A nuclear export sequence promotes CRM1-dependent targeting of the nucleoporin Nup214 to the nuclear pore complex

ABSTRACT Nup214 is a major nucleoporin on the cytoplasmic side of nuclear pore complex with roles in late steps protein and mRNA export. It interacts export receptor CRM1 (also known as XPO1) via characteristic phenylalanine-glycine (FG) repeats its C-terminal region. Here, we identify classic sequence (NES) that mediates Ran-dependent binding to CRM1. versions mutations NES, well wild-type presence selective inhibitor leptomycin B, accumulate nucleus Nup214-overexpressing cells. Furthermore, physiological partners Nup214, such Nup62 Nup88, are recruited together Nup214. Nuclear mutant can be rescued by artificial sequences at end leading also correct localization Nup88. Our results suggest function NES biogenesis and/or terminal CRM1-dependent