A homopolymer-sphere model is shown to accurately reproduce the interactions that underpin selective gating of macromolecular transport into and out of the cell nucleus.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

Computational modelling predicts spatial segregation of different types of nuclear transport receptors in assemblies of nuclear pore proteins, lending support to the idea of separate transport pathways in the nuclear pore complex as a way to enhance transport efficiency.

How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.

The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.

The Ran GTPase plays a role in defining the physical properties of the nuclear pore complex transport channel by remodeling the binding interactions of importin-β with the nucleoporin Nup153 at the nuclear face of the pore.

T-cell receptor signaling actively regulates gating of the nuclear pore complex (NPC) in T cells by inducing translocation of protein kinase C-θ to the NPC to promote the sumoylation of RanGAP1.

Some nuclear export signals (NESs) bind to the transport receptor CRM1 in the opposite orientation to those previously studied.

Transport-based high-throughput identification of cargo proteins specific to all 12 human importin-β family nuclear import receptors revealed biological processes that the cargo cohorts of each receptor are involved in.

Efficient nuclear transport of very large biomolecules, relevant for viral transport, scales non-linearly with size and its kinetics can be explained by a simple two-parameter energetic model.