PMID:23429704

Citation	Robitaille, AM, Christen, S, Shimobayashi, M, Cornu, M, Fava, LL, Moes, S, Prescianotto-Baschong, C, Sauer, U, Jenoe, P and Hall, MN (2013) Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science 339:1320-3
Abstract	The Ser-Thr kinase mammalian target of rapamycin (mTOR) controls cell growth and metabolism by stimulating glycolysis and synthesis of proteins and lipids. To further understand the central role of mTOR in cell physiology, we used quantitative phosphoproteomics to identify substrates or downstream effectors of the two mTOR complexes. mTOR controlled the phosphorylation of 335 proteins, including CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase). CAD catalyzes the first three steps in de novo pyrimidine synthesis. mTORC1 indirectly phosphorylated CAD-S1859 through S6 kinase (S6K). CAD-S1859 phosphorylation promoted CAD oligomerization and thereby stimulated de novo synthesis of pyrimidines and progression through S phase of the cell cycle in mammalian cells. Thus, mTORC1 also stimulates the synthesis of nucleotides to control cell proliferation.
Links	PubMed Online version:10.1126/science.1228771
Keywords
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
MOUSE:MTOR		GO:0006207: 'de novo' pyrimidine nucleobase biosynthetic process	ECO:0000314:		P		Figure 2. HeLa cells exhibited a higher rate of de novo pyrimidine synthesis in the presence of growth factors and amino acids. It was then concluded that mTORC1 activates de novo pyrimidine synthesis.	complete CACAO 7005
MOUSE:MTOR	involved_in	GO:0006207: 'de novo' pyrimidine nucleobase biosynthetic process	ECO:0000314: direct assay evidence used in manual assertion		P		Seeded From UniProt	complete

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