Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import - PubMed (original) (raw)
Review
. 2001 Jun 8;498(2-3):145-9.
doi: 10.1016/s0014-5793(01)02489-9.
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- PMID: 11412846
- DOI: 10.1016/s0014-5793(01)02489-9
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Review
Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
M Stewart et al. FEBS Lett. 2001.
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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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