Structural analysis of the nuclear pore complex by integrated approaches
Related Experiment Video
Updated: Jun 24, 2026

Single-Molecule Imaging of Nuclear Transport
Published on: June 9, 2010
Nadav Elad1, Tal Maimon, Daphna Frenkiel-Krispin
1Department of Life Science, Ben Gurion University and the NIBN, Beer-Sheva, Israel.
Abstract:
In eukaryotic cells, the nucleus is surrounded by a double membrane system, the nuclear envelope (NE), in which the outer membrane is continuous with the endoplasmic reticulum (ER). Nuclear pore complexes (NPCs) fuse the inner and outer nuclear membranes to form aqueous translocation channels that allow the free diffusion of small molecules and ions, as well as receptor-mediated transport of large macromolecules. Being the sole gateways for import and export to and from the nucleus, NPCs regulate the nucleocytoplasmic transport of macromolecules in a highly selective manner to maintain cellular functions. The large size and complexity of these multimolecular assemblies, which are composed of approximately 30 different proteins (termed nucleoporins), present a major challenge for structural biologists. Here, we discuss the latest structural findings related to the functional organization of the NPC.
Related Concept Videos
Nuclear Protein Sorting
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
Regulation of Nuclear Protein Sorting
Nuclear Export of mRNA
Nuclear Export
NES are of three types- the canonical 10-residue long leucine-rich signal and other...
Nuclear Localization Signals and Import
Directionality of Nuclear Transport