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Journal Article

Ultrathin nucleoporin FG repeat films and their interaction with nuclear transport receptors.

MPS-Authors
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Frey,  S.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

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Görlich,  D.
Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

587724.pdf
(Publisher version), 875KB

Supplementary Material (public)

587724-Suppl.pdf
(Supplementary material), 2MB

Citation

Eisele, N. B., Frey, S., Piehler, J., Görlich, D., & Richter, R. P. (2010). Ultrathin nucleoporin FG repeat films and their interaction with nuclear transport receptors. EMBO Reports, 11(5), 366-372. doi:10.1038/embor.2010.34.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-D5CF-0
Abstract
Nuclear pore complexes (NPCs) are highly selective gates that mediate the exchange of all proteins and nucleic acids between the cytoplasm and the nucleus. Their selectivity relies on a supramolecular assembly of natively unfolded nucleoporin domains containing phenylalanine–glycine (FG)-rich repeats (FG repeat domains), in a way that is at present poorly understood. We have developed ultrathin FG domain films that reproduce the mode of attachment and the density of FG repeats in NPCs, and that exhibit a thickness that corresponds to the nanoscopic dimensions of the native permeability barrier. By using a combination of biophysical characterization techniques, we quantified the binding of nuclear transport receptors (NTRs) to such FG domain films and analysed how this binding affects the swelling behaviour and mechanical properties of the films. The results extend our understanding of the interaction of FG domain assemblies with NTRs and contribute important information to refine the model of transport across the permeability barrier.