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.
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.
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.
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.
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.