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.

In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.

NMR spectroscopy has been used to explain a central unresolved issue of nuclear transport, namely how it can be both fast and specific.

ESCRT-driven mechanisms that sense and seal holes in the nuclear membranes directly monitor the nuclear transport system and the exposure of the inner nuclear membrane.

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.

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.

Animal RanBP1 nuclear export and cargo dissociation mechanisms are surprisingly different from yeast, due to mutations of critical residues, leading to greater nuclear transport efficiency and higher energy cost.

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

Activation of the subthalamic nucleus (STN) pauses or disrupts behavior, while STN inhibition reduces the disruptive effects of surprise, indicating that STN activation is both sufficient and necessary for behavioral inhibition.

Slx9 is a newly discovered type of RanGTP-binding protein required for Crm1-mediated nuclear export.