Supplemental data for Figs. 5 and 6 with EFGR and LC3 degradation. (A) IB showing similar levels of stable STING-GFP expression in WT and VPS13C^KO cells. (B) IB showing increased levels of p-STING in VPS13C^KO cells (both endogenous and STING-GFP). (C) IB showing increased levels of p-TBK1 in VPS13C^KO cells. (D) Time course of WT and VPS13C^KO cells treated with HT-DNA (500 ng/ml) for 0, 3, 6, and 24 h. (E) As with cGAMP treatment, STING is not significantly degraded in VPS13C^KO cells, quantified in E. n = 2 biological replicates. (F) Intact blot from which the data from Fig. 6, E and G, were extracted. (G) IB of the same samples as in F with anti p-STING antibody. (H) IB of EGFR in WT and VPS13C^KO cells treated with 100 ng/ml EGF for 0.5, 1, and 3 h. (I) Quantification from A of band intensity at various timepoints (F) normalized to EGFR intensity at 0 h (F₀), showing no defect in EGFR degradation kinetics. n = 3 biological replicates. (J) IB of LC3 in WT and VPS13C^KO cells after 6-h starvation in Earle’s balanced salt solution (EBSS). Note that the ratio of lipidated LC3-II to LC3-I is elevated under basal conditions in VPS13C^KO cells, possibly downstream of STING activation, as previously reported (Fischer et al., 2020; Gui et al., 2019). **, P < 0.01. Time course data were compared using two-way ANOVA followed by FDR multiple comparisons testing. All other data were compared using two-sided t tests. Error bars represent ±SD. Source data associated with this figure can be found at https://doi.org/10.5281/zenodo.6416363. Source data are available for this figure: SourceData FS4.