Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import. |
| |
Authors: | M Stewart R P Baker R Bayliss L Clayton R P Grant T Littlewood Y Matsuura |
| |
Institution: | MRC 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. |
| |
Keywords: | |
|
|