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10.1016/j.celrep.2017.10.029

http://scihub22266oqcxt.onion/10.1016/j.celrep.2017.10.029
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C5689476!5689476!29091770
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suck abstract from ncbi


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pmid29091770      Cell+Rep 2017 ; 21 (5): 1331-46
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  • The mTORC1 signaling network senses changes in cellular purine nucleotide levels #MMPMID29091770
  • Hoxhaj G; Hughes-Hallett J; Timson R; Ilagan E; Yuan M; Asara JM; Ben-Sahra I; Manning BD
  • Cell Rep 2017[Oct]; 21 (5): 1331-46 PMID29091770show ga
  • mTORC1 integrates signals from growth factors and nutrients to control biosynthetic processes, including protein, lipid and nucleic acid synthesis. We find that the mTORC1 pathway is responsive to changes in purine nucleotides in a manner analogous to its sensing of amino acids. Depletion of cellular purines, but not pyrimidines, inhibits mTORC1, and restoration of intracellular adenine nucleotides via addition of exogenous purine nucleobases or nucleosides acutely reactivates mTORC1. Adenylate sensing by mTORC1 is dependent on the tuberous sclerosis complex (TSC) protein complex and its regulation of Rheb upstream of mTORC1, but independent of energy stress and AMPK. While mTORC1 signaling is not acutely sensitive to changes in intracellular guanylates, long-term depletion of guanylates decreases Rheb protein levels. Our findings suggest that nucleotide sensing, like amino acid sensing, enables mTORC1 to tightly coordinate nutrient availability with the synthesis of macromolecules, such as protein and nucleic acids, produced from those nutrients.
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