title: A physical model describing the interaction of nuclear transport receptors with FG nucleoporin domain assemblies.
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.
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE, San Sebastian, Spain.
authors.forename: Raphael
authors.identifier: 0000-0003-0223-0697
authors.initials: R
authors.lastname: Zahn
authors.affiliation: London Centre for Nanotechnology, University College London, London, United Kingdom.|Department of Physics and Astronomy, University College London, London, United Kingdom.|Department of Physics, Bar-Ilan University, Ramat Gan, Israel.|Institute of Nanotechnology and Advanced Materials, Bar-Ilan University, Ramat Gan, Israel.
authors.forename: Dino
authors.initials: D
authors.lastname: Osmanović
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE, San Sebastian, Spain.
authors.forename: Severin
authors.initials: S
authors.lastname: Ehret
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE, San Sebastian, Spain.
authors.forename: Carolina
authors.initials: C
authors.lastname: Araya Callis
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Steffen
authors.initials: S
authors.lastname: Frey
authors.affiliation: Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
authors.forename: Murray
authors.initials: M
authors.lastname: Stewart
authors.affiliation: Department of Biology, University of Osnabrück, Osnabrück, Germany.
authors.forename: Changjiang
authors.initials: C
authors.lastname: You
authors.affiliation: Department of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany.
authors.forename: Dirk
authors.initials: D
authors.lastname: Görlich
authors.affiliation: London Centre for Nanotechnology, University College London, London, United Kingdom.|Department of Physics and Astronomy, University College London, London, United Kingdom.
authors.forename: Bart W
authors.identifier: 0000-0002-8882-4324
authors.initials: BW
authors.lastname: Hoogenboom
authors.affiliation: Biosurfaces Lab, CIC biomaGUNE, San Sebastian, Spain.|Laboratory of Interdisciplinary Physics, University Grenoble Alpes - CNRS, Grenoble, France.|Max-Planck-Institute for Intelligent Systems, Stuttgart, Germany.
authors.forename: Ralf P
authors.identifier: 0000-0003-3071-2837
authors.initials: RP
authors.lastname: Richter
mesh_terms: D021581:Active Transport, Cell Nucleus; D008954:Models, Biological; D029543:Nucleocytoplasmic Transport Proteins / Q000378:metabolism*; D011485:Protein Binding
chemical_list: D029543:Nucleocytoplasmic Transport Proteins
keywords: biophysics; computational modeling; intrinsically disordered proteins; none; nuclear transport receptor; nucleo-cytoplasmic transport; quartz crystal microbalance; spectroscopic ellipsometry; structural biology