期刊
EUKARYOTIC CELL
卷 8, 期 12, 页码 1814-1827出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/EC.00225-09
关键词
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资金
- National Institutes of Health [R01 GM051219]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM051219, R37GM051219] Funding Source: NIH RePORTER
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.
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