The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin-β 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. © 2001 Federation of European Biochemical Societies.
Stewart, M., Baker, R. P., Bayliss, R., Clayton, L., Grant, R. P., Littlewood, T., & Matsuura, Y. (2001, June 8). Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. FEBS Letters. https://doi.org/10.1016/S0014-5793(01)02489-9