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Nature study finds liquid-like motion in the nuclear pore transport barrier

Nature reported that NUP98 proteins in the nuclear-pore barrier move dynamically in living cells, with importin-beta and a sugar modification helping maintain that state.

A Nature research briefing describes experiments and simulations indicating that flexible proteins in the nuclear-pore transport barrier behave in a liquid-like way. The report says importin-beta and glycosylation help preserve the barrier's dynamic state.

Sources

  1. Nature — Glycosylation and importins liquefy the FG barrier in live nuclear pores ↗
  2. Nature — Proteins that form the nuclear pore barrier move like liquids ↗