Timothy A. Isgro and Klaus Schulten.
Cse1p binding dynamics reveal a novel binding pattern for FG-repeat
nucleoporins on transport receptors.
Structure, 15:977-991, 2007.
ISGR2007A
Nuclear pore proteins with phenylalanine-glycine repeats are vital to the functional transport of molecules across the nuclear pore complex. The current study investigates the binding of these FG-nucleoporins to the Cse1p:Kap60p:RanGTP nuclear export complex. Fourteen binding spots for FG-nup peptides are revealed on the surface of Cse1p, and five are revealed on the Kap60p surface. Taken together and along with binding data for two other transport receptors, the data suggest that the ability to bind FG-nucleoporins by itself is not enough to ensure viable nuclear transport. Rather, it is proposed that the density of
binding spots on the transport receptor surface is key in determining transport viability. The number of binding spots on the transport receptor surface should be large enough to ensure multiple, simultaneous FG-repeat binding, and their arrangement should be close enough, perhaps to ensure multiple binding from the same FG-nucleoporin.
