1997年11月
CRM1 is responsible for intracellular transport mediated by the nuclear export signal
NATURE
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- 巻
- 390
- 号
- 6657
- 開始ページ
- 308
- 終了ページ
- 311
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/36894
- 出版者・発行元
- MACMILLAN MAGAZINES LTD
The discovery of nuclear export signals (NESs) in a number of proteins revealed the occurrence of signal-dependent transport of proteins from the nucleus to the cytoplasm(1-14). Although the consensus motif of the NESs has been shown to be a leucine-rich, short amino-acid sequence(2,6,7), its receptor has not been identified. A cytotoxin leptomycin B (LMB) has recently been suggested to inhibit the NES-mediated transport of Rev protein(15). Here we show that LMB is a potent and specific inhibitor of the NES-dependent nuclear export of proteins. Moreover, we have found a protein of relative molecular mass 110K (p110) in Xenopus oocyte extracts that binds to the intact NES but not to the mutated, non-functional NES. The binding of p110 to NES is inhibited by LMB. We show that p110 is CRM1, which is an evolutionarily conserved protein(16-18) originally found as an essential nuclear protein in fission yeas(16) and known as a likely target of LMB19. We also show that nuclear export of a fission yeast protein, Dsk1, which has a leucine-rich NES, is disrupted in wildtype yeast treated with LMB or in the crm1 mutant. These results indicate that CRM1 is an essential mediator of the NES-dependent nuclear export of proteins in eukaryotic cells.
- リンク情報
- ID情報
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- DOI : 10.1038/36894
- ISSN : 0028-0836
- PubMed ID : 9384386
- Web of Science ID : WOS:A1997YG66700069