![[feed]](/style/images/feed-icon-14x14.png){kind=icon}
Tools
Tools
| Item Type: | Article |
|---|---|
| Title: | A 41 amino acid motif in importin-alpha confers binding to importin-beta and hence transit into the nucleus |
| Creators Name: | Goerlich, D., Henklein, P., Laskey, R.A. and Hartmann, E. |
| Abstract: | The complex of importin-alpha and -beta is essential for nuclear protein import. It binds the import substrate in the cytosol, and the resulting trimeric complex moves through the nuclear pores, probably as a single entity. Importin-alpha provides the nuclear localization signal binding site, importin-beta the site of initial docking to the pore. Here we show that the conserved, basic N-terminus of importin-alpha is sufficient for importin-beta binding and essential for protein import. The fusion product of this 41 amino acid domain to a heterologous protein if transported into the nucleus in the same way as full-length importin-alpha itself. Transport is dependent on importin-beta but competed by importin-alpha. As no additional part of importin-alpha is needed for translocation, the movement which drives the import substrate complex into the nucleus appears to be generated between importin-beta and structures of the nuclear pore. The domain that binds to importin-beta appears to confer import only, but not re-export out of the nucleus, suggesting that the return of importin-alpha into the cytoplasm is not a simple reversal of its entry. |
| Keywords: | IBB Domain, Importin, Nuclear Pore, Nuclear Transport, Ran, Animals, Xenopus |
| Source: | EMBO Journal |
| ISSN: | 0261-4189 |
| Publisher: | Oxford University Press |
| Volume: | 15 |
| Number: | 8 |
| Page Range: | 1810-1817 |
| Date: | 15 April 1996 |
| Official Publication: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC450097/?tool=pubmed |
| PubMed: | View item in PubMed |
Repository Staff Only: item control page
