Aggregation, Phase Separation and Spatial Morphologies of the Assemblies of FG Nucleoporins

Nuclear pore complex (NPC) is a biomolecular "nanomachine" that controls nucleocytoplasmic transport in eukaryotic cells. The key component of the functional architecture of the NPC is the assembly of intrinsically disordered proteins that line its passageway and play a central role in the NPC transport mechanism. Due to paucity of experimental methods capable to directly probe the morphology of this assembly in intact NPCs, much of our knowledge about its properties derives from in vitro experiments augmented by theoretical and computational modeling. I review the major insights into the biophysics of the assemblies of the intrinsically disordered proteins of the NPC arising from the theoretical analysis of the recent in vitro experimental results, with the emphasis on the phase separation and aggregation phenomena.