Poly-PR and poly-GR interact with importin β, disrupt importin-cargo loading, and inhibit nuclear import in permeabilized cells in a manner that can be rescued by RNA.

HIV-1 Vpr antagonises innate immune sensing of viral and non-viral stimuli by preventing activated IRF3 and NF-κB nuclear transport.

Structural and biochemical studies of Kap123 revealed the mechanisms by which Kap123 recognizes H3- and H4-NLSs through two lysine-binding pockets and by which evolutionarily conserved diacetylation of H4-NLS facilitates Kap123-H3-NLS mediated nuclear translocation.

Genetic and proteomic screening with Wolbachia's CidB enzyme reveal the mechanisms and targets of cytoplasmic incompatibility (CI).

Polarized fluorescence microscopy of individual nuclear pores in vivo reveals conformational changes in select domains of proteins of the inner ring.

The 24 ankyrin repeats of ankyrin proteins form an extended solenoid that provides an extremely conserved groove for binding to numerous targets via combinatorial usage of multiple weak interaction sites.

In an unusual complex that is not dissociated by RanGTP alone, Importin-9 sequesters the H2A-H2B core from promiscuous interactions.

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.

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.

Simple biophysical considerations explain the collective behavior of molecularly diverse complex protein assemblies that regulate transport between the nucleus and the cytoplasm in eukaryotic organisms.