Glycosylation and importins liquefy the FG barrier in live nuclear pores.

FG-rich nucleoporins in live cells show nanosecond-scale, liquid-like segmental motion, while reconstituted FG condensates undergo a liquid-to-solid transition in vitro.

• Why it matters: The field lacks direct evidence for how intrinsically disordered FG-NUPs behave in living nuclear pores, limiting understanding of selective, rapid transport.
• What they did: The authors used site-specific labeling with time-resolved fluorescence anisotropy, plus molecular-dynamics simulations, and tested how importin-β and O-linked β-N-acetylglucosamine stabilize the FG network.
• The result: Finely tuned FG–FG and FG–importin-β interactions maintain FG liquidity and produce radial organization with importin-β enriched at the periphery, supported by MINFLUX imaging of importin-β in mammalian cells.

AI summary of the abstract · may contain errors · not medical advice · read the paper.