Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import

Murray Stewart, Rosanna Baker, Richard Bayliss, Lesley Clayton, Richard P. Grant, Trevor Littlewood, Yoshiyuki Matsuura

Research output: Contribution to journalArticle

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-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.

Original languageEnglish (US)
Pages (from-to)145-149
Number of pages5
JournalFEBS Letters
Volume498
Issue number2-3
DOIs
StatePublished - Jun 8 2001
Externally publishedYes

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Keywords

  • Cell biology
  • Molecular interaction
  • Nuclear trafficking
  • Nucleoporin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Stewart, M., Baker, R., Bayliss, R., Clayton, L., Grant, R. P., Littlewood, T., & Matsuura, Y. (2001). Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. FEBS Letters, 498(2-3), 145-149. https://doi.org/10.1016/S0014-5793(01)02489-9