Remodelling of cellular membranes is critical for many key steps of autophagy including autophagosome biogenesis, autophagosome-lysosome fusion and lysosome regeneration. BAR domains contribute to membrane remodelling of most cellular organelles by forming homodimers that bind directly to membrane lipids and induce membrane curvature. There is emerging evidence that BAR domain containing proteins (BARDCPs) contribute to autophagy via membrane remodelling of autophagosomes, Golgi-derived vesicles, recycling endosomes or lysosomes, but how these proteins contribute to selective vs non-selective autophagy pathways remains unclear. We have performed image-based siRNA screens and Halo processing assays to examine how BARDCPs regulate degradation of different autophagy cargoes. Our results identify several novel BARDCPs required for starvation-induced autophagy, including one that has a predicted LC3 interacting region that may bind to ATG8 proteins on autophagosomes. We also discovered two BARDCPs that are selectively required for ER-phagy but not starvation-induced autophagy, which are recruited to the ER following autophagy induction and may promote degradation of distinct ER subunits. Furthermore, these BARDCPs are independent prognostic markers for breast cancer relapse, which we speculate contribute to breast cancer progression via regulation of autophagy. Our findings show that BARDCPs exert distinct effects depending on autophagy cargoes, which may contribute to tumourigenesis.