Autophagy-induced vFLIP degradation.

<p>(A) Immunoblots of LC3B, p62, vFLIP, MAVS, and β-actin from WT and <i>MAVS</i> KO BCBL-1 cells cultured at low (seeded at 5 x 10⁴ cells/ml) and high (seeded at 2 x 10⁵ cells/ml) densities in the presence and absence of 20 nM rapamycin for 2 days. Relative band intensities normalized by β-actin were calculated and noted below each panel. (B) Real-time quantitative PCR (RT-qPCR) analysis of vFLIP mRNA from the cells cultured as in (A). Data are represented as mean ± SD of triplicate. (C) Immunoblots of vFLIP and loading control lactate dehydrogenase (LDH) from vFLIP-transfected 293T treated with 10 μM MG132, 100 nM bafilomycin A1 (Baf A1), 5 μM chloroquine (CQ), and 5 mM 3-methyladenine (3-MA) for 1 day. Relative vFLIP intensities normalized by LDH are shown below each panel. (D) Immunoblots of vFLIP, MAVS, and loading control β-actin from WT and <i>MAVS</i> KO BCBL-1 cell lines cultured at high density for 2 days and then treated with 20 nM Baf A1 and 10 μM MG-132 for 8 h. Relative vFLIP intensities normalized by β-actin are shown below each panel.