Enzymes
UniProtKB help_outline | 1,149 proteins |
Reaction participants Show >> << Hide
- Name help_outline L-asparagine Identifier CHEBI:58048 Charge 0 Formula C4H8N2O3 InChIKeyhelp_outline DCXYFEDJOCDNAF-REOHCLBHSA-N SMILEShelp_outline NC(=O)C[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 27 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:73423 | RHEA:73424 | RHEA:73425 | RHEA:73426 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1.
Rebsamen M., Pochini L., Stasyk T., de Araujo M.E., Galluccio M., Kandasamy R.K., Snijder B., Fauster A., Rudashevskaya E.L., Bruckner M., Scorzoni S., Filipek P.A., Huber K.V., Bigenzahn J.W., Heinz L.X., Kraft C., Bennett K.L., Indiveri C., Huber L.A., Superti-Furga G.
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. mTORC1 is activated at the surfac ... >> More
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. 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 H(+)-ATPase. 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. << Less
Nature 519:477-481(2015) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.