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.

β-catenin, a key effector of the Wnt signaling pathway, is transported into the nucleus via a direct interaction between its PY-NLS and TNPO1 offering new potential targets for cancer therapeutics.

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.

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.

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.

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

The THAP-domain protein Bip1, along with other proteins Nup98 and RpS8, controls the expression of the protein Pvr, a critical non-cell-autonomous regulator of Drosophila blood progenitor maintenance.

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.

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.

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