Abstract
ACELL'S NUCLEAR ENVELOPE is like a building with thousands of screen doors. Galled nuclear pore complexes (NPCs), these gateways control entry to and exit from the nucleus. The basis of this lifesustaining selectivity remains a matter of debate, but new evidence suggests that the central canal of NPCs may be filled with a protein gel bearing molecular motifs key to the pores' selectivity (Science 2006,314,815). NPCs allow free passage of water, ions, and metabolites and other small solutes while carefully controlling the comings and goings of big molecules such as messenger RNA and proteins. The only way molecules larger than about 30 kilodaltons can pass through NPCs is by hitching a ride with nuclear transport receptors (NTRs), a class of proteins with an open invitation to traverse nuclear pore complexes. These shuttling runs, up to 1,000 per second for a single NPC, are perpetrated via interactions between the passenger-carrying NTRs and a common repeating motif ...
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