Microtubule nucleation from the nuclear envelope in fission yeast involves repurposing of nuclear export proteins for a non-export-related function, docking cytoplasmic proteins at nuclear pore complexes.
The super-resolution fluorescence microscopy approach polarization PALM (p-PALM) reveals that macromolecular crowding and inhomogeneity within nuclear pores generate a structurally and dynamically complex permeability barrier.
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.
Nuclear pores assemble asymmetrically, by an inside-out evagination of the inner nuclear membrane that grows in diameter and depth until it fuses with the flat outer nuclear membrane.
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.
In replicative ageing yeast cells, an age-dependent impediment in proper assembly of nuclear pore complexes is associated with altered nuclear transport.
Biomimetic nanopores reveal that the sequence-dependent spatial distribution of intrinsically disordered proteins plays a crucial role in establishing the selective permeability barrier of the nuclear pore complex.
Simple biophysical considerations explain the collective behavior of molecularly diverse complex protein assemblies that regulate transport between the nucleus and the cytoplasm in eukaryotic organisms.
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.
