, U.3
  • 29
    • 38949132114 scopus 로고    scopus 로고
    • Mechanisms of Mitotic Spindle Assembly and Function
    • DOI 10.1016/S0074-7696(07)65003-7, PII S0074769607650037, A Survey of Cell Biology
    • Walczak CE, Heald R. Mechanisms of mitotic spindle assembly and function. Int Rev Cytol 2008; 265:111-58. (Pubitemid 351215987)
    • (2008) International Review of Cytology , vol.265 , pp. 111-158
    • Walczak, C.E.1    Heald, R.2
  • 31
    • 0017744795 scopus 로고
    • Nuclear pore complexes. Elimination and reconstruction during mitosis
    • DOI 10.1083/jcb.74.2.492
    • Maul GG. Nuclear pore complexes. Elimination and reconstruction during mitosis. J Cell Biol 1977; 74:492-500. (Pubitemid 8153984)
    • (1977) Journal of Cell Biology , vol.74 , Issue.2 , pp. 492-500
    • Maul, G.G.1
  • 32
    • 0017636049 scopus 로고
    • The nuclear and the cytoplasmic pore complex: Structure, dynamics, distribution and evolution
    • Maul GG. The nuclear and the cytoplasmic pore complex: structure, dynamics, distribution and evolution. Int Rev Cytol 1977; 75-186.
    • (1977) Int Rev Cytol , pp. 75-186
    • Maul, G.G.1
  • 33
    • 52949107958 scopus 로고    scopus 로고
    • Structure, dynamics and function of nuclear pore complexes
    • D'Angelo MA, Hetzer MW. Structure, dynamics and function of nuclear pore complexes. Trends Cell Biol 2008; 18:456-66.
    • (2008) Trends Cell Biol , vol.18 , pp. 456-466
    • D'Angelo, M.A.1    Hetzer, M.W.2
  • 34
    • 77954043950 scopus 로고    scopus 로고
    • Nuclear transport and the mitotic apparatus: An evolving relationship
    • Wozniak R, Burke B, Doye V. Nuclear transport and the mitotic apparatus: an evolving relationship. Cell Mol Life Sci 2010; 67:2215-30.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2215-2230
    • Wozniak, R.1    Burke, B.2    Doye, V.3
  • 38
    • 0344171991 scopus 로고    scopus 로고
    • RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains
    • Pritchard CE, Fornerod M, Kasper LH, van Deursen JM. RAE1 is a shuttling mRNA export factor that binds to a GLEBS-like NUP98 motif at the nuclear pore complex through multiple domains. J Cell Biol 1999; 145:237-54.
    • (1999) J Cell Biol , vol.145 , pp. 237-254
    • Pritchard, C.E.1    Fornerod, M.2    Kasper, L.H.3    Van Deursen, J.M.4
  • 39
    • 77953800169 scopus 로고    scopus 로고
    • Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1
    • Ren Y, Seo HS, Blobel G, Hoelz A. Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1. Proc Natl Acad Sci USA 2010; 107:10406-11.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10406-10411
    • Ren, Y.1    Seo, H.S.2    Blobel, G.3    Hoelz, A.4
  • 40
    • 30744477013 scopus 로고    scopus 로고
    • The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation
    • DOI 10.1038/nature04221, PII NATURE04221
    • Jeganathan KB, Malureanu L, van Deursen JM. The Rae1-Nup98 complex prevents aneuploidy by inhibiting securin degradation. Nature 2005; 438:1036-9. (Pubitemid 43093978)
    • (2005) Nature , vol.438 , Issue.7070 , pp. 1036-1039
    • Jeganathan, K.B.1    Malureanu, L.2    Van, D.J.M.3
  • 41
    • 0035544296 scopus 로고    scopus 로고
    • Mrnp41 (Rae1p) associates with microtubules in HeLa cells and in neurons
    • Kraemer D, Dresbach T, Drenckhahn D. Mrnp41 (Rae 1p) associates with microtubules in HeLa cells and in neurons. Eur J Cell Biol 2001; 80:733-40. (Pubitemid 34092942)
    • (2001) European Journal of Cell Biology , vol.80 , Issue.12 , pp. 733-740
    • Kraemer, D.1    Dresbach, T.2    Drenckhahn, D.3
  • 42
    • 17444411537 scopus 로고    scopus 로고
    • A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly
    • DOI 10.1016/j.cell.2005.02.016
    • Blower MD, Nachury M, Heald R, Weis K. A Rae1-containing ribonucleoprotein complex is required for mitotic spindle assembly. Cell 2005; 121:223-34. (Pubitemid 40546390)
    • (2005) Cell , vol.121 , Issue.2 , pp. 223-234
    • Blower, M.D.1    Nachury, M.2    Heald, R.3    Weis, K.4
  • 43
    • 55749115817 scopus 로고    scopus 로고
    • Cohesin subunit SMC1 associates with mitotic microtubules at the spindle pole
    • Wong RW, Blobel G. Cohesin subunit SMC1 associates with mitotic microtubules at the spindle pole. Proc Natl Acad Sci USA 2008; 105:15441-5.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 15441-15445
    • Wong, R.W.1    Blobel, G.2
  • 44
    • 74549154688 scopus 로고    scopus 로고
    • Interaction between Rae1 and cohesin subunit SMC1 is required for proper spindle formation
    • Wong RW. Interaction between Rae1 and cohesin subunit SMC1 is required for proper spindle formation. Cell Cycle 2010; 9:198-200.
    • (2010) Cell Cycle , vol.9 , pp. 198-200
    • Wong, R.W.1
  • 45
    • 77953580240 scopus 로고    scopus 로고
    • An update on cohesin function as a 'molecular glue' on chromosomes and spindles
    • Wong RW. An update on cohesin function as a 'molecular glue' on chromosomes and spindles. Cell Cycle 2010; 9:1754-8.
    • (2010) Cell Cycle , vol.9 , pp. 1754-1758
    • Wong, R.W.1
  • 46
    • 65249146121 scopus 로고    scopus 로고
    • Cohesin associates with spindle poles in a mitosis-specific manner and functions in spindle assembly in vertebrate cells
    • Kong X, Ball AR Jr, Sonoda E, Feng J, Takeda S, Fukagawa T, et al. Cohesin associates with spindle poles in a mitosis-specific manner and functions in spindle assembly in vertebrate cells. Mol Biol Cell 2009; 20:1289-301.
    • (2009) Mol Biol Cell , vol.20 , pp. 1289-1301
    • Kong, X.1    Ball Jr., A.R.2    Sonoda, E.3    Feng, J.4    Takeda, S.5    Fukagawa, T.6
  • 48
    • 69749083046 scopus 로고    scopus 로고
    • Chromosome cohesion and the spindle checkpoint
    • Diaz-Martinez LA, Clarke DJ. Chromosome cohesion and the spindle checkpoint. Cell Cycle 2009; 8:2733-40.
    • (2009) Cell Cycle , vol.8 , pp. 2733-2740
    • Diaz-Martinez, L.A.1    Clarke, D.J.2
  • 50
    • 77953582924 scopus 로고    scopus 로고
    • Rad21 is required for centrosome integrity in human cells independently of its role in chromosome cohesion
    • Beauchene NA, Diaz-Martinez LA, Furniss K, Hsu WS, Tsai HJ, Chamberlain C, et al. Rad21 is required for centrosome integrity in human cells independently of its role in chromosome cohesion. Cell Cycle 2010; 9:1774-80.
    • (2010) Cell Cycle , vol.9 , pp. 1774-1780
    • Beauchene, N.A.1    Diaz-Martinez, L.A.2    Furniss, K.3    Hsu, W.S.4    Tsai, H.J.5    Chamberlain, C.6
  • 51
    • 70249109233 scopus 로고    scopus 로고
    • Enhanced genomic instabilities caused by deregulated microtubule dynamics and chromosome segregation: A perspective from genetic studies in mice
    • Rao CV, Yamada HY, Yao Y, Dai W. Enhanced genomic instabilities caused by deregulated microtubule dynamics and chromosome segregation: a perspective from genetic studies in mice. Carcinogenesis 2009; 30:1469-74.
    • (2009) Carcinogenesis , vol.30 , pp. 1469-1474
    • Rao, C.V.1    Yamada, H.Y.2    Yao, Y.3    Dai, W.4
  • 52
    • 55749104738 scopus 로고    scopus 로고
    • Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint
    • Lee SH, Sterling H, Burlingame A, McCormick F. Tpr directly binds to Mad1 and Mad2 and is important for the Mad1-Mad2-mediated mitotic spindle checkpoint. Genes Dev 2008; 22:2926-31.
    • (2008) Genes Dev , vol.22 , pp. 2926-2931
    • Lee, S.H.1    Sterling, H.2    Burlingame, A.3    McCormick, F.4
  • 53
    • 64749091329 scopus 로고    scopus 로고
    • Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator
    • Lince-Faria M, Maffini S, Orr B, Ding Y, Claudia F, Sunkel CE, et al. Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator. J Cell Biol 2009; 184:647-57.
    • (2009) J Cell Biol , vol.184 , pp. 647-657
    • Lince-Faria, M.1    Maffini, S.2    Orr, B.3    Ding, Y.4    Claudia, F.5    Sunkel, C.E.6
  • 54
    • 77951209602 scopus 로고    scopus 로고
    • Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis
    • Nakano H, Funasaka T, Hashizume C, Wong RW. Nucleoporin translocated promoter region (Tpr) associates with dynein complex, preventing chromosome lagging formation during mitosis. J Biol Chem 2010; 285:10841-9.
    • (2010) J Biol Chem , vol.285 , pp. 10841-10849
    • Nakano, H.1    Funasaka, T.2    Hashizume, C.3    Wong, R.W.4
  • 55
    • 33847292778 scopus 로고    scopus 로고
    • From Tpr-Met to Met, tumorigenesis and tubes
    • DOI 10.1038/sj.onc.1210201, PII 1210201
    • Peschard P, Park M. From Tpr-Met to Met, tumorigenesis and tubes. Oncogene 2007; 26:1276-85. (Pubitemid 46328462)
    • (2007) Oncogene , vol.26 , Issue.9 , pp. 1276-1285
    • Peschard, P.1    Park, M.2
  • 57
    • 17044457744 scopus 로고    scopus 로고
    • The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis
    • DOI 10.1091/mbc.E03-12-0878
    • Loiodice I, Alves A, Rabut G, Van Overbeek M, Ellenberg J, Sibarita JB, et al. The entire Nup107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol Biol Cell 2004; 15:3333-44. (Pubitemid 38850127)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.7 , pp. 3333-3344
    • Loiodice, I.1    Alves, A.2    Rabut, G.3    Van, O.M.4    Ellenberg, J.5    Sibarita, J.-B.6    Doye, V.7
  • 58
    • 40749091704 scopus 로고    scopus 로고
    • Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export
    • Resendes KK, Rasala BA, Forbes DJ. Centrin 2 localizes to the vertebrate nuclear pore and plays a role in mRNA and protein export. Mol Cell Biol 2008; 28:1755-69.
    • (2008) Mol Cell Biol , vol.28 , pp. 1755-1769
    • Resendes, K.K.1    Rasala, B.A.2    Forbes, D.J.3
  • 61
    • 55549131172 scopus 로고    scopus 로고
    • Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly
    • Rasala BA, Ramos C, Harel A, Forbes DJ. Capture of AT-rich chromatin by ELYS recruits POM121 and NDC1 to initiate nuclear pore assembly. Mol Biol Cell 2008; 19:3982-96.
    • (2008) Mol Biol Cell , vol.19 , pp. 3982-3996
    • Rasala, B.A.1    Ramos, C.2    Harel, A.3    Forbes, D.J.4
  • 62
    • 73849084214 scopus 로고    scopus 로고
    • The Nup107-160 nucleoporin complex promotes mitotic events via control of the localization state of the chromosome passenger complex
    • Platani M, Santarella-Mellwig R, Posch M, Walczak R, Swedlow JR, Mattaj IW. The Nup107-160 nucleoporin complex promotes mitotic events via control of the localization state of the chromosome passenger complex. Mol Biol Cell 2009; 20:5260-75.
    • (2009) Mol Biol Cell , vol.20 , pp. 5260-5275
    • Platani, M.1    Santarella-Mellwig, R.2    Posch, M.3    Walczak, R.4    Swedlow, J.R.5    Mattaj, I.W.6
  • 63
    • 75949103898 scopus 로고    scopus 로고
    • The Nup107-160 complex and gamma-TuRC regulate microtubule polymerization at kinetochores
    • Mishra RK, Chakraborty P, Arnaoutov A, Fontoura BM, Dasso M. The Nup107-160 complex and gamma-TuRC regulate microtubule polymerization at kinetochores. Nat Cell Biol 2010; 12:164-9.
    • (2010) Nat Cell Biol , vol.12 , pp. 164-169
    • Mishra, R.K.1    Chakraborty, P.2    Arnaoutov, A.3    Fontoura, B.M.4    Dasso, M.5
  • 65
    • 0029070074 scopus 로고
    • Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain and a leucine-rich region
    • Wu J, Matunis MJ, Kraemer D, Blobel G, Coutavas E. Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain and a leucine-rich region. J Biol Chem 1995; 270:14209-13.
    • (1995) J Biol Chem , vol.270 , pp. 14209-14213
    • Wu, J.1    Matunis, M.J.2    Kraemer, D.3    Blobel, G.4    Coutavas, E.5
  • 67
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • DOI 10.1016/j.cub.2004.03.031, PII S0960982204002106
    • Joseph J, Liu ST, Jablonski SA, Yen TJ, Dasso M. The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr Biol 2004; 14:611-7. (Pubitemid 38458952)
    • (2004) Current Biology , vol.14 , Issue.7 , pp. 611-617
    • Joseph, J.1    Liu, S.-T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 69
    • 0141545024 scopus 로고    scopus 로고
    • Nup358 integrates nuclear envelope breakdown with kinetochore assembly
    • DOI 10.1083/jcb.200304080
    • Salina D, Enarson P, Rattner JB, Burke B. Nup358 integrates nuclear envelope breakdown with kinetochore assembly. J Cell Biol 2003; 162:991-1001. (Pubitemid 37174183)
    • (2003) Journal of Cell Biology , vol.162 , Issue.6 , pp. 991-1001
    • Salina, D.1    Enarson, P.2    Rattner, J.B.3    Burke, B.4
  • 70
    • 41149146735 scopus 로고    scopus 로고
    • Resolution of Sister Centromeres Requires RanBP2-Mediated SUMOylation of Topoisomerase IIalpha
    • DOI 10.1016/j.cell.2008.01.045, PII S0092867408002109
    • Dawlaty MM, Malureanu L, Jeganathan KB, Kao E, Sustmann C, Tahk S, et al. Resolution of sister centromeres requires RanBP2-mediated SUMOylation of topoisomerase IIalpha. Cell 2008; 133:103-15. (Pubitemid 351442988)
    • (2008) Cell , vol.133 , Issue.1 , pp. 103-115
    • Dawlaty, M.M.1    Malureanu, L.2    Jeganathan, K.B.3    Kao, E.4    Sustmann, C.5    Tahk, S.6    Shuai, K.7    Grosschedl, R.8    Van, D.J.M.9
  • 71
    • 77954080048 scopus 로고    scopus 로고
    • Characterization of the role of the tumor marker Nup88 in mitosis
    • Hashizume C, Nakano H, Yoshida K, Wong RW. Characterization of the role of the tumor marker Nup88 in mitosis. Mol Cancer 2010; 9:119.
    • (2010) Mol Cancer , vol.9 , pp. 119
    • Hashizume, C.1    Nakano, H.2    Yoshida, K.3    Wong, R.W.4
  • 72
    • 65249089181 scopus 로고    scopus 로고
    • The nucleoporin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis
    • Mackay DR, Elgort SW, Ullman KS. The nucleoporin Nup153 has separable roles in both early mitotic progression and the resolution of mitosis. Mol Biol Cell 2009; 20:1652-60.
    • (2009) Mol Biol Cell , vol.20 , pp. 1652-1660
    • Mackay, D.R.1    Elgort, S.W.2    Ullman, K.S.3
  • 73
    • 77954177001 scopus 로고    scopus 로고
    • The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1
    • Lussi Y, Shumaker D, Shimi T, Fahrenkrog B. The nucleoporin Nup153 affects spindle checkpoint activity due to an association with Mad1. Nucleus 2010; 1:71-84.
    • (2010) Nucleus , vol.1 , pp. 71-84
    • Lussi, Y.1    Shumaker, D.2    Shimi, T.3    Fahrenkrog, B.4
  • 74
    • 78649685697 scopus 로고    scopus 로고
    • Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint
    • Mackay DR, Makise M, Ullman KS. Defects in nuclear pore assembly lead to activation of an Aurora B-mediated abscission checkpoint. J Cell Biol 2010; 191:923-31.
    • (2010) J Cell Biol , vol.191 , pp. 923-931
    • Mackay, D.R.1    Makise, M.2    Ullman, K.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.