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S-adenosylmethionine sensor upstream of mTORC1 (SAMTOR) is a cytoplasmic protein that serves as a sensor of S-adenosylmethionine (SAM), a metabolite derived from methionine and ATP, and acts upstream of the mechanistic target of rapamycin complex 1 (mTORC1). SAMTOR binds SAM via its C-terminal methyltransferase-like domain. Under methionine-rich conditions, elevated SAM levels bind to SAMTOR, leading to its dissociation from the GATOR1-KICSTOR complex and resulting in activation of mTORC1 signaling, which drives cellular growth and metabolism. In methionine- or SAM-deficient states, SAMTOR associates with GATOR1-KICSTOR, thereby inhibiting mTORC1. SAMTOR is essential for the nutrient-sensing function of mTORC1 and connects methionine/SAM metabolism with fundamental processes such as protein synthesis, lipid biosynthesis, and autophagy. Dysfunction or misregulation of SAMTOR or the pathways it regulates is implicated in diseases characterized by altered mTORC1 activity, including obesity, diabetes, and cancer[1][2][3][5][7].
Not applicable (targeted drugs unknown)
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