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- W2159923856 endingPage "1827" @default.
- W2159923856 startingPage "1814" @default.
- W2159923856 abstract "The nuclear envelope is a physical barrier between the nucleus and cytoplasm and, as such, separates the mechanisms of transcription from translation. This compartmentalization of eukaryotic cells allows spatial regulation of gene expression; however, it also necessitates a mechanism for transport between the nucleus and cytoplasm. Macromolecular trafficking of protein and RNA occurs exclusively through nuclear pore complexes (NPCs), specialized channels spanning the nuclear envelope. A novel family of NPC proteins, the FG-nucleoporins (FG-Nups), coordinates and potentially regulates NPC translocation. The extensive repeats of phenylalanine-glycine (FG) in each FG-Nup directly bind to shuttling transport receptors moving through the NPC. In addition, FG-Nups are essential components of the nuclear permeability barrier. In this review, we discuss the structural features, cellular functions, and evolutionary conservation of the FG-Nups." @default.
- W2159923856 created "2016-06-24" @default.
- W2159923856 creator A5017446481 @default.
- W2159923856 creator A5081423114 @default.
- W2159923856 date "2009-12-01" @default.
- W2159923856 modified "2023-10-03" @default.
- W2159923856 title "Flexible Gates: Dynamic Topologies and Functions for FG Nucleoporins in Nucleocytoplasmic Transport" @default.
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