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

Zahn, R; Osmanović, D; Ehret, S; Araya Callis, C; Frey, S; Stewart, M; You, C; ... Richter, RP; + view all (2016) A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies. Elife , 5 , Article e14119. 10.7554/eLife.14119. Green open access

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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 β, 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.

Type: Article
Title: A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies
Location: England
Open access status: An open access version is available from UCL Discovery
DOI: 10.7554/eLife.14119
Publisher version: http://dx.doi.org/10.7554/eLife.14119
Additional information: © Copyright Zahn et al. This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.
Keywords: biophysics, computational modeling, intrinsically disordered proteins, none, nuclear transport receptor, nucleo-cytoplasmic transport, quartz crystal microbalance, spectroscopic ellipsometry, structural biology
UCL classification: UCL
UCL > Provost and Vice Provost Offices > UCL BEAMS
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences
UCL > Provost and Vice Provost Offices > UCL BEAMS > Faculty of Maths and Physical Sciences > Dept of Physics and Astronomy
URI: https://discovery-pp.ucl.ac.uk/id/eprint/1479817
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