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Updated: Jul 20, 2026

Single-Molecule Imaging of Nuclear Transport
Published on: June 9, 2010
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
M Stewart1, R P Baker, R Bayliss
1MRC Laboratory of Molecular Biology, Hills Rd., CB2 2QH, Cambridge, UK. ms@mrc-lmb.cam.ac.uk
Abstract:
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin-beta family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between successive FG cores. A major question is why some macromolecules are transported while others are not. This selectivity may be generated by the ability to bind FG repeats, a local concentration of carrier-cargo complexes near the entrance to the pore channel, and steric hindrance produced by high concentrations of nucleoporins in the channel.
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