Ultrathin nucleoporin phenylalanine–glycine repeat films and their interaction with nuclear transport receptors

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Nuclear pore complexes (NPCs) are highly selective gates that mediate the exchange of all proteins and nucleic acids between the cytoplasm and the nucleus. Their selectivity relies on a supramolecular assembly of natively unfolded nucleoporin domains containing phenylalanine–glycine (FG)‐rich repeats (FG repeat domains), in a way that is at present poorly understood. We have developed ultrathin FG domain films that reproduce the mode of attachment and the density of FG repeats in NPCs, and that exhibit a thickness that corresponds to the nanoscopic dimensions of the native permeability barrier. By using a combination of biophysical characterization techniques, we quantified the binding of nuclear transport receptors (NTRs) to such FG domain films and analysed how this binding affects the swelling behaviour and mechanical properties of the films. The results extend our understanding of the interaction of FG domain assemblies with NTRs and contribute important information to refine the model of transport across the permeability barrier. To gain insight into the mechanisms behind transport of molecules across the nuclear pore complex, Richter and co‐workers have developed ultrathin films of nucleoporin FG repeat domains and quantify how these films bind dedicated shuttle molecules—the so‐called nuclear transport receptors (NTRs). They find that NTRs can efficiently permeate the films, but do not affect their global morphology, which suggests that the FG repeat domains form a dense meshwork of entangled or transiently crosslinked polymers.