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

A member of the Drosophila Nuclear Export Factor (Nxf) family, Nxf2, forms part of the piRNA-dependent co-transcriptional silencing complex and is essential for transposon repression in fly ovaries.

The nuclear export receptor Crm1 cooperatively binds its HIV Rev-RRE cargo as a dimer using a species-specific interface that supports viral replication by enhancing nuclear export of HIV RNA.

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

Ubp15 regulates the ubiquitylation of the export adaptor Mex67.

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.

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.

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.

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