Flexible gates: dynamic topologies and functions for FG nucleoporins in nucleocytoplasmic transport.

Terry LJ, Wente SR
Eukaryot Cell. 2009 8 (12): 1814-27

PMID: 19801417 · PMCID: PMC2794212 · DOI:10.1128/EC.00225-09

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.

MeSH Terms (8)

Active Transport, Cell Nucleus Animals Cell Nucleus Conserved Sequence Evolution, Molecular Humans Nuclear Pore Complex Proteins Repetitive Sequences, Amino Acid

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