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.
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.
Nup98-HoxA9 is recruited to Hox gene cluster regions together with the chromosomally pre-bound nuclear export factor Crm1, which induces aberrant expression of several Hox genes and affecting the differentiation of embryonic stem cells.