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.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.

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.

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.

Protein aggregates resulting from mutations in C9orf72 impair different aspects of cellular quality control in the cytosol and the nucleus, but mRNA-mediated effects contribute more strongly to toxicity.

KPNB1 regulates rhythmic spatio-temporal nuclear import of the PER/CRY complex and is required for negative feedback repression in mammalian and fly clock function.

How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.

T-cell receptor signaling actively regulates gating of the nuclear pore complex (NPC) in T cells by inducing translocation of protein kinase C-θ to the NPC to promote the sumoylation of RanGAP1.

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.

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.