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

Raphael Zahn, Dino Osmanović, Severin Ehret, Carolina Araya Callis, Steffen Frey, Murray Stewart, Changjiang You, Dirk Görlich, Bart W. Hoogenboom, Ralf P. Richter

Research output: Contribution to journalArticlepeer-review

56 Scopus citations

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 b, 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.

Original languageEnglish
Article numbere14119
JournaleLife
Volume5
Issue numberAPRIL2016
DOIs
StatePublished - 8 Apr 2016

Bibliographical note

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© Zahn et al.

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