Open AccessFlexible Gates: Dynamic Topologies and Functions for FG Nucleoporins in Nucleocytoplasmic Transport
Author(s) -
Laura J. Terry,
Susan R. Wente
Publication year - 2009
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.00225-09
Subject(s) - nucleoporin , nuclear pore , microbiology and biotechnology , nuclear transport , biology , cytoplasm , importin , transport protein , translation (biology) , compartmentalization (fire protection) , cell nucleus , genetics , messenger rna , gene , biochemistry , enzyme
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.