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Transport receptor occupancy in nuclear pore complex mimics

Nano Research 2022年第11期15卷 9689-9703页

作者： Alessio Fragasso Hendrik W.de Vries John Andersson eli ovan der sluis Erik van der Giessen Patrick R.Onck Cees Dekker Department of Bionanoscience Kavli Institute of NanoscienceDelft University of TechnologyVan der Maasweg 9Delft 2629 HZThe Netherlands Zernike Institute for Advanced Materials University of GroningenNijenborgh 4Groningen 9747AGThe Netherlands Department of Chemistry and Chemical Engineering Chalmers University of TechnologyKemivägen 10Gothenburg SE-41296Sweden

Nuclear pore complexes(NPCs)regulate all molecular transport between the nucleus and the cytoplasm in eukaryotic *** disordered Phe-Gly nucleoporins(FG-Nups)line the central conduit of NPCs to impart a selective barrier where large proteins are excluded unless bound to a transport receptor(karyopherin;Kap).Here,we assess“Kap-centric”NPC models,which postulate that Kaps participate in establishing the selective *** combine biomimetic nanopores,formed by tethering Nsp1 to the inner wall of a solid-state nanopore,with coarse-grained modeling to show that yeast Kap95 exhibits two populations in Nsp1-coated pores:one population that is transported across the pore in milliseconds,and a second population that is stably assembled within the FG mesh of the *** current measurements show a conductance decrease for increasing Kap concentrations and noise data indicate an increase in rigidity of the *** reveals an accumulation of Kap95 near the pore wall,yielding a conductance *** find that Kaps only mildly affect the conformation of the Nsp1 mesh and that,even at high concentrations,Kaps only bind at most 8%of the FG-motifs in the nanopore,indicating that Kap95 occupancy is limited by steric constraints rather than by depletion of available *** data provide an alternative explanation of the origin of bimodal NPC binding of Kaps,where a stable population of Kaps binds avidly to the NPC periphery,while fast transport proceeds via a central FG-rich channel through lower affinity interactions between Kaps and the cohesive domains of Nsp1.

关键词： nuclear pore complex intrinsically disordered proteins nuclear transport receptors karyopherins nanopores biomimetics molecular dynamics coarse-grained modeling

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