Nup214-Nup88 Nucleoporin Subcomplex Is Required for CRM1-mediated 60 S Preribosomal Nuclear Export

摘要: The nuclear pore complex (NPC) conducts macromolecular transport to and from the nucleus provides a kinetic/hydrophobic barrier composed of phenylalanine-glycine (FG) repeats. Nuclear is achieved through permeation this by receptors. receptor CRM1 facilitates export large variety cargoes. Export preribosomal 60 S subunit follows pathway adaptor protein NMD3. Using RNA interference, we depleted two FG-containing cytoplasmically oriented NPC complexes, Nup214-Nup88 Nup358, investigated CRM1-mediated export. A dramatic defect in NMD3-mediated preribosomes was found Nup214-Nup88-depleted cells, whereas only minor defects were evident other cargoes or upon depletion Nup358. We show that C-terminal FG domain Nup214 not accessible freely diffusing molecules nucleus, indicating it does conduct NPC. Consistently, derivatives lacking FG-repeat rescued defect. coiled-coil region sufficient for export, coinciding with recruitment Nup88 Our data indicate plays independent roles function participating its FG-rich enabling gating association Nup88.