Cse1p-binding dynamics reveal a binding pattern for FG-repeat nucleoporins on transport receptors.
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-nucleoporin peptides are revealed on the surface of Cse1p, and 5 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 to ensure multiple binding from the same FG-nucleoporin.
Isgro
Timothy A
TA
Department of Physics, University of Illinois at Urbana-Champaign, Beckman Institute for Advanced Science and Technology, Urbana, IL 61801, USA.
Schulten
Klaus
K
D000595:Amino Acid Sequence; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism; D003198:Computer Simulation; D008954:Models, Biological; D008958:Models, Molecular; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D018160:Receptors, Cytoplasmic and Nuclear / Q000378:metabolism*; D020449:Repetitive Sequences, Amino Acid
D028861:Nuclear Pore Complex Proteins; D018160:Receptors, Cytoplasmic and Nuclear