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.

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.

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.

Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.

YTHDC1 facilitates selective clearance of N6-methyladenosine methylated mRNAs from the nucleus to the cytoplasm through binding by nuclear 'reader' proteins and incorporation into the canonical mRNA export pathway.

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.

Within the nucleus, Dbp5p supports tRNA export providing a parallel mechanism by which this conserved DEAD-box protein functions to support eukaryotic gene expression.

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

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

The Toxoplasma parasite requires an enzyme called ASP5 to cleave proteins for export into host cells.