Nucleocytoplasmic transport is mediated by the interplay between soluble tr
ansport factors and nucleoporins resident within the nuclear pore complex (
NPC). Understanding this process demands knowledge of components of both th
e soluble and stationary phases and the interface between them, Here, we pr
ovide evidence that Nup2p, previously considered to be a typical yeast nucl
eoporin that binds import- and export-bound karyopherins, dynamically assoc
iates with the NPC in a Ran-facilitated manner. When bound to the NPC, Nup2
p associates with regions corresponding to the nuclear basket and cytoplasm
ic fibrils. On the nucleoplasmic face, where the Ran-GTP levels are predict
ed to be high, Nup2p binds to Nup60p. Deletion of NUP60 kenders Nup2p nucle
oplasmic and compromises Nup2p-mediated recycling of Kap60p/Srplp. Depletio
n of Ran-GTP by metabolic poisoning, disruption of the Ran cycle, or in vit
ro by cell lysis, results in a shift of Nup2p from the nucleoplasm to the c
ytoplasmic face of the NPC. This mobility of Nup2p was also detected using
heterokaryons where, unlike nucleoporins, Nup2p was observed to move from o
ne nucleus to the other. Together, our data support a model in which Nup2p
movement facilitates the transition between the import and export phases of
nucleocytoplasmic transport.