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.

The Tsr2 carrier protein connects the nuclear import machinery with the ribosome assembly pathway.

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.

Cellular and genetic approaches reveal that exposure of a normally buried nuclear export signal (NES)-like sequence mediates export of ALS-linked mutant and misfolded wild-type SOD1 to the cytoplasm by CRM1.

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

The stimulation of lipopolysaccharides induced nuclear localization of IRAK2 to facilitate nuclear export of a specific subset of inflammation-related messenger RNAs for translation in murine macrophages.

Building on previous work (Fung et al., 2015), the structures of eight new nuclear export signal (NES) peptides bound to Exportin CRM1 are reported, revealing striking diversity in NES structures, a small conserved secondary structural element, and a CRM1 residue that functions as a selectivity filter.

A major cytoplasmic chaperone, Ssa2p, acts as a nuclear import carrier for tRNAs upon nutrient starvation in Saccharomyces cerevisiae.

Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.

Interaction of HIV capsids with the cellular protein cleavage-and-polyadenylation factor 6 at the inner side of nuclear pores promotes nuclear entry of the viral replication complex in primary human macrophages.