CLC number: Q291
On-line Access: 2024-08-27
Received: 2023-10-17
Revision Accepted: 2024-05-08
Crosschecked: 2019-07-09
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Xiu-Zhi Li, Xiang-Hua Yan. Sensors for the mTORC1 pathway regulated by amino acids[J]. Journal of Zhejiang University Science B, 2019, 20(9): 699-712.
@article{title="Sensors for the mTORC1 pathway regulated by amino acids",
author="Xiu-Zhi Li, Xiang-Hua Yan",
journal="Journal of Zhejiang University Science B",
volume="20",
number="9",
pages="699-712",
year="2019",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1900181"
}
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%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1900181
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A1 - Xiang-Hua Yan
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%@ 1673-1581
Y1 - 2019
PB - Zhejiang University Press & Springer
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DOI - 10.1631/jzus.B1900181
Abstract: The mechanistic target of rapamycin complex 1 (mTORC1) controls cell growth and metabolism in response to various environmental inputs, especially amino acids. In fact, the activity of mTORC1 is highly sensitive to changes in amino acid levels. Over past decades, a variety of proteins have been identified as participating in the mTORC1 pathway regulated by amino acids. Classically, the Rag guanosine triphosphatases (GTPases), which reside on the lysosome, transmit amino acid availability to the mTORC1 pathway and recruit mTORC1 to the lysosome upon amino acid sufficiency. Recently, several sensors of leucine, arginine, and S-adenosylmethionine for the amino acid-stimulated mTORC1 pathway have been coming to light. Characterization of these sensors is requisite for understanding how cells adjust amino acid sensing pathways to their different needs. In this review, we summarize recent advances in amino acid sensing mechanisms that regulate mTORC1 activity and highlight these identified sensors that accurately transmit specific amino acid signals to the mTORC1 pathway.
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