Role of AMPK-mTOR-Ulk1/2 in the Regulation of Autophagy: Cross Talk, Shortcuts, and Feedbacks

By S. Alers, Antje S. Löffler, S. Wesselborg, B. Stork. Molecular and Cellular Biology, 2011

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Autophagy and multidrug resistance in cancer (2017, background): “By contrast, mTOR is inactive under nutrient-poor conditions: dephosphorylated ULK1 dissociates from the mTOR complex and then phosphorylates Atg13 and RB1inducible coiled-coil (1RB1CC1/FIP200), thus triggering autophagy [26].”
Metabolic Regulation of T Lymphocytes (2013, background): “ULK1 and ULK2 are also AMPK substrates and can promote autophagy (79).”
Autophagy and autophagy-related proteins in cancer (2020, background): “In mammal, the ULK1/2, a homologous protein of the kinase Atg1, forms a ULK1/2 kinase complex with ATG13 (homologous to Atg13 in yeast), FIP200 (homologous to Atg17 in yeast) and ATG101 (no homolog in yeast) [99] (Fig.”
An Overview of Autophagy: Morphology, Mechanism, and Regulation (2014, background): “Both growth factor concentrations and hypoxia regulate macroautophagy at least in part through MTORC1, and hypoxia can inhibit MTORC1 even in the presence of adequate nutrients and growth factors (2, 4).”
The hallmarks of aging. (2013, background): “AMPK activation has multiple effects on metabolism and, remarkably, shuts off mTORC1 (Alers et al., 2012).”