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Int. J. Mol. Sci. 2016, 17(10), 1684; doi:10.3390/ijms17101684

Methionine Regulates mTORC1 via the T1R1/T1R3-PLCβ-Ca2+-ERK1/2 Signal Transduction Process in C2C12 Cells

1
Department of Animal Nutrition and Feed Science, College of Animal Science and Technology, Huazhong Agriculture University, Wuhan 430070, Hubei, China
2
The Cooperative Innovation Center for Sustainable Pig Production, Wuhan 430070, Hubei, China
*
Author to whom correspondence should be addressed.
Academic Editor: Kathleen Van Craenenbroeck
Received: 2 August 2016 / Revised: 20 September 2016 / Accepted: 27 September 2016 / Published: 11 October 2016
(This article belongs to the Collection G Protein-Coupled Receptor Signaling and Regulation)
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Abstract

The mammalian target of rapamycin complex 1 (mTORC1) integrates amino acid (AA) availability to support protein synthesis and cell growth. Taste receptor type 1 member (T1R) is a G protein-coupled receptor that functions as a direct sensor of extracellular AA availability to regulate mTORC1 through Ca2+ stimulation and extracellular signal–regulated kinases 1 and 2 (ERK1/2) activation. However, the roles of specific AAs in T1R1/T1R3-regulated mTORC1 are poorly defined. In this study, T1R1 and T1R3 subunits were expressed in C2C12 myotubes, and l-AA sensing was accomplished by T1R1/T1R3 to activate mTORC1. In response to l-AAs, such as serine (Ser), arginine (Arg), threonine (Thr), alanine (Ala), methionine (Met), glutamine (Gln), and glycine (Gly), Met induced mTORC1 activation and promoted protein synthesis. Met also regulated mTORC1 via T1R1/T1R3-PLCβ-Ca2+-ERK1/2 signal transduction. Results revealed a new role for Met-regulated mTORC1 via an AA receptor. Further studies should be performed to determine the role of T1R1/T1R3 in mediating extracellular AA to regulate mTOR signaling and to reveal its mechanism. View Full-Text
Keywords: T1R1/T1R3; mTORC1; Ca2+; methionine T1R1/T1R3; mTORC1; Ca2+; methionine
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Zhou, Y.; Ren, J.; Song, T.; Peng, J.; Wei, H. Methionine Regulates mTORC1 via the T1R1/T1R3-PLCβ-Ca2+-ERK1/2 Signal Transduction Process in C2C12 Cells. Int. J. Mol. Sci. 2016, 17, 1684.

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