Researchers use fluorescent probes to study nuclear pores

New findings on pore interiors

For the first time, researchers quantified internal protein movements inside a living cell's nanocanal. They demonstrated that the interior of this canal behaves like a fluid rather than a solid gel. The present research, directed by Professor Edward Lemke of Johannes Gutenberg University Mainz alongside Professor Gerhard Hummer from the Max Planck Institute for Biophysics in Frankfurt am Main and Wuhan University in China, has now clarified the issue. The researchers published their findings in the journal Nature.

Simulation model answers transport questions

Using these findings, scientists from the Max Planck Institute for Biophysics have developed the most complete simulation model of a nuclear pore available so far. JUPITER, Europe's initial exascale supercomputer located at the Jülich Research Center, enabled these intricate calculations. This model addresses the transport route through the pore and explains how molecules travel within the cell nucleus.

Protein barrier nature remains debated

Research into separate proteins produced inconsistent outcomes, describing structures as stretched polymers, liquid-like condensates, or solid-like gels resembling the texture of gummy bears. Until now, no direct conclusions regarding the barrier's behavior inside a living cell could be drawn from such studies. According to Professor Miao Yu of Wuhan University, the nuclear pore safeguards the genome while regulating every interaction between the cell nucleus and the cytoplasm.