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. 2021 May 10;118(20):e2026104118. doi: 10.1073/pnas.2026104118

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Copyright © 2021 the Author(s). Published by PNAS.

This open access article is distributed under Creative Commons Attribution-NonCommercial-NoDerivatives License 4.0 (CC BY-NC-ND).

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Fig. 5. — AGO2 promotes MAPK signaling through direct interaction. (A) Organoids isolated from lung nodules of KPC-Ago2^+/+ versus KPC-Ago2^−/− mice. Bright field image. (Scale bar, 500 μm.) (B) Histological sections of KPC-Ago2^+/+ and KPC-Ago2^−/− organoids stained with H&E and antibodies directed against AGO2 and Ki67. (Scale bar, 150 μm.) (C) GSEA assessing genes associated with increased KRAS signaling (SWEET_LUNG_CANCER_KRAS_UP and SWEET_LUNG_CANCER_KRAS_DOWN). Comparison of genes differentially expressed in KPC-Ago2^+/+ versus KPC-Ago2^−/− organoids. NES, normalized enrichment score. (D, Left) Immunoblot analysis of protein lysates from KPC-Ago2^+/+ versus KPC-Ago2^−/− organoid-derived cells. Phosphorylated ERK (pERK), total ERK (tERK), and histone H3 (H3). (D, Right) Immunoblot analysis of KPC-Ago2^−/− organoid-derived cells transfected with constructs encoding wild-type AGO2 (WT AGO2), AGO2K112A/E114A (K112A/E114A), and AGO2K98A (K98A).