Journal
ELIFE
Volume 5, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.14119
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Funding
- European Commission [FP7-PEOPLE-2012-IEF-327975]
- European Research Council [FP7-ERC-2012-StG-306435]
- Dr. Mortimer and Theresa Sackler Foundation
- Deutsche Forschungsgemeinschaft [SFB 944]
- Medical Research Council [U105178939]
- Spanish Ministry for Economy and Competitiveness [MAT2011-24306]
- Medical Research Council [MC_U105178939] Funding Source: researchfish
- MRC [MC_U105178939] Funding Source: UKRI
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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.
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