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.
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.
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.
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.
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.
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.