A conserved mechanism of membrane fusion in nuclear pore complex assembly.

A conserved membrane fusion mechanism involving Brl1, Brr6, and CLCC1 drives nuclear pore complex assembly across eukaryotes.

• Why it matters: Understanding how nuclear pore complexes (NPCs) form is crucial because they regulate transport between the nucleus and cytoplasm, yet the membrane fusion process involved has remained unknown.
• What they did: The study used molecular dynamics simulations, genetic disruption, and phylogenetic analysis to investigate membrane fusion in NPC assembly, focusing on proteins Brl1 and Brr6 in yeast, and CLCC1 in metazoans.
• The result: Findings reveal that Brl1 and Brr6 form complexes that facilitate membrane fusion, a mechanism conserved across eukaryotes, enabling NPC biogenesis and potentially informing broader membrane fusion processes.