Liver tissues or cell pellets were homogenized or suspended in lysis buffer [30 mM Tris (pH 7.5), 150 mM NaCl, 1% NP-40, 0.5% Na deoxycholate, 0.1% SDS, 10% glycerol, and 2mM EDTA] containing the Complete Protease Inhibitor Cocktail (ThermoFisher Scientific). Protein concentrations were determined with the Bio-Rad Protein Assay Kit (Bio-Rad, Hercules, CA) using bovine serum albumin as a standard. Aliquots of 30 μg lysates were denatured by boiling in Tris-Glycine SDS Sample Buffer (Bio-Rad), separated by SDS-PAGE, and transferred to nitrocellulose membranes (Bio-Rad) by electroblotting. Membranes were blocked in 5% non-fat dry milk in Tris-buffered saline containing 0.1% Tween 20 for 1 hour and probed with following specific antibodies: AKT (9272), Phospho-AKT(S473) (4060), Phospho-AKT(T308) (13038), Phospho-mTOR (2971), Phospho-p70 S6 Kinase (9205), Phospho-RPS6 (4858), Phospho-4E-BP1(T37/46) (2855), Phospho-4E-BP1(S65) (9451), Phospho-NDRG1 (5482), Survivin (2808), YAP/TAZ (8418), Cleaved Caspase-3 (CC-3) (9664), Mcl-1 (94296), Bcl-Xl (2764), Bak (12105; Cell Signaling Technology), SLC38A1 (HPA052272; Sigma-Aldrich, St. Louis, MO). Anti-β-catenin antibody (610153) was purchased from BD Biosciences (Franklin Lakes, NJ). Anti-GAPDH (MAB374; EMD Millipore, Billerica, MA), anti-β-Actin (A5441; Sigma-Aldrich, St. Louis, MO), and anti-β-tubulin (6046; Abcam) antibodies were used as loading controls. Each primary antibody was followed by incubation with horseradish peroxidase-secondary antibody (Jackson ImmunoResearch Laboratories Inc., West Grove, PA) diluted 1:10000 for 1 hour and then visualized by the Super Signal West Dura (ThermoFisher Scientific). For nuclear protein extraction, proteins were extracted by using the Cytoplasmic Extraction Reagent I and II (ThermoFisher Scientific). After thoroughly removing the supernatant (cytoplasmic extract), Nuclear Extraction Reagent (ThermoFisher Scientific) was added for the nuclear protein extraction. Aliquots of 5-10 μg of nuclear and cytoplasmic lysates were used for Western blotting. Isolation of cytoplasmic proteins was validated by β-tubulin, while Histone H3 (D1H2) (4499; Cell Signaling Technology) was used as loading control of nuclear proteins.