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.

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.

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

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.

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 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.

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

Histone H3 can translocate to the nucleus as a monomer through a pathway governed by importin-5 and transfers to the histone chaperone NASP, having implications in the folding of H3-H4 dimers and, therefore, the kinetics of genome packaging during replication.

Advanced microscopy techniques reveal unique biological features that distinguish androgen receptor variant 7 (AR-V7) from the canonical AR, including high intranuclear mobility and rapid nuclear import that occurs independently of importin-α/β.