期刊
NATURE
卷 519, 期 7544, 页码 477-+出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nature14107
关键词
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资金
- Austrian Academy of Sciences
- ERC [i-FIVE 250179]
- EMBO [ALTF 1346-2011, IEF 301663, ALTF 314-2012]
- Swiss NSF [P300P3_147897]
- Vienna Science and Technology Fund [WWTF VRG10-001]
- Austrian Science Fund [FWF P 25522-B20, MCBO/SFB021]
- Italian Ministry of Instruction University and Research, PON-ricerca e competitivita [PON01_00937]
- Austrian Federal Ministry for Science and Research
- Austrian Science Fund (FWF) [P25522] Funding Source: Austrian Science Fund (FWF)
- Austrian Science Fund (FWF) [P 25522] Funding Source: researchfish
- Swiss National Science Foundation (SNF) [P300P3_147897] Funding Source: Swiss National Science Foundation (SNF)
Cell growth and proliferation are tightly linked to nutrient availability. The mechanistic target of rapamycin complex 1 (mTORC1) integrates the presence of growth factors, energy levels, glucose and amino acids to modulate metabolic status and cellular responses(1-3). mTORC1 is activated at the surface of lysosomes by the RAG GTPases and the Ragulator complex through a not fully understood mechanism monitoring amino acid availability in the lysosomal lumen and involving the vacuolar H1-ATPase(4-8). Here we describe the uncharacterized human member 9 of the solute carrier family 38 (SLC38A9) as a lysosomal membrane-resident protein competent in amino acid transport. Extensive functional proteomic analysis established SLC38A9 as an integral part of the Ragulator-RAG GTPases machinery. Gain of SLC38A9 function rendered cells resistant to amino acid withdrawal, whereas loss of SLC38A9 expression impaired amino-acid-induced mTORC1 activation. Thus SLC38A9 is a physical and functional component of the amino acid sensing machinery that controls the activation of mTOR.
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