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

FEBS Letters

Littlewood, Trevor¹  Matsuura, Yoshiyuki¹  Bayliss, Richard¹  Baker, Rosanna P¹  Clayton, Lesley¹  Grant, Richard P¹  Stewart, Murray¹ 

[1] MRC Laboratory of Molecular Biology, Hills Rd., Cambridge CB2 2QH, UK

关键词: Nuclear trafficking;    Nucleoporin;    Molecular interaction;    Cell biology;   

DOI  :  10.1016/S0014-5793(01)02489-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown