Real-time monitoring of proteins in the nuclear pore complex
In human cells, the nucleus is enclosed by a structure called the nuclear pore complex (NPC). It acts as a 'gatekeeper' controlling the transport of molecules between the nucleus and the surrounding cytoplasm (the protein-containing solution in the inside of a cell). The NPC consists of proteins known as nucleoporins; some of these, the so-called FG-NUPs, belong to the class of intrinsically disordered proteins (IDPs) and capable of forming liquid-liquid phase separation (LLPS), lacking a well-defined tertiary structure (that is, a particular 3-D shape). Although a lot is known about FG-NUPs, a thorough understanding of how their structure varies in time and space has been missing. But now, by applying high-speed atomic force microscopy (HS-AFM), Richard Wong from Kanazawa University and colleagues provide much-needed insights into the spatiotemporal structure of FG-NUPs.