Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis

Robitaille, Aaron M. and Christen, Stefan and Shimobayashi, Mitsugu and Cornu, Marion and Fava, Luca and Moes, Suzette and Prescianotto-Baschong, Cristina and Sauer, Uwe and Jenö , Paul and Hall, Michael N.. (2013) Quantitative phosphoproteomics reveal mTORC1 activates de novo pyrimidine synthesis. Science, 339 (6125). pp. 1320-1323.

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Official URL: http://edoc.unibas.ch/dok/A6093990

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Growth & Development > Biochemistry (Hall)
UniBasel Contributors:Hall, Michael N. and Robitaille, Aaron Mark and Shimobayashi, Mitsugu and Prescianotto-Baschong, cristina and Jenoe, Paul and , and , and ,
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Association for the Advancement of Science
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:25 Apr 2018 09:55
Deposited On:24 May 2013 09:03

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