How do nuclear pores decide which molecules can enter the cell nucleus?

New research published in Nature Communications reveals how the molecular architecture of nuclear pore complexes influences the selective transport of molecules between the nucleus and the cytoplasm.

In a collaborative study the team of Prof. Patrick Onck used rationally designed FG-nucleoporins to investigate how the amino-acid sequence of these proteins affect their interactions with transport receptors.

Their findings reveal that:

* The spacing between FG motifs influences how transport receptors partition into the protein phase.

* The ratio between charged and hydrophobic amino acids affects the accessibility of FG motifs and the pore’s barrier function.

* The balance between steric hindrance and enthalpic gain leads to optimal transport selectivity for designs close to native FG-Nups.

These insights help us better understand the physical principles that govern transport through one of the cell's most important molecular gateways.

Congratulations to all authors on this publication!

Read the open-access paper: https://doi.org/10.1038/s41467-026-77818-0

Spatial control of karyopherin binding avidity within NPC mimics revealed by designer FG-nucleoporins.

Published in Nature Communications, 28 September 2026.