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

A combination of in vivo and in vitro approaches using Xenopus eggs and embryos reveals how dimensions of mitotic chromosomes scale with decreasing cell size and increasing nuclear-cytoplasmic ratio during early embryogenesis.

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

Degradation of a mitotic inducer coordinates the transition of two successive cell cycle arrests during the infective process of a plant pathogenic fungus.

Computational modelling predicts spatial segregation of different types of nuclear transport receptors in assemblies of nuclear pore proteins, lending support to the idea of separate transport pathways in the nuclear pore complex as a way to enhance transport efficiency.

Human cells respond to cytoplasmic mRNA depletion during early apoptosis by inhibiting RNA polymerase II transcription, thereby magnifying the gene expression shutdown during stress.

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.

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.