a plethora of biological consequences, only one of which is autophagy, as reviewed in June 2022 by Deretic and Lazarou. Membrane atg8ylation controls many functions, and has recently been shown to elicit and coordinate during lysosomal membrane stress multiple effector mechanisms: mTOR inactivation, stress granule formation, inhibition of general protein translation via IF2α phosphorylation, and integrated stress response via ATF4. The most recent studies by Deretic's group from the AIM center for autophagy, inflammation and metabolism studies, provide insight into how cells detect endomembrane and plasma membrane damage and what systems are deployed to help repair or eliminate/replace such membranes. In a paper in Molecular Cell, this group has shown that a novel system termed GALTOR, based on Galectin-8, interacts with the mTOR regulatory system composed of SLC38A9, Ragulator, RagA/B, RagCD. Following lysosomal damage, GALTOR inhibits mTOR causing its dissociation from damaged lysosomes. The key to GALTOR's action are galectins, sugar-binding cytosolic proteins, which can detect glycoconjugates exposed on the lumenal (exofacial) side of the lysosomal membrane upon membrane damage, thus transducing the breach of the membrane to mTOR. The physiological consequences of mTOR inhibition following endomembrane damage are many including induction of autophagy and metabolic switching. The functional roles of galectins in cellular response to membrane damage are rapidly expanding and Deretic's group has recently shown that Galectin-3 recruits ESCRTs to damaged lysosomes so that lysosomes can be repaired. Most recent findings show that Galectin-9 responds to lysosomal damage by activating AMPK, a central regulator of metabolism and autophagy. This occurs by Galectin-9-dependent activation of the ubiquitination systems on damaged lysosomes resulting in K63-ubiqutination of TAK1, an upstream kinase that phosphorylates and activates AMPK. Continuing the theme of homeostatic responses to membrane damage, Deretic's group has recently shown that ATG9A, primarily considered to be a core autophagy gene and one of the few that are membrane integral proteins, organizes the ESCRT machinery along with a Ca2+ responsive protein IQGAP1 to protect plasma membrane from damage, and programmed or incidental permeabilization. ATG9A marshals ESCRT proteins to repair pores on plasma membrane introduced by gasdermin (GSDMD) during pyroptosis, by MLKL during necroptosis, by Mycobacterium tuberculosis during infection of host cells, and by SARS-CoV-2 ORF3a's MLKL-like action at the plama membrane. This expands the scope of the membrane homeostasis role of autophagy proteins beyond the process of degradative autophagy. The Deretic laboratory has shown that autophagy in mammalian cells plays not only