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. 2020 Aug 1;31(17):1879–1891. doi: 10.1091/mbc.E20-04-0233

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© 2020 Baumhardt et al. “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology.

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FIGURE 6: — Accessibility of the NESs of Mek1 and RPS2 in the full-length cargoes. (A) Left panel: residues in the predicted NES of Mek1 (cyan) are shown in the structure of the full-length protein (gray; PDB 3W8Q). Middle panel: the CRM1-bound Mek1^NES peptide (cyan). Right panel: binding affinities of the Mek1^NES peptide and the full-length Mek1 protein for WT and E571K CRM1. (B) Residues in the predicted NES of RPS2 (cyan) shown in the structure of full-length RPS2 in the 40S ribosome (green; PDB 4V88). (C) Localization of endogenous RPS2 was detected by immunostaining with anti-RPS2 and a fluorescently labeled secondary antibody and is predominantly cytoplasmic in HEK 293 cells in the presence and absence of LMB. (D) The cytoplasmic/nuclear ratio of endogenous RPS2 in HEK 293 CRM1^WT/WT, CRM1^WT/E571K, and CRM1^E571K/E571K cells.