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This paper established the role of NTF2. It was the first paper to clearly demonstrate that Ran is recycled after each round of nuclear transport by NTF2, a Ran-GDP-binding protein that is essential for nuclear transport.
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Ribbeck K., Lipowsky G., Kent H.M., Stewart M., Gorlich D. NTF2 mediates nuclear import of Ran. EMBO J. 17:1998;6587-6598. This paper established the role of NTF2. It was the first paper to clearly demonstrate that Ran is recycled after each round of nuclear transport by NTF2, a Ran-GDP-binding protein that is essential for nuclear transport.
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Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
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This report provides crystal structures for the importin-β-Ran-GppNHp complex. This reports provides insight into the capacity of Ran-GTP, but not Ran-GDP, to bind to transport receptors, as well as to the capacity of this complex to interact with RanBP1.
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Chook Y.M., Blobel G. Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature. 399:1999;230-237. This report provides crystal structures for the importin-β-Ran-GppNHp complex. This reports provides insight into the capacity of Ran-GTP, but not Ran-GDP, to bind to transport receptors, as well as to the capacity of this complex to interact with RanBP1.
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Nature
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Chi N.C., Adam E.J.H., Adam S.A. Different binding domains for Ran-GTP and Ran-GDP/RanBP1 on nuclear import factor p97. J Biol Chem. 272:1997;6818-6822.
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Structural view of the Ran-importin beta interaction at 2.3 A resolution
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The crystal structure of rna1p: A new fold for a GTPase-activating protein
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Hillig R.C., Renault L., Vetter I.R., Drell T., Wittinghofer A., Becker J. The crystal structure of rna1p: a new fold for a GTPase-activating protein. Mol Cell. 3:1999;781-791.
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RanBP1 is crucial for the release of RanGTP from importin beta-related nuclear transport factors
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This paper reports the crystal structure of the complex containing Ran and an isolated Ran-binding domain of RanBP2, as well as information regarding the conformational changes from the GDP-bound to the GppNHp-bound form of Ran. This information has been essential for modelling the interactions of RanBP1 with the switch I domain of Ran.
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Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A. Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. Nature. 398:1999;39-46. This paper reports the crystal structure of the complex containing Ran and an isolated Ran-binding domain of RanBP2, as well as information regarding the conformational changes from the GDP-bound to the GppNHp-bound form of Ran. This information has been essential for modelling the interactions of RanBP1 with the switch I domain of Ran.
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Vetter, I.R.1
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Stewart M., Kent H.M., McCoy A.J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J Mol Biol. 277:1998;635-646.
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The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
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Renault L., Nassar N., Vetter I., Becker J., Klebe C., Roth M., Wittinghofer A. The 1.7 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature. 392:1998;97-101.
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22
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0032522343
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Mtr10p functions as a nuclear import receptor for the mRNA-binding protein Npl3p
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This paper documents that Mtr10p is the transport receptor for the RNA-binding protein Npl3p. It demonstrates that Npl3p dissociates from Mtr10p only in the presence of both Ran-GTP and RNA. These results suggest that the release of some transport substrates may be dependent upon their association with the correct macromolecular complexes within nuclei.
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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. This paper documents that Mtr10p is the transport receptor for the RNA-binding protein Npl3p. It demonstrates that Npl3p dissociates from Mtr10p only in the presence of both Ran-GTP and RNA. These results suggest that the release of some transport substrates may be dependent upon their association with the correct macromolecular complexes within nuclei.
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Senger, B.1
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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.
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The direction of transport through the nuclear pore can be inverted
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This paper demonstrates that the vectorial nature of nuclear transport is derived from the gradient of Ran-GTP. Inversion of the gradient can invert direction of nucleocytoplasmic transport in the permeabilized cell transport assay.
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Nachury M.V., Weis K. The direction of transport through the nuclear pore can be inverted. Proc Natl Acad Sci USA. 96:1999;9622-9627. This paper demonstrates that the vectorial nature of nuclear transport is derived from the gradient of Ran-GTP. Inversion of the gradient can invert direction of nucleocytoplasmic transport in the permeabilized cell transport assay.
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Ribbeck K., Kutay U., Paraskeva E., Gorlich D. The translocation of transportin-cargo complexes through nuclear pores is independent of both Ran and energy. Curr Biol. 9:1999;47-50.
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0033591373
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Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran
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This paper examines the role of Ran in spindle assembly. In particular, this paper documents that the asters induced by Ran-GTP contain centriolar proteins and form in a manner that is dependent upon many of the functions normally required for spindle assembly.
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Wilde A., Zheng Y. Stimulation of microtubule aster formation and spindle assembly by the small GTPase Ran. Science. 284:1999;1359-1362. This paper examines the role of Ran in spindle assembly. In particular, this paper documents that the asters induced by Ran-GTP contain centriolar proteins and form in a manner that is dependent upon many of the functions normally required for spindle assembly.
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Wilde, A.1
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0033591386
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Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran
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This paper examines the role of Ran in spindle assembly. In particular, it documents that RanGEF-depleted Xenopus egg extracts have defects in aster formation that can be restored through the addition of recombinant RanGEF.
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Ohba T., Nakamura M., Nishitani H., Nishimoto T. Self-organization of microtubule asters induced in Xenopus egg extracts by GTP-bound Ran. Science. 284:1999;1356-1358. This paper examines the role of Ran in spindle assembly. In particular, it documents that RanGEF-depleted Xenopus egg extracts have defects in aster formation that can be restored through the addition of recombinant RanGEF.
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The ran GTPase regulates mitotic spindle assembly
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This paper examines the role of Ran in spindle assembly. In particular, it documents that excess RanBP1 can disrupt spindle assembly, whereas RanGEF or RanG19V-GTPγS cause microtubule polymerization and the formation of asters and spindle-like structures.
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Kalab P., Pu R.T., Dasso M. The ran GTPase regulates mitotic spindle assembly. Curr Biol. 9:1999;481-484. This paper examines the role of Ran in spindle assembly. In particular, it documents that excess RanBP1 can disrupt spindle assembly, whereas RanGEF or RanG19V-GTPγS cause microtubule polymerization and the formation of asters and spindle-like structures.
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Kahana J.A., Cleveland D.W. Beyond nuclear transport. Ran-GTP as a determinant of spindle assembly. J Cell Biol. 146:1999;1205-1210. This paper gives a clear review of recent reports on the role of Ran in spindle assembly.
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