![Insights into Cellular Transport of Macromolecules]()
The nuclear pore complex (NPC) tightly regulates the movement of large molecules between the cell nucleus and cytoplasm. While small molecules like water pass easily through the NPC, large molecules must bind to transport factors (TFs) that traverse the pore’s central core by interacting with phenylalanine-glycine (FG) proteins. But how do TFs and their cargoes diffuse through the NPC’s FG repeats so rapidly even while the NPC remains selective about what it lets through—David Cowburn, Ph.D., and colleagues have discovered that TFs interact with FG repeats through a dynamic sliding motion. This enables faster movement through the NPC than could be attained through a two-state binding mechanism (requiring full disengagement and reengagement) for excluding macromolecules that don’t bind to TFs. Understanding NPCs is important since mutations in this structure contribute to cancer, viral infections, and other diseases. The study was published online on April 18, 2016 in PNAS. Dr. Cowburn is professor of biochemistry and of physiology & biophysics.
Posted on: Wednesday, May 25, 2016