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.
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.
E3 ubiquitin ligase Bre1-induced H2B monoubiquitination is epigenetically important for recruiting replication factor Mcm10 and cohesion establishment factors Ctf4, Ctf18 and Eco1 to early replication origins to establish sister chromatid cohesion.
Soon after fertilisation, a critical portion of the embryonic genome is switched on through the actions of maternally inherited Stella, in part through controlling the activation of transposable elements.
Models that generate tandem alignments of cell polarities are more readily compatible with the formation of PIN1 polarity patterns in plant leaf buds than the most widely accepted “up-the-gradient” model.
The molecular microenvironment of coronaviral replicase complexes provides functional and spatial links between conserved cellular processes and viral RNA synthesis, and highlights potential targets for the development of novel antivirals.
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.