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

Manuele Rebsamen, Lorena Pochini, Taras Stasyk, Mariana E. G. de Araújo, Michele Galluccio, Richard K. Kandasamy, Berend Snijder, Astrid Fauster, Elena L. Rudashevskaya, Manuela Bruckner, Stefania Scorzoni, Przemyslaw A. Filipek, Kilian V. M. Huber, Johannes W. Bigenzahn, Leonhard X. Heinz, Claudine Kraft, Keiryn L. Bennett, Cesare Indiveri, Lukas A. Huber and Giulio Superti-Furga ()
Additional contact information
Manuele Rebsamen: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Lorena Pochini: Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy
Taras Stasyk: Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria
Mariana E. G. de Araújo: Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria
Michele Galluccio: Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy
Richard K. Kandasamy: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Berend Snijder: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Astrid Fauster: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Elena L. Rudashevskaya: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Manuela Bruckner: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Stefania Scorzoni: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Przemyslaw A. Filipek: Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria
Kilian V. M. Huber: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Johannes W. Bigenzahn: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Leonhard X. Heinz: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Claudine Kraft: Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria
Keiryn L. Bennett: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria
Cesare Indiveri: Ecology and Earth Sciences), University of Calabria, 87036 Arcavacata di Rende, Italy
Lukas A. Huber: Biocenter, Innsbruck Medical University, 6020 Innsbruck, Austria
Giulio Superti-Furga: CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria

Nature, 2015, vol. 519, issue 7544, 477-481

Abstract: The mTORC1 protein kinase complex integrates nutrient and growth stimuli to modulate signalling pathways that regulate cellular metabolism and physiology, but the molecular nature of the amino acid sensing mechanism at the lysosome is unknown; here, an orphan member of the human solute carrier group of proteins, SLC38A9, is shown to be an integral component of the lysosomal machinery that can directly sense amino acids and activate mTORC1.

Date: 2015
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DOI: 10.1038/nature14107

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