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- W2022506021 abstract "The permeability barrier of nuclear pore complexes (NPCs) controls the exchange between nucleus and cytoplasm. It suppresses the flux of inert macromolecules > or = 30 kDa but allows rapid passage of even very large cargoes, provided these are bound to appropriate nuclear transport receptors. We show here that a saturated hydrogel formed by a single nucleoporin FG-repeat domain is sufficient to reproduce the permeability properties of NPCs. Importin beta and related nuclear transport receptors entered such hydrogel >1000x faster than a similarly sized inert macromolecule. The FG-hydrogel even reproduced import signal-dependent and importin-mediated cargo influx, allowing importin beta to accelerate the gel entry of a large cognate cargo more than 20,000-fold. Intragel diffusion of the importin beta-cargo complex occurred rapidly enough to traverse an NPC within approximately 12 ms. We extend the selective phase model to explain these effects." @default.
- W2022506021 created "2016-06-24" @default.
- W2022506021 creator A5033345296 @default.
- W2022506021 creator A5048192188 @default.
- W2022506021 date "2007-08-01" @default.
- W2022506021 modified "2023-10-17" @default.
- W2022506021 title "A Saturated FG-Repeat Hydrogel Can Reproduce the Permeability Properties of Nuclear Pore Complexes" @default.
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- W2022506021 doi "https://doi.org/10.1016/j.cell.2007.06.024" @default.
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