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Back when the world was young I had a deep and abiding interest in the structure of components of the nuclear pore, especially those involved in getting messenger RNA out of the nucleus. The nuclear pore, you’ll recall, is a massive structure in the nuclear membrane of eukaryotes that keeps the DNA in and all that messy cytoplasmic stuff out–except when it needs to let it cross.

And that’s a very interesting problem. How do you allow the transport of cargo you want to move across the nuclear membrane without letting through undesirables? This was, and still is, an area of intense research–Günter Blobel won the Nobel Prize in 1999 for identifying nuclear localization sequences (and donated his prize money to the restoration of Dresden). And while the pathways, including RanGTP and importin ß and all the rest of them are pretty much mapped out, how the FG-repeats of the pore actually work to do this is still a bit puzzling.

Related, as you might expect there’s been quite a bit of work on the molecular structure of the pore. The problem is, this is very difficult to get a handle on, and there’s a gap between the technically impressive yet still rather fuzzy electron microscopy work and high resolution atomic detail of the sort I used to be involved in.

A paper from the Rockefeller University on a technique called polarized fluorescence microscopy^{10.1038/nsmb.2056} a is going to cause quite a stir then, in a good way. There’s a lot of math in there, but the authors say that this will help us “generate a high-resolution map of the entire NPC [nuclear pore complex],” with the aim of, eventually, measuring “nucleoporin rearrangements during nucleocytoplasmic transport and NPC assembly.” They’ve used the technique to confirm the arrangement of the critical Nup84 complex in pores, and, importantly, they can use the technique in live cells.

Read more about it at the Rockefeller website.