作者: Makoto Fukuda , Shiro Asano , Takahiro Nakamura , Makoto Adachi , Minoru Yoshida
DOI: 10.1038/36894
关键词: Conserved sequence 、 Nuclear protein 、 Nucleocytoplasmic Transport Proteins 、 XPO1 、 Exportin-1 、 Biochemistry 、 Leptomycin 、 Biology 、 Nuclear export signal 、 Plasma protein binding
摘要: The discovery of nuclear export signals (NESs) in a number proteins revealed the occurrence signal-dependent transport from nucleus to cytoplasm. Although consensus motif NESs has been shown be leucine-rich, short amino-acid sequence, its receptor not identified. A cytotoxin leptomycin B (LMB) recently suggested inhibit NES-mediated Rev protein. Here we show that LMB is potent and specific inhibitor NES-dependent proteins. Moreover, have found protein relative molecular mass 110K (p110) Xenopus oocyte extracts binds intact NES but mutated, non-functional NES. binding p110 inhibited by LMB. We CRM1, which an evolutionarily conserved originally as essential fission yeast known likely target also protein, Dsk1, leucine-rich NES, disrupted wild-type treated with or crm1 mutant. These results indicate CRM1 mediator eukaryotic cells.