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. 2019 Aug 1;30(17):2171–2184. doi: 10.1091/mbc.E18-11-0702

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© 2019 Aryanpur 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 4: — The Ded1 C-terminus has a role in remodeling eIF4G1 from translation complexes following rapamycin treatment. (A) DED1 and ded1-ΔCT cells were grown in the presence of rapamycin for 40 min, after which formaldehyde cross-linking was performed. Polysome profiles were generated as in Figure 2, and fractions were collected for Western blotting using antibodies against Tif4631 (eIF4G1), Ded1, HA (Tif1/eIF4A), and rabbit IgG for Protein-A (Nip1/eIF3c). Representative results for the distributions of each protein are shown. (B, C) Densitometry was performed on eIF4G1 (B) and eIF4A (C) from A. The figure depicts the distribution as a percentage of the total protein in each subfraction. The averages of five independent experiments are shown. *p < 0.05 vs. untreated fraction. (D) WT and TOR1^L2134M cells were treated with rapamycin for 40 min, and cells were analyzed as in A using antibodies against Tif4631 (eIF4G1).