ER-phagy is a selective type of autophagy, whereby parts of the endoplasmic reticulum (ER) network (sheets or tubules) are engulfed by autophagosomes through specific ER-phagy receptors and then removed by lysosomal degradation. ER-phagy has been implicated in the response to ER stress, specifically in the unfolded protein response (UPR). Nevertheless, the mechanisms and regulation of ER-phagy remain elusive. In their work published in Cell, Liang et al. now identify 200 ER-phagy regulators and specifically dissect the role of two processes: one centred on mitochondrial oxidative metabolism and the other on protein UFMylation — a recently discovered ubiquitin-like post-translational modification.