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SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1.

Nature | Mar 26, 2015

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.

Pubmed ID: 25561175 RIS Download

Mesh terms: Amino Acid Transport Systems | Amino Acids | Animals | Cell Line | Humans | Lysosomes | Mice | Monomeric GTP-Binding Proteins | Multiprotein Complexes | Nucleotides | TOR Serine-Threonine Kinases

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Associated grants

  • Agency: Austrian Science Fund FWF, Id: FWF_P 26682

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Interaction database from an international collaboration between major public interaction data providers who have agreed to share curation effort and: * Develop and work to a single set of curation rules when capturing data from both directly deposited interaction data or from publications in peer-reviewed journals * Capture full details of an interaction in a ����??deep����?? curation model * Perform a complete curation of all protein-protein interactions experimentally demonstrated within a publication * Make these interaction available in a single search interface on a common website * Provide the data in standards compliant download formats * Make all IMEx records freely accessible under the Creative Commons Attribution License Data Availability IMEx partners all produce their own separate resources, which range from all encompassing molecular interaction databases, such as are maintained by IntAct, MINT and DIP, organism-centric resources such as BioGrid or MPIDB or biological domain centric, such as MatrixDB. However additionally to this, they have committed to making records available, via a dedicated PSICQUIC webservice, which have been curated to IMEx rules and are available to the user as a single, non-redundant set of curated publications which can be searched at the IMEx website. Data is made available in standards-compliant tab-deliminated and XML formats, enabling users to visualize the data in a wide range of tools such as Cytoscape and the R Bioconductor software. IMEx partners: * DIP (http://dip.doe-mbi.ucla.edu) (Active) * IntAct (www.ebi.ac.uk/intact) (Active) * MINT (http://mint.bio.uniroma2.it/mint) (Active) * MPact (http://mips.gsf.de/genre/proj/mpact) (Active) * MatrixDB (http://matrixdb.ibcp.fr/) (Active) * MPIDB (http://www.jcvi.org/mpidb) (Active) * Molecular Connections (http://www.molecularconnections.com) (Active) * BioGRID (http://www.thebiogrid.org/) (Observer) * InnateDB (www.innatedb.com) (Observer) * BIND (www.blueprint.org) (Inactive) The IMEx consortium is open to the participation of additional partners. The IMEx consortium actively encourages the deposition of data, prior to publication, and will supply unique accession numbers which may be referenced within the final article. Submitters may send their data directly to any of the member databases using a variety of formats, but should conform to the guidelines as to the minimum information required to describe the data.

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