All articles tagged with #karyopherins
New high-speed imaging and modeling show the nuclear pore’s center is a dynamic, disorder‑driven environment where FG‑nucleoporins and transport proteins form a moving central plug; this flexible 'virtual gate' controls which molecules enter the nucleus, challenging the idea of a static gel and linking pore dysfunction to disease, with implications for drug delivery.
The HIV capsid, crucial for viral infection, has been found to interact with FG-nucleoporins (FG-Nups) of the nuclear pore complex (NPC) through weak but specific interactions, similar to karyopherins. The capsid's ability to bind to FG-Nups, which form the selectivity barrier of the NPC, allows it to overcome the size restriction and enter the nucleus. This interaction is mediated by an FG-binding pocket on the capsid, and mutations affecting this pocket disrupt the binding. Additionally, the capsid can enter phase-separated FG-Nup condensates, demonstrating its ability to engage with the NPC autonomously. These findings shed light on the mechanism of HIV nuclear entry and provide insights into potential targets for antiviral therapies.