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Int. J. Mol. Sci. 2014, 15(11), 20753-20769;

Current Models of Mammalian Target of Rapamycin Complex 1 (mTORC1) Activation by Growth Factors and Amino Acids

College of Life Sciences, Inner Mongolia University, Hohhot 010021, China
Department of Clinical Laboratory, Hulunbeir Municipal People's Hospital, Hailar 021008, China
College of Basic Medical Science, Inner Mongolia Medical University, Hohhot 010110, China
These authors contributed equally to this work.
Authors to whom correspondence should be addressed.
Received: 4 September 2014 / Revised: 24 September 2014 / Accepted: 29 October 2014 / Published: 13 November 2014
(This article belongs to the Section Biochemistry, Molecular and Cellular Biology)
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Mammalian target of rapamycin (mTOR), which is now referred to as mechanistic target of rapamycin, integrates many signals, including those from growth factors, energy status, stress, and amino acids, to regulate cell growth and proliferation, protein synthesis, protein degradation, and other physiological and biochemical processes. The mTOR-Rheb-TSC-TBC complex co-localizes to the lysosome and the phosphorylation of TSC-TBC effects the dissociation of the complex from the lysosome and activates Rheb. GTP-bound Rheb potentiates the catalytic activity of mTORC1. Under conditions with growth factors and amino acids, v-ATPase, Ragulator, Rag GTPase, Rheb, hVps34, PLD1, and PA have important but disparate effects on mTORC1 activation. In this review, we introduce five models of mTORC1 activation by growth factors and amino acids to provide a comprehensive theoretical foundation for future research. View Full-Text
Keywords: mTORC1; Rheb; Ragulator; Rag GTPases; hVps34; PA mTORC1; Rheb; Ragulator; Rag GTPases; hVps34; PA

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Zheng, X.; Liang, Y.; He, Q.; Yao, R.; Bao, W.; Bao, L.; Wang, Y.; Wang, Z. Current Models of Mammalian Target of Rapamycin Complex 1 (mTORC1) Activation by Growth Factors and Amino Acids. Int. J. Mol. Sci. 2014, 15, 20753-20769.

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