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Volumn 15, Issue 3, 2003, Pages 338-344

The small GTPase Ran: Interpreting the signs

Author keywords

[No Author keywords available]

Indexed keywords

GUANOSINE TRIPHOSPHATASE; KARYOPHERIN BETA; RAN PROTEIN;

EID: 0038699131     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(03)00046-2     Document Type: Review
Times cited : (165)

References (44)
  • 1
    • 0029090517 scopus 로고
    • Catalysis of guanine nucleotide exchange of Ran by RCC1 and stimulation of hydrolysis of Ran-bound GTP by Ran-GAP1
    • Bischoff F.R., Ponstingl H. Catalysis of guanine nucleotide exchange of Ran by RCC1 and stimulation of hydrolysis of Ran-bound GTP by Ran-GAP1. Methods Enzymol. 257:1995;135-144.
    • (1995) Methods Enzymol. , vol.257 , pp. 135-144
    • Bischoff, F.R.1    Ponstingl, H.2
  • 2
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • Mahajan R., Delphin C., Guan T., Gerace L., Melchior F. A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell. 88:1997;97-107.
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 3
    • 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., Coutavas E., Blobel G. 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. 135:1996;1457-1470.
    • (1996) J. Cell Biol. , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 4
    • 0026419320 scopus 로고
    • Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1
    • Bischoff F.R., Ponstingl H. Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature. 354:1991;80-82.
    • (1991) Nature , vol.354 , pp. 80-82
    • Bischoff, F.R.1    Ponstingl, H.2
  • 5
    • 0024445582 scopus 로고
    • The RCC1 protein, a regulator for the onset of chromosome condensation locates in the nucleus and binds to DNA
    • Ohtsubo M., Okazaki H., Nishimoto T. The RCC1 protein, a regulator for the onset of chromosome condensation locates in the nucleus and binds to DNA. J. Cell Biol. 109:1989;1389-1397.
    • (1989) J. Cell Biol. , vol.109 , pp. 1389-1397
    • Ohtsubo, M.1    Okazaki, H.2    Nishimoto, T.3
  • 6
    • 0035947299 scopus 로고    scopus 로고
    • Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B
    • The authors demonstrate that RCC1 binds directly to mononucleosomes through histones H2A and H2B, identifying the mechanism by which RCC1 binds to chromatin.
    • Nemergut M.E., Mizzen C.A., Stukenberg T., Allis C.D., Macara I.G. Chromatin docking and exchange activity enhancement of RCC1 by histones H2A and H2B. Science. 292:2001;1540-1543 The authors demonstrate that RCC1 binds directly to mononucleosomes through histones H2A and H2B, identifying the mechanism by which RCC1 binds to chromatin.
    • (2001) Science , vol.292 , pp. 1540-1543
    • Nemergut, M.E.1    Mizzen, C.A.2    Stukenberg, T.3    Allis, C.D.4    Macara, I.G.5
  • 7
    • 0032814745 scopus 로고    scopus 로고
    • Ran-GTP stabilises microtubule asters and inhibits nuclear assembly in Xenopus egg extracts
    • Zhang C., Hughes M., Clarke P.R. Ran-GTP stabilises microtubule asters and inhibits nuclear assembly in Xenopus egg extracts. J. Cell Sci. 112:1999;2453-2461.
    • (1999) J. Cell Sci. , vol.112 , pp. 2453-2461
    • Zhang, C.1    Hughes, M.2    Clarke, P.R.3
  • 8
    • 0037046812 scopus 로고    scopus 로고
    • Ran binds to chromatin by two distinct mechanisms
    • Data presented here provide the first evidence that Ran binds directly to chromatin through histones H3 and H4.
    • Bilbao-Cortes D., Hetzer M., Laengst G., Becker P.B., Mattaj I.W. Ran binds to chromatin by two distinct mechanisms. Curr. Biol. 12:2002;1151-1156 Data presented here provide the first evidence that Ran binds directly to chromatin through histones H3 and H4.
    • (2002) Curr. Biol. , vol.12 , pp. 1151-1156
    • Bilbao-Cortes, D.1    Hetzer, M.2    Laengst, G.3    Becker, P.B.4    Mattaj, I.W.5
  • 9
    • 0035203632 scopus 로고    scopus 로고
    • Transport into and out of the nucleus
    • table of contents
    • Macara I.G. Transport into and out of the nucleus. Microbiol. Mol. Biol. Rev. 65:2001;570-594. table of contents.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 570-594
    • Macara, I.G.1
  • 10
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • The authors demonstrate that RanGAP localizes to the mitotic spindle and kinetochores in HeLa cells. This localization is dependent on modification of Ran GTPase-activating protein by the small ubiquitin-like molecule SUMO1.
    • Joseph J., Tan S.H., Karpova T.S., McNally J.G., Dasso M. SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 156:2002;595-602 The authors demonstrate that RanGAP localizes to the mitotic spindle and kinetochores in HeLa cells. This localization is dependent on modification of Ran GTPase-activating protein by the small ubiquitin-like molecule SUMO1.
    • (2002) J. Cell Biol. , vol.156 , pp. 595-602
    • Joseph, J.1    Tan, S.H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 11
    • 0036017872 scopus 로고    scopus 로고
    • Plant RanGAPs are localized at the nuclear envelope in interphase and associated with microtubules in mitotic cells
    • This paper demonstrates that plant Ran GTPase-activating protein (RanGAP), like metazoan RanGAP, localizes to the nuclear rim in interphase. In addition, plant RanGAP localizes to the spindle during mitosis.
    • Pay A., Resch K., Frohnmeyer H., Fejes E., Nagy F., Nick P. Plant RanGAPs are localized at the nuclear envelope in interphase and associated with microtubules in mitotic cells. Plant J. 30:2002;699-709 This paper demonstrates that plant Ran GTPase-activating protein (RanGAP), like metazoan RanGAP, localizes to the nuclear rim in interphase. In addition, plant RanGAP localizes to the spindle during mitosis.
    • (2002) Plant J. , vol.30 , pp. 699-709
    • Pay, A.1    Resch, K.2    Frohnmeyer, H.3    Fejes, E.4    Nagy, F.5    Nick, P.6
  • 12
    • 0028937195 scopus 로고
    • Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1
    • Bischoff F.R., Krebber H., Smirnova E., Dong W., Ponstingl H. Co-activation of RanGTPase and inhibition of GTP dissociation by Ran-GTP binding protein RanBP1. EMBO J. 14:1995;705-715.
    • (1995) EMBO J. , vol.14 , pp. 705-715
    • Bischoff, F.R.1    Krebber, H.2    Smirnova, E.3    Dong, W.4    Ponstingl, H.5
  • 13
    • 0028784164 scopus 로고
    • Mutants in a yeast Ran binding protein are defective in nuclear transport
    • Schlenstedt G., Wong D.H., Koepp D.M., Silver P.A. Mutants in a yeast Ran binding protein are defective in nuclear transport. EMBO J. 14:1995;5367-5378.
    • (1995) EMBO J. , vol.14 , pp. 5367-5378
    • Schlenstedt, G.1    Wong, D.H.2    Koepp, D.M.3    Silver, P.A.4
  • 14
    • 0345647103 scopus 로고    scopus 로고
    • RanBP1 is crucial for the release of RanGTP from importin-beta-related nuclear transport factors
    • Bischoff F.R., Gorlich D. RanBP1 is crucial for the release of RanGTP from importin-beta-related nuclear transport factors. FEBS Lett. 419:1997;249-254.
    • (1997) FEBS Lett. , vol.419 , pp. 249-254
    • Bischoff, F.R.1    Gorlich, D.2
  • 15
    • 0037192461 scopus 로고    scopus 로고
    • Visualization of a RanGTP gradient in interphase and mitotic Xenopus egg extracts
    • The authors used biosensors to visualize Ran-GTP. They demonstrate that a steep Ran-GTP gradient exists between the cytoplasm and nucleus and that Ran-GTP is concentrated around mitotic chromatin. This is the first experimental evidence for the existence of the Ran-GTP gradient.
    • Kalab P., Weis K., Heald R. Visualization of a RanGTP gradient in interphase and mitotic Xenopus egg extracts. Science. 295:2002;2452-2456 The authors used biosensors to visualize Ran-GTP. They demonstrate that a steep Ran-GTP gradient exists between the cytoplasm and nucleus and that Ran-GTP is concentrated around mitotic chromatin. This is the first experimental evidence for the existence of the Ran-GTP gradient.
    • (2002) Science , vol.295 , pp. 2452-2456
    • Kalab, P.1    Weis, K.2    Heald, R.3
  • 16
    • 0037119367 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer biosensors that detect Ran conformational changes and a Ran x GDP-importin-beta-RanBP1 complex in vitro and in intact cells
    • The authors use fluorescent resonance energy transfer to analyze the conformation of the carboxyl terminus of Ran. They demonstrate that the carboxyl terminus of Ran does not re-orient when Ran-GDP is converted to Ran-GTP. In addition, they provide the first in vivo evidence for a ternary complex between importin-β, Ran-GTP and Ran binding protein 1.
    • Plafker K., Macara I.G. Fluorescence resonance energy transfer biosensors that detect Ran conformational changes and a Ran x GDP-importin-beta-RanBP1 complex in vitro and in intact cells. J. Biol. Chem. 277:2002;30121-30127 The authors use fluorescent resonance energy transfer to analyze the conformation of the carboxyl terminus of Ran. They demonstrate that the carboxyl terminus of Ran does not re-orient when Ran-GDP is converted to Ran-GTP. In addition, they provide the first in vivo evidence for a ternary complex between importin-β, Ran-GTP and Ran binding protein 1.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30121-30127
    • Plafker, K.1    Macara, I.G.2
  • 17
    • 0029847386 scopus 로고    scopus 로고
    • RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import
    • Chi N.C., Adam E.J., Visser G.D., Adam S.A. RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import. J. Cell Biol. 135:1996;559-569.
    • (1996) J. Cell Biol. , vol.135 , pp. 559-569
    • Chi, N.C.1    Adam, E.J.2    Visser, G.D.3    Adam, S.A.4
  • 19
    • 0035911152 scopus 로고    scopus 로고
    • The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins
    • The authors identified a nuclear import pathway mediated by Kap142p/Msn5p, a protein that was previously shown to act as an export receptor for trimeric replication protein A. This is the first report of a single transport receptor functioning as both an import and an export receptor.
    • Yoshida K., Blobel G. The karyopherin Kap142p/Msn5p mediates nuclear import and nuclear export of different cargo proteins. J. Cell Biol. 152:2001;729-740 The authors identified a nuclear import pathway mediated by Kap142p/Msn5p, a protein that was previously shown to act as an export receptor for trimeric replication protein A. This is the first report of a single transport receptor functioning as both an import and an export receptor.
    • (2001) J. Cell Biol. , vol.152 , pp. 729-740
    • Yoshida, K.1    Blobel, G.2
  • 20
    • 0035898685 scopus 로고    scopus 로고
    • Importin 13: A novel mediator of nuclear import and export
    • The authors identify importin-13 as a novel import receptor for RNA-binding motif protein 8 and the SUMO-1-conjugating enzyme hUBC9. In addition, they demonstrate that this novel importer can act as an export receptor for eIF1A, indicating that bi-directional transport by a single receptor can occur.
    • Mingot J.M., Kostka S., Kraft R., Hartmann E., Gorlich D. Importin 13: a novel mediator of nuclear import and export. EMBO J. 20:2001;3685-3694 The authors identify importin-13 as a novel import receptor for RNA-binding motif protein 8 and the SUMO-1-conjugating enzyme hUBC9. In addition, they demonstrate that this novel importer can act as an export receptor for eIF1A, indicating that bi-directional transport by a single receptor can occur.
    • (2001) EMBO J. , vol.20 , pp. 3685-3694
    • Mingot, J.M.1    Kostka, S.2    Kraft, R.3    Hartmann, E.4    Gorlich, D.5
  • 21
    • 0032522343 scopus 로고    scopus 로고
    • Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p
    • Senger B., Simos G., Bischoff F.R., Podtelejnikov A., Mann M., Hurt E. Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p. EMBO J. 17:1998;2196-2207.
    • (1998) EMBO J. , vol.17 , pp. 2196-2207
    • Senger, B.1    Simos, G.2    Bischoff, F.R.3    Podtelejnikov, A.4    Mann, M.5    Hurt, E.6
  • 22
    • 0033612576 scopus 로고    scopus 로고
    • Nuclear import of the TATA-binding protein: Mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting
    • Pemberton L.F., Rosenblum J.S., Blobel G. Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting. J. Cell Biol. 145:1999;1407-1417.
    • (1999) J. Cell Biol. , vol.145 , pp. 1407-1417
    • Pemberton, L.F.1    Rosenblum, J.S.2    Blobel, G.3
  • 23
    • 0035954439 scopus 로고    scopus 로고
    • Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export
    • The authors show that Ran binding protein 3 (RanBP3) acts as a cofactor for Crm1-mediated nuclear protein export, and propose a model where RanBP3 interacts with nuclear Crm1 and Ran-GTP to facilitate cargo loading. This is the first evidence for cofactors in nucleocytoplasmic transport.
    • Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G. Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J. Cell Biol. 153:2001;1391-1402 The authors show that Ran binding protein 3 (RanBP3) acts as a cofactor for Crm1-mediated nuclear protein export, and propose a model where RanBP3 interacts with nuclear Crm1 and Ran-GTP to facilitate cargo loading. This is the first evidence for cofactors in nucleocytoplasmic transport.
    • (2001) J. Cell Biol. , vol.153 , pp. 1391-1402
    • Lindsay, M.E.1    Holaska, J.M.2    Welch, K.3    Paschal, B.M.4    Macara, I.G.5
  • 24
    • 0034760338 scopus 로고    scopus 로고
    • RanBP3 influences interactions between CRM1 and its nuclear protein export substrates
    • Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U. RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2:2001;926-932.
    • (2001) EMBO Rep. , vol.2 , pp. 926-932
    • Englmeier, L.1    Fornerod, M.2    Bischoff, F.R.3    Petosa, C.4    Mattaj, I.W.5    Kutay, U.6
  • 25
    • 0037047430 scopus 로고    scopus 로고
    • Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import
    • The authors identify the nucleoporin NUP50 as a cofactor for importin-α/β nuclear import and rename this protein Npap60. They demonstrate that Npap60 acts as a tri-stable switch that changes its binding to importin-β to facilitate translocation of the Npap60-importin-β-importin-α-cargo complex through the nuclear pore complex.
    • Lindsay M.E., Plafker K., Smith A.E., Clurman B.E., Macara I.G. Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import. Cell. 110:2002;349-360 The authors identify the nucleoporin NUP50 as a cofactor for importin-α/β nuclear import and rename this protein Npap60. They demonstrate that Npap60 acts as a tri-stable switch that changes its binding to importin-β to facilitate translocation of the Npap60-importin-β-importin-α-cargo complex through the nuclear pore complex.
    • (2002) Cell , vol.110 , pp. 349-360
    • Lindsay, M.E.1    Plafker, K.2    Smith, A.E.3    Clurman, B.E.4    Macara, I.G.5
  • 27
    • 0035830499 scopus 로고    scopus 로고
    • Running on Ran: Nuclear transport and the mitotic spindle
    • Dasso M. Running on Ran: nuclear transport and the mitotic spindle. Cell. 104:2001;321-324.
    • (2001) Cell , vol.104 , pp. 321-324
    • Dasso, M.1
  • 28
    • 17744380396 scopus 로고    scopus 로고
    • Ran induces spindle assembly by reversing the inhibitory effect of importin on TPX2 activity
    • The authors identify the microtubule-associated protein TPX2 as a downstream intermediate in Ran-GTP-mediated spindle assembly. They demonstrate that TPX2 binds to importin-α in the absence of Ran-GTP, inhibiting microtubule assembly.
    • Gruss O.J., Carazo-Salas R.E., Schatz C.A., Guarguaglini G., Kast K., Wilm M., Le Bot N., Vernos I., Karsenti E., Mattaj I.W. Ran induces spindle assembly by reversing the inhibitory effect of importin on TPX2 activity. Cell. 104:2001;83-93 The authors identify the microtubule-associated protein TPX2 as a downstream intermediate in Ran-GTP-mediated spindle assembly. They demonstrate that TPX2 binds to importin-α in the absence of Ran-GTP, inhibiting microtubule assembly.
    • (2001) Cell , vol.104 , pp. 83-93
    • Gruss, O.J.1    Carazo-Salas, R.E.2    Schatz, C.A.3    Guarguaglini, G.4    Kast, K.5    Wilm, M.6    Le Bot, N.7    Vernos, I.8    Karsenti, E.9    Mattaj, I.W.10
  • 29
    • 0035951480 scopus 로고    scopus 로고
    • Role of importin-beta in coupling Ran to downstream targets in microtubule assembly
    • The authors demonstrate that importin-β inhibits microtubule aster assembly in Xenopus egg extracts by binding to the microtubule-binding protein NuMA. They also show that Ran regulates the interaction between importin-β and NuMA.
    • Wiese C., Wilde A., Moore M.S., Adam S.A., Merdes A., Zheng Y. Role of importin-beta in coupling Ran to downstream targets in microtubule assembly. Science. 291:2001;653-656 The authors demonstrate that importin-β inhibits microtubule aster assembly in Xenopus egg extracts by binding to the microtubule-binding protein NuMA. They also show that Ran regulates the interaction between importin-β and NuMA.
    • (2001) Science , vol.291 , pp. 653-656
    • Wiese, C.1    Wilde, A.2    Moore, M.S.3    Adam, S.A.4    Merdes, A.5    Zheng, Y.6
  • 30
    • 0035846901 scopus 로고    scopus 로고
    • Importin beta is a mitotic target of the small GTPase Ran in spindle assembly
    • The authors provide evidence that importin-β binds and inhibits multiple cargoes that are required for microtubule polymerization. They identified the microtubule-associated protein NuMA as one such cargo and demonstrate that the inhibition by importin-β is regulated by Ran-GTP.
    • Nachury M.V., Maresca T.J., Salmon W.C., Waterman-Storer C.M., Heald R., Weis K. Importin beta is a mitotic target of the small GTPase Ran in spindle assembly. Cell. 104:2001;95-106 The authors provide evidence that importin-β binds and inhibits multiple cargoes that are required for microtubule polymerization. They identified the microtubule-associated protein NuMA as one such cargo and demonstrate that the inhibition by importin-β is regulated by Ran-GTP.
    • (2001) Cell , vol.104 , pp. 95-106
    • Nachury, M.V.1    Maresca, T.J.2    Salmon, W.C.3    Waterman-Storer, C.M.4    Heald, R.5    Weis, K.6
  • 32
    • 0034631960 scopus 로고    scopus 로고
    • The Xenopus laevis Aurora/Ip11p-related kinase pEg2 participates in the stability of the bipolar mitotic spindle
    • Giet R., Prigent C. The Xenopus laevis Aurora/Ip11p-related kinase pEg2 participates in the stability of the bipolar mitotic spindle. Exp. Cell Res. 258:2000;145-151.
    • (2000) Exp. Cell Res. , vol.258 , pp. 145-151
    • Giet, R.1    Prigent, C.2
  • 34
    • 0036006303 scopus 로고    scopus 로고
    • The GTPase Ran regulates chromosome positioning and nuclear envelope assembly in vivo
    • The authors use RNA interference (RNAi) in C. elegans to analyze the in vivo role of Ran and its effector proteins. They demonstrate that the Ran GTPase cycle is required for correct chromosome positioning and nuclear envelope assembly.
    • Bamba C., Bobinnec Y., Fukuda M., Nishida E. The GTPase Ran regulates chromosome positioning and nuclear envelope assembly in vivo. Curr. Biol. 12:2002;503-507 The authors use RNA interference (RNAi) in C. elegans to analyze the in vivo role of Ran and its effector proteins. They demonstrate that the Ran GTPase cycle is required for correct chromosome positioning and nuclear envelope assembly.
    • (2002) Curr. Biol. , vol.12 , pp. 503-507
    • Bamba, C.1    Bobinnec, Y.2    Fukuda, M.3    Nishida, E.4
  • 35
    • 0036911347 scopus 로고    scopus 로고
    • Ran GTPase cycle and importins alpha and beta are essential for spindle formation and nuclear envelope assembly in living Caenorhabditis elegans embryos
    • The authors use RNA interference (RNAi) to investigate the role of the Ran GTPase cycle in C. elegans embryos. Reducing the levels of Ran, Ran binding protein 2, Ran GTPase-activating protein and RCC1 disrupts spindle formation and nuclear envelope reformation. The authors also use RNAi to reduce the levels of importin-α and -β. They observe similar phenotypes as those seen with Ran and its effectors, suggesting that Ran is affecting spindle assembly and nuclear envelope reformation in a manner analogous to its role in nucleocytoplasmic transport.
    • Askjaer P., Galy V., Hannak E., Mattaj I.W. Ran GTPase cycle and importins alpha and beta are essential for spindle formation and nuclear envelope assembly in living Caenorhabditis elegans embryos. Mol. Biol. Cell. 13:2002;4355-4370 The authors use RNA interference (RNAi) to investigate the role of the Ran GTPase cycle in C. elegans embryos. Reducing the levels of Ran, Ran binding protein 2, Ran GTPase-activating protein and RCC1 disrupts spindle formation and nuclear envelope reformation. The authors also use RNAi to reduce the levels of importin-α and -β. They observe similar phenotypes as those seen with Ran and its effectors, suggesting that Ran is affecting spindle assembly and nuclear envelope reformation in a manner analogous to its role in nucleocytoplasmic transport.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4355-4370
    • Askjaer, P.1    Galy, V.2    Hannak, E.3    Mattaj, I.W.4
  • 36
    • 0037046808 scopus 로고    scopus 로고
    • Ran localizes around the microtubule spindle in vivo during mitosis in Drosophila embryos
    • The authors examine the localization of RCC1 and Ran in Drosophila embryos. During mitosis, RCC1 localizes to chromatin and Ran localizes around mitotic spindles.
    • Trieselmann N., Wilde A. Ran localizes around the microtubule spindle in vivo during mitosis in Drosophila embryos. Curr. Biol. 12:2002;1124-1129 The authors examine the localization of RCC1 and Ran in Drosophila embryos. During mitosis, RCC1 localizes to chromatin and Ran localizes around mitotic spindles.
    • (2002) Curr. Biol. , vol.12 , pp. 1124-1129
    • Trieselmann, N.1    Wilde, A.2
  • 37
    • 0037143453 scopus 로고    scopus 로고
    • Targeting of RCC1 to chromosomes is required for proper mitotic spindle assembly in human cells
    • Moore W., Zhang C., Clarke P.R. Targeting of RCC1 to chromosomes is required for proper mitotic spindle assembly in human cells. Curr. Biol. 12:2002;1442-1447.
    • (2002) Curr. Biol. , vol.12 , pp. 1442-1447
    • Moore, W.1    Zhang, C.2    Clarke, P.R.3
  • 38
    • 0036724599 scopus 로고    scopus 로고
    • Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex
    • Zhang H., Saitoh H., Matunis M.J. Enzymes of the SUMO modification pathway localize to filaments of the nuclear pore complex. Mol. Cell Biol. 22:2002;6498-6508.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6498-6508
    • Zhang, H.1    Saitoh, H.2    Matunis, M.J.3
  • 39
    • 0035909896 scopus 로고    scopus 로고
    • A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim
    • Rose A., Meier I. A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim. Proc. Natl. Acad Sci. USA. 98:2001;15377-15382.
    • (2001) Proc. Natl. Acad Sci. USA , vol.98 , pp. 15377-15382
    • Rose, A.1    Meier, I.2
  • 40
    • 0037162398 scopus 로고    scopus 로고
    • The Ran GTPase: Theme and variations
    • Dasso M. The Ran GTPase: theme and variations. Curr. Biol. 12:2002;R502-508.
    • (2002) Curr. Biol. , vol.12 , pp. 502-508
    • Dasso, M.1
  • 42
    • 0034717035 scopus 로고    scopus 로고
    • Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts
    • Zhang C., Clarke P.R. Chromatin-independent nuclear envelope assembly induced by Ran GTPase in Xenopus egg extracts. Science. 288:2000;1429-1432.
    • (2000) Science , vol.288 , pp. 1429-1432
    • Zhang, C.1    Clarke, P.R.2
  • 43
    • 0036006299 scopus 로고    scopus 로고
    • Role of importin-beta in the control of nuclear envelope assembly by Ran
    • The authors show that importin-β attached to beads can support nuclear envelope assembly and that the ability of importin-β to bind to nuclear pore proteins is necessary for this to occur.
    • Zhang C., Hutchins J.R., Muhlhausser P., Kutay U., Clarke P.R. Role of importin-beta in the control of nuclear envelope assembly by Ran. Curr. Biol. 12:2002;498-502 The authors show that importin-β attached to beads can support nuclear envelope assembly and that the ability of importin-β to bind to nuclear pore proteins is necessary for this to occur.
    • (2002) Curr. Biol. , vol.12 , pp. 498-502
    • Zhang, C.1    Hutchins, J.R.2    Muhlhausser, P.3    Kutay, U.4    Clarke, P.R.5
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    • 0035128451 scopus 로고    scopus 로고
    • Roles of Ran-GTP and Ran-GDP in precursor vesicle recruitment and fusion during nuclear envelope assembly in a human cell-free system
    • Zhang C., Clarke P.R. Roles of Ran-GTP and Ran-GDP in precursor vesicle recruitment and fusion during nuclear envelope assembly in a human cell-free system. Curr. Biol. 11:2001;208-212.
    • (2001) Curr. Biol. , vol.11 , pp. 208-212
    • Zhang, C.1    Clarke, P.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.