EC Accepts, published online ahead of print on 2 October 2009

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Eukaryotic Cell doi:10.1128/EC.00225-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

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

Laura J. Terry and Susan R. Wente^*

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

^* To whom correspondence should be addressed. Email: susan.wente{at}vanderbilt.edu.

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 nuclear envelope pores. A novel family of NPC proteins, the 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.