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.

Structural and biochemical studies of Kap123 revealed the mechanisms by which Kap123 recognizes H3- and H4-NLSs through two lysine-binding pockets and by which evolutionarily conserved diacetylation of H4-NLS facilitates Kap123-H3-NLS mediated nuclear translocation.

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

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.

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.

Elevating FUS level by saturating autoregulation loop in mice causes aggressive motor neuron disease via disrupting protein and RNA homeostasis.

RNA processing regulates gene expression of the key transcription factor FOXP3 in T regulatory cells impacting immune tolerance and susceptibility to autoimmune disease.

Single molecule reconstitution of PI3Kβ synergistic activation reveals mechanism for rapid PI(3,4,5)P₃ production during immune cell signaling.