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Journal Article

A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.

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;

External Ressource
Fulltext (public)

2307026.pdf
(Publisher version), 2MB

Supplementary Material (public)

2307026_Suppl.pdf
(Supplementary material), 6MB

Citation

Zahn, R., Osmanovic, D., Ehret, S., Callis, C. A., Frey, S., Stewart, M., et al. (2016). A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies. eLife, 5: e14119. doi:10.7554/eLife.14119.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002A-EE01-7
Abstract
The permeability barrier of nuclear pore complexes (NPCs) controls bulk nucleocytoplasmic exchange. It consists of nucleoporin domains rich in phenylalanine-glycine motifs (FG domains). As a bottom-up nanoscale model for the permeability barrier, we have used planar films produced with three different end-grafted FG domains, and quantitatively analyzed the binding of two different nuclear transport receptors (NTRs), NTF2 and Importin beta, together with the concomitant film thickness changes. NTR binding caused only moderate changes in film thickness; the binding isotherms showed negative cooperativity and could all be mapped onto a single master curve. This universal NTR binding behavior a key element for the transport selectivity of the NPC was quantitatively reproduced by a physical model that treats FG domains as regular, flexible polymers, and NTRs as spherical colloids with a homogeneous surface, ignoring the detailed arrangement of interaction sites along FG domains and on the NTR surface.