A theoretical basis for the spatial regulation of protein aggregation shows how aggregates can partition preferentially into intracellular liquid compartments.
An image-based multiplex autophagosome RNAi screen targeting all Rab GTPases as well as their GAPs and GEFs identifies the Rab GEF SMCR8 as multifaceted autophagy modulator, which regulates kinase activity and gene expression of ULK1.
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.
Efficient nuclear transport of very large biomolecules, relevant for viral transport, scales non-linearly with size and its kinetics can be explained by a simple two-parameter energetic model.
A genome-organizing protein that is present only in the olfactory system of mice has been found to orchestrate changes in the relative numbers of different odor-sensing neurons on the basis of how active these neurons are.
The equilibrium between solubility and aggregation of proteins in the nucleus is controlled by co-aggregates like RNA and the action of ATP as both an energy source and a destabilizing chemical agent.
