Sheung Chun Ng

Conserved features of Nup98 FG domains Nup98 FG repeat domains readily phase-separate to form an FG phase with NPC-typical transport selectivity. They are intrinsically disordered, but in contrast to typical intrinsically disordered domains, they show a high degree of sequence conservation32. In fact, the Nup98 FG domain of vertebrates is as conserved as its globular anchor domain. This points to considerable evolutionary pressure to maintain its interactions.

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Nuclear pore complexes (NPCs) conduct nucleocytoplasmic transport through an FG domain-controlled barrier. We now explore how surface-features of a mobile species determine its NPC passage rate. Negative charges and lysines impede passage. Hydrophobic residues, certain polar residues (Cys, His), and, surprisingly, charged arginines have striking translocation-promoting effects. Favorable cation-π interactions between arginines and FG-phenylalanines may explain this apparent paradox.