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A designer FG-Nup that reconstitutes the selective transport barrier of the Nuclear Pore Complex

View ORCID ProfileAlessio Fragasso, View ORCID ProfileHendrik W. de Vries, View ORCID ProfileEli O. van der Sluis, View ORCID ProfileErik van der Giessen, View ORCID ProfilePatrick R. Onck, View ORCID ProfileCees Dekker
doi: https://doi.org/10.1101/2020.02.04.933994
Alessio Fragasso
1Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
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  • ORCID record for Alessio Fragasso
Hendrik W. de Vries
2Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands
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Eli O. van der Sluis
1Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
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Erik van der Giessen
2Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands
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Patrick R. Onck
2Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands
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  • For correspondence: p.r.onck@rug.nl c.dekker@tudelft.nl
Cees Dekker
1Department of Bionanoscience, Kavli Institute of Nanoscience, Delft University of Technology, Van der Maasweg 9, 2629 HZ Delft, The Netherlands
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  • For correspondence: p.r.onck@rug.nl c.dekker@tudelft.nl
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Abstract

Nuclear Pore Complexes (NPCs) regulate bidirectional transport between the nucleus and the cytoplasm. Intrinsically disordered FG-Nups line the NPC lumen and form a selective barrier, where transport of most proteins is inhibited whereas specific transporter proteins freely pass. The mechanism underlying selective transport through the NPC is still debated. Here, we reconstitute the selective behaviour of the NPC bottom-up by introducing a rationally designed artificial FG-Nup that mimics natural Nups. Using QCM-D, we measure a strong affinity of the artificial FG-Nup brushes to the transport receptor Kap95, whereas no binding occurs to cytosolic proteins such as BSA. Solid-state nanopores with the artificial FG-Nups lining their inner walls support fast translocation of Kap95 while blocking BSA, thus demonstrating selectivity. Coarse-grained molecular dynamics simulations highlight the formation of a selective meshwork with densities comparable to native NPCs. Our findings show that simple design rules can recapitulate the selective behaviour of native FG-Nups and demonstrate that no specific spacer sequence nor a spatial segregation of different FG-motif types are needed to create functional NPCs.

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Posted February 04, 2020.
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A designer FG-Nup that reconstitutes the selective transport barrier of the Nuclear Pore Complex
Alessio Fragasso, Hendrik W. de Vries, Eli O. van der Sluis, Erik van der Giessen, Patrick R. Onck, Cees Dekker
bioRxiv 2020.02.04.933994; doi: https://doi.org/10.1101/2020.02.04.933994
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A designer FG-Nup that reconstitutes the selective transport barrier of the Nuclear Pore Complex
Alessio Fragasso, Hendrik W. de Vries, Eli O. van der Sluis, Erik van der Giessen, Patrick R. Onck, Cees Dekker
bioRxiv 2020.02.04.933994; doi: https://doi.org/10.1101/2020.02.04.933994

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