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

Author

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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)

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.

Suggested Citation

  • Makoto Fukuda & Shiro Asano & Takahiro Nakamura & Makoto Adachi & Minoru Yoshida & Mitsuhiro Yanagida & Eisuke Nishida, 1997. "CRM1 is responsible for intracellular transport mediated by the nuclear export signal," Nature, Nature, vol. 390(6657), pages 308-311, November.
    • Handle: RePEc:nat:nature:v:390:y:1997:i:6657:d:10.1038_36894
    DOI: 10.1038/36894
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    Cited by:

    1. Anja Deutzmann & Delaney K. Sullivan & Renumathy Dhanasekaran & Wei Li & Xinyu Chen & Ling Tong & Wadie D. Mahauad-Fernandez & John Bell & Adriane Mosley & Angela N. Koehler & Yulin Li & Dean W. Felsh, 2024. "Nuclear to cytoplasmic transport is a druggable dependency in MYC-driven hepatocellular carcinoma," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    2. Haofan Sun & Bin Fu & Xiaohong Qian & Ping Xu & Weijie Qin, 2024. "Nuclear and cytoplasmic specific RNA binding proteome enrichment and its changes upon ferroptosis induction," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    3. Jun Woo Park & Eun Jung Lee & Eunyoung Moon & Hong-Lim Kim & In-Beom Kim & Didier Hodzic & Namsuk Kim & Hee-Seok Kweon & Jin Woo Kim, 2023. "Orthodenticle homeobox 2 is transported to lysosomes by nuclear budding vesicles," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    4. Caroline E. Dewar & Silke Oeljeklaus & Jan Mani & Wignand W. D. Mühlhäuser & Corinne Känel & Johannes Zimmermann & Torsten Ochsenreiter & Bettina Warscheid & André Schneider, 2022. "Mistargeting of aggregation prone mitochondrial proteins activates a nucleus-mediated posttranscriptional quality control pathway in trypanosomes," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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