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Eukaryot Cell. 2009 Dec;8(12):1814-27. doi: 10.1128/EC.00225-09. Epub 2009 Oct 2.

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

Author information

1
Department of Cell and Developmental Biology, Vanderbilt University Medical Center, Nashville, TN 37232-8240, USA.

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.

PMID:
19801417
PMCID:
PMC2794212
DOI:
10.1128/EC.00225-09
[Indexed for MEDLINE]
Free PMC Article

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