CRM1 is responsible for intracellular transport mediated by the nuclear export signal

Makoto Fukuda, Shiro Asano, Takahiro Nakamura, Makoto Adachi, Minoru Yoshida, Mitsuhiro Yanagida and Eisuke Nishida ()
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Makoto Fukuda: Graduate School of Science, Kyoto University
Shiro Asano: Graduate School of Science, Kyoto University
Takahiro Nakamura: Graduate School of Science, Kyoto University
Makoto Adachi: Graduate School of Science, Kyoto University
Minoru Yoshida: Graduate School of Agriculture and Life Sciences, The University of Tokyo
Mitsuhiro Yanagida: Graduate School of Science, Kyoto University
Eisuke Nishida: Graduate School of Science, Kyoto University

Nature, 1997, vol. 390, issue 6657, 308-311

Abstract: Abstract 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 cytoplasm1,2,3,4,5,6,7,8,9,10,11,12,13,14. Although the consensus motif of the NESs has been shown to be a leucine-rich, short amino-acid sequence2,6,7, its receptor has not been identified. A cytotoxin leptomycin B (LMB) has recently been suggested to inhibit the NES-mediated transport of Rev protein15. 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 protein16,17,18 originally found as an essential nuclear protein in fission yeast16 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 wild-type 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.

Date: 1997
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DOI: 10.1038/36894

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