Results 171 to 180 of about 3,517 (188)
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Analysis of a RanGTP-regulated gradient in mitotic somatic cells
Nature, 2006The RanGTPase cycle provides directionality to nucleocytoplasmic transport, regulating interactions between cargoes and nuclear transport receptors of the importin-beta family. The Ran-importin-beta system also functions in mitotic spindle assembly and nuclear pore and nuclear envelope formation.
Rebecca Heald, Karsten Weis, Arnd Pralle
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RanGTP regulates the augmin complex
2022SUMMARY Spindles are composed of microtubules that must nucleate at the right place and time during mitosis. Spindle microtubule nucleation is regulated by the GTPase Ran, which, through importin-αβ, releases a gradient of spindle assembly factors (SAFs) centered at chromosomes.
Jodi Kraus +3 more
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Structural basis for nuclear import complex dissociation by RanGTP
Nature, 2005Nuclear protein import is mediated mainly by the transport factor importin-beta that binds cytoplasmic cargo, most often via the importin-alpha adaptor, and then transports it through nuclear pore complexes. This active transport is driven by disassembly of the import complex by nuclear RanGTP.
Murray Stewart +2 more
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Nuclear RanGTP is not required for targeting small nucleolar RNAs to the nucleolus [PDF]
The small GTPase Ran is the central regulator of macromolecular transport between the cytoplasm and the nucleus. Recent work has suggested that RanGTP also plays an important role in regulating some intra-nuclear processes. In this study, we have investigated whether RanGTP is required for the intra-nuclear transport of RNAs.
Michael P Terns +2 more
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Disassembly of RanGTP-Karyopherin β Complex, an Intermediate in Nuclear Protein Import* [PDF]
We previously showed that RanGTP forms a 1:1 complex with karyopherin beta that renders RanGTP inaccessible to RanGAP (Floer, M., and Blobel, G. (1996) J. Biol. Chem. 271, 5313-5316) and karyopherin beta functionally inactive (Rexach, M., and Blobel, G. (1995) Cell 83, 683-692).
Günter Blobel
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The Role of RanGTP Gradient in Vertebrate Oocyte Maturation
2011The maturation of vertebrate oocyte into haploid gamete, the egg, consists of two specialized asymmetric cell divisions with no intervening S-phase. Ran GTPase has an essential role in relaying the active role of chromosomes in their own segregation by the meiotic process. In addition to its conserved role as a key regulator of macromolecular transport
Petr, Kaláb, Petr, Solc, Jan, Motlík
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The site of RanGTP generation can act as an organizational cue for mitotic microtubules
Biology of the Cell, 2011RanGTP, which is generated on chromosomes during mitosis, is required for microtubule spindle assembly. Due to its restricted spatial generation within the cell it has been suggested that RanGTP acts as a spatial cue to organize site-specific spindle assembly within the cell.
Andrew Wilde
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Hyperosmotic Stress Signaling to the Nucleus Disrupts the Ran Gradient and the Production of RanGTP [PDF]
The RanGTP gradient depends on nucleocytoplasmic shuttling of Ran and its nucleotide exchange in the nucleus. Here we show that hyperosmotic stress signaling induced by sorbitol disrupts the Ran protein gradient and reduces the production of RanGTP. Ran gradient disruption is rapid and is followed by early (10–20 min) and late (30–60 min) phases of ...
Paschal, Bryce M, Joshua B Kelley
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A Mitotic Lamin B Matrix Induced by RanGTP Required for Spindle Assembly
Science, 2006Mitotic spindle morphogenesis is a series of highly coordinated movements that lead to chromosome segregation and cytokinesis. We report that the intermediate filament protein lamin B, a component of the interphase nuclear lamina, functions in spindle assembly.
Ming-Ying, Tsai +6 more
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Human RanBP3, a group of nuclear RanGTP binding proteins.
FEBS letters, 1998A group of novel human Ran-binding proteins, RanBP3, was identified using the yeast two-hybrid system via Ran-mediated interaction with the nucleotide exchange factor RCC1. Several open reading frames, representing putative alternatively spliced products, were established by cDNA cloning.
L, Mueller +3 more
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